@article{liu_lanier_osborne_2016, title={Capillarity proposed as the predominant mechanism of water and fat stabilization in cooked comminuted meat batters}, volume={111}, ISSN={["1873-4138"]}, DOI={10.1016/j.meatsci.2015.08.018}, abstractNote={Fat- and nonfat-containing meat gels structurally became coarser and porous by partial substitution of whey protein isolate for myofibrillar protein, creating a weaker texture plus greater cook loss (CL: fat + water) and expressible water (EW). Microstructure examinations revealed a tendency for fat to coalesce during cooking of the more coarse-structured gels. This tendency was unaffected by fat pre-emulsification prior to addition, arguing against a strong role of an interfacial protein film in stabilizing fat. Instead, a gel structure with evenly distributed small pores leads to lower CL and EW, thus controlling both water- and fat- holding since fat cannot readily permeate small water-filled hydrophilic pores. Only when large pores or continuous fissures are structurally present can water be released, allowing liquid fat to also migrate and coalesce. This changes the current paradigm of understanding regarding the mechanism of fat/water-holding in comminuted meat products: gel capillarity (gel structure), not fat emulsifying ability of protein, is the likely determining factor.}, journal={MEAT SCIENCE}, author={Liu, Wenjie and Lanier, Tyre C. and Osborne, Jason A.}, year={2016}, month={Jan}, pages={67–77} }
 @article{liu_lanier_2016, title={Rapid (microwave) heating rate effects on texture, fat/water holding, and microstructure of cooked comminuted meat batters}, volume={81}, ISSN={["1873-7145"]}, DOI={10.1016/j.foodres.2016.01.005}, abstractNote={Comminuted and gelled, fat-containing meat products such as frankfurters and luncheon meats are commercially processed by heating relatively slowly (for up to 2 h or more) to an endpoint of about 70 °C prior to cooling. This study compared such a slow, ramp heating regime (0.5 °C/min), terminated at 70 °C, to rapid, square-wave cooking (one step: rapid 100 °C/min heating to 70 °C endpoint, plus isothermal holding prior to cooling, or two-step: rapid heating to 50 °C, holding, then rapid heating to 70 °C plus holding prior to cooling) on meat batter gel properties (fracture and small strain rheology, microstructure, cook loss, and expressible water). The results indicated that a rapid cooking process, with its inherent advantages of reduced process time, lower equipment footprint, and more efficient use of energy, can produce a product nearly equivalent in textural properties and cook yield to one processed by traditional smokehouse cooking when the cook value of the processes is similar and an intermediate (near 50 °C) holding step is included (two-step rapid heating). One-step rapid heating negatively affected gel structural homogeneity and water/fat holding properties of fat-containing gels.}, journal={FOOD RESEARCH INTERNATIONAL}, author={Liu, Wenjie and Lanier, Tyre C.}, year={2016}, month={Mar}, pages={108–113} }
 @article{liu_lanier_2015, title={Combined use of variable pressure scanning electron microscopy and confocal laser scanning microscopy best reveal microstructure of comminuted meat gels}, volume={62}, ISSN={["1096-1127"]}, DOI={10.1016/j.lwt.2015.02.001}, abstractNote={Observing the distribution of protein and fat phases in comminuted meat products can be helpful to understanding the mechanisms of texture development and fat/water binding. In this study variable pressure scanning electron microscopy (VP-SEM) was compared to conventional scanning electron microscopy (SEM), and contrasted with confocal laser scanning microcopy (CLSM), as tools to characterize gel morphology of cooked meat batters or non-fat pastes. Gel morphology was varied by inclusion of whey protein isolate (WPI) that gels only at high temperature, in partial substitution of myofibrillar protein (MFP). CLSM (magnification:10–1000×) revealed that, when no WPI was added, a homogeneous gel structure was produced enmeshing small, well-distributed fat particles. Substituting 30 g/100 g MFP by WPI produced a coarse gel structure with clear microphase separation of fat. VP-SEM (magnification:1000–2000×) enabled visualization of small pore structure of gel matrix whereas SEM obscured details of this, as well as of the relationship between fat globules and gel matrix that were visible by VP-SEM. Since meat gels properties can be affected by multiple morphological features, visible only at different levels of magnification, the relationships between microstructure and important properties of meat gels can be most advantageously observed when both VP-SEM and CLSM are used in tandem.}, number={2}, journal={LWT-FOOD SCIENCE AND TECHNOLOGY}, author={Liu, Wenjie and Lanier, Tyre C.}, year={2015}, month={Jul}, pages={1027–1033} }
 @article{zhu_lanier_farkas_2015, title={High pressure effects on heat-induced gelation of threadfin bream (Nemipterus spp.) surimi}, volume={146}, ISSN={["1873-5770"]}, DOI={10.1016/j.jfoodeng.2014.08.021}, abstractNote={We sought to determine, in threadfin bream surimi system, if 40 °C incubation carried out simultaneous with, or following, HPP might also induce a more effective setting on subsequently cooked gels. Threadfin bream surimi pastes were subjected to HPP 200 or 300; at 5 °C (little or no setting effect expected during HPP at this temperature) for 15 min or at 40 °C (optimal setting temperature for threadfin bream pastes) for 15 or 30 min. Pastes were then directly cooked (90 °C for 20 min) (pressureP°C/time > C), or first allowed to undergo setting at atmospheric pressure (40 °C for 60 min), followed by cooking (90 °C 20 min) (pressureP°C/time > Stime > C). With or without followed setting treatment at 40 °C, HPP treatment at 40 °C, or even lower pressure at 5 °C for shorter time (200MPaP5°C/15min > S40°C/60min > C) produce weak cooking gels. Two opposite actions of cross-linked polymer (CP) and degraded protein (DP) was observed during the HPP treatment. The given HPP treatment was sure to triggered the detriment of protein in combined treatments, the followed setting treatment after HPP enhanced the degradation of protein as well. The formation of disulfide bonds during HPP and cooking treatments was retarded, which was attributed to the influence of protein degradation behavior. Scanning electron microscopy revealed, with giving a prior HPP treatment, the fiberlike structure gradually disappeared and the compact microstructure increased in final cooking gel.}, journal={JOURNAL OF FOOD ENGINEERING}, author={Zhu, Zhiwei and Lanier, Tyre C. and Farkas, Brian E.}, year={2015}, month={Feb}, pages={23–27} }
 @article{suriaatmaja⁎_lanier_2014, title={Mechanism of meat tenderization by sous vide cooking}, volume={96}, ISSN={0309-1740}, url={http://dx.doi.org/10.1016/J.MEATSCI.2013.07.073}, DOI={10.1016/J.MEATSCI.2013.07.073}, abstractNote={Consumers are the final step in the meat supply chain and meeting consumer expectations of quality and tenderness are important for satisfaction and repeat purchase. High pressure processing, shockwaves, ultrasound, pulsed electric field and muscle stretching can be applied to pre- and post-rigor meat for tenderisation. These non-thermal and thermal innovative technologies can be used with varying levels of success to cause physical disruption to muscle structure, enhanced proteolysis and ageing and muscle protein denaturation and solubilisation resulting in changes to texture and juiciness. Results of a meta-analysis are used to compare the effects of these technologies on meat tenderisation. In the future, a combination of new and innovative technologies will be ideally suited to deliver a range of desired textures for meat products.}, number={1}, journal={Meat Science}, publisher={Elsevier BV}, author={Suriaatmaja⁎, D. and Lanier, T.}, year={2014}, month={Jan}, pages={457} }
 @article{zhu_lanier_farkas_li_2014, title={Transglutaminase and high pressure effects on heat-induced gelation of Alaska pollock (Theragra chalcogramma) surimi}, volume={131}, ISSN={["1873-5770"]}, DOI={10.1016/j.jfoodeng.2014.01.022}, abstractNote={Abstract A prior high pressure processing (HPP) treatment has previously been shown to enhance subsequent (at atmospheric pressure) low temperature ‘setting’ (glutamyl-lysine, non-disulfide protein crosslinking) induced by transglutaminase (TGase; endogenous or added microbial enzyme). This enhanced setting induces greater gel strength and deformability of subsequently cooked surimi gels. We sought to determine if 25 °C incubation carried out simultaneous with, rather than following, HPP might similarly induce a setting effect on subsequently cooked gels. Pollock surimi pastes (± added microbial TGase) were subjected to HPP 200, 300, or 400 MPa; at 5 °C (little or no setting effect expected during HPP at this temperature) for 30 min or at 25 °C (optimal setting temperature for pollock pastes) for 30, 60, or 120 min. Pastes were then directly cooked (90 °C for 20 min) ( pressure P °C/time  > C), or first allowed to undergo setting at atmospheric pressure (25 °C for 30, 60, or 120 min), followed by cooking (90 °C 20 min) ( pressure P °C/time  > S time  > C). With no microbial TGase added to the raw paste (e.g., endogenous TGase only), 300MPa P 5°C/30min  > S 25°C/120min  > C induced highest gel fracture stress and strain. The same treatment but with HPP at 200 or 400 MPa gave only slightly lower fracture stress (gel strength). Increasing the temperature of the HPP treatment to 25 °C ( 300MPa P 25°C/30min  > S 25°C/120min  > C), even with longer HPP time ( 300MPa P 25°C/60 or 120min  > C), gave weaker gels, similar to those obtained by setting and cooking without a prior HPP treatment (S 25°C/60min  > C). Thus, attempting to induce TGase crosslinking by setting at 25 °C during HPP treatment actually seemed detrimental to gel strength development. However, when HPP was carried out at 25 °C and microbial TGase was added, gel strength and deformability (fracture stress, strain) were enhanced above that of all other treatments tested. All treatments containing microbial TGase evidenced enhanced protein polymerization. Scanning electron microscopy revealed a more dense and fibrous structure in such gels, and reduction of free thiol (SH) groups was noted as a result of microbial TGase addition.}, journal={JOURNAL OF FOOD ENGINEERING}, author={Zhu, Zhiwei and Lanier, Tyre C. and Farkas, Brian E. and Li, BianSheng}, year={2014}, month={Jun}, pages={154–160} }
 @article{stevenson_dykstra_lanier_2013, title={Capillary Pressure as Related to Water Holding in Polyacrylamide and Chicken Protein Gels}, volume={78}, ISSN={["1750-3841"]}, DOI={10.1111/1750-3841.12036}, abstractNote={Abstract}, number={2}, journal={JOURNAL OF FOOD SCIENCE}, author={Stevenson, Clinton D. and Dykstra, Michael J. and Lanier, Tyre C.}, year={2013}, month={Feb}, pages={C145–C151} }
 @article{liu_stevenson_lanier_2013, title={Rapid Heating of Alaska Pollock and Chicken Breast Myofibrillar Proteins as Affecting Gel Rheological Properties}, volume={78}, ISSN={["0022-1147"]}, DOI={10.1111/1750-3841.12147}, abstractNote={Abstract}, number={7}, journal={JOURNAL OF FOOD SCIENCE}, author={Liu, Wenjie and Stevenson, Clint D. and Lanier, Tyre C.}, year={2013}, month={Jul}, pages={C971–C977} }
 @article{stagg_amato_giesbrecht_lanier_2012, title={Autolytic Degradation of Skipjack Tuna during Heating As Affected by Initial Quality and Processing Conditions}, volume={77}, ISSN={["1750-3841"]}, DOI={10.1111/j.1750-3841.2011.02543.x}, abstractNote={Abstract:  Several factors were studied as affecting protein degradation and texture of skipjack tuna muscle following ambient pressure thermal processing (precooking). These included degree of mushy tuna syndrome (MTS) evidenced in the raw meat, raw meat pH, abusive thawing/holding, and precooking temperature/time. Slurries and intact pieces from frozen skipjack tuna, either tempered for 2 h or thawed and held at 25 °C for 22 h (abusive treatment) were heated at temperatures ranging from 40 to 80 °C for up to 2 h, and also at 90 °C for 1 h, with or without prior adjustment of pH to 5 or 7 to favor cathepsin or calpain activity, respectively. Proteolysis of precooked samples was monitored by Lowry assay and SDS–PAGE; cooked texture of intact meat was measured using a Kramer shear press and by sensory profile analysis. Proteolysis maximally occurred in slurries of skipjack tuna muscle that had been abusively stored (22 h at 25 °C) and adjusted to pH 5 prior to heating at 55 °C. Intact pieces of tuna abusively thawed/held for 22 h with subsequent heating at 55 °C also evidenced the most proteolysis and were the least firm in texture. Raw fish that evidenced higher severity of MTS when raw displayed higher levels of proteolysis prior to cooking, which were further increased after cooking at 55 °C.}, number={2}, journal={JOURNAL OF FOOD SCIENCE}, author={Stagg, Nicola J. and Amato, Penny M. and Giesbrecht, Francis and Lanier, Tyre C.}, year={2012}, month={Feb}, pages={C149–C155} }
 @article{leksrisompong_lanier_foegeding_2012, title={Effects of Heating Rate and pH on Fracture and Water-Holding Properties of Globular Protein Gels as Explained by Micro-Phase Separation}, volume={77}, ISSN={["1750-3841"]}, DOI={10.1111/j.1750-3841.2011.02550.x}, abstractNote={Abstract:  The effect of heating rate and pH on fracture properties and held water (HW) of globular protein gels was investigated. The study was divided into 2 experiments. In the 1st experiment, whey protein isolate (WPI) and egg white protein (EWP) gels were formed at pH 4.5 and 7.0 using heating rates ranging from 0.1 to 35 °C/min and holding times at 80 °C up to 240 min. The 2nd experiment used one heating condition (80 °C for 60 min) and probed in detail the pH range of 4.5 to 7.0 for EWP gels. Fracture properties of gels were measured by torsional deformation and HW was measured as the amount of fluid retained after a mild centrifugation. Single or micro‐phase separated conditions were determined by confocal laser scanning microscopy. The effect of heating rate on fracture properties and HW of globular protein gels can be explained by phase stability of the protein dispersion and total thermal input. Minimal difference in fracture properties and HW of EWP gels at pH 4.5 compared with pH 7.0 were observed while WPI gels were stronger and had higher HW at pH 7.0 as compared to 4.5. This was due to a mild degree of micro‐phase separation of EWP gels across the pH range whereas WPI gels only showed an extreme micro‐phase separation in a narrow pH range. In summary, gel formation and physical properties of globular protein gels can be explained by micro‐phase separation.}, number={2}, journal={JOURNAL OF FOOD SCIENCE}, author={Leksrisompong, Phanin N. and Lanier, Tyre C. and Foegeding, E. Allen}, year={2012}, month={Feb}, pages={E60–E67} }
 @article{stevenson_liu_lanier_2012, title={Rapid Heating of Alaska Pollock and Chicken Breast Myofibrillar Protein Gels as Affecting Water-Holding Properties}, volume={60}, ISSN={["1520-5118"]}, DOI={10.1021/jf3032292}, abstractNote={The gelation response of salted muscle minces to rapid versus slow heating rates is thought to differ between homeotherm and poikilotherm species. This study investigated water-holding (WH) properties of pastes prepared from refined myofibrils, at equal pH, of chicken breast versus Alaska pollock both during [cook loss (CL)] and following [expressible water (EW)] their cooking by rapid [microwave (MW)] versus slow [water bath (WB)] heating and whether such properties were related to gel matrix structure parameters and water mobility. Results did not confirm the industrial experience that pastes of meat from homeotherms benefit from slower cooking. Gels of equally high WH ability (low CL or EW) were made by rapid heating when the holding time did not exceed 5 min prior to cooling, which was sufficient for completion of gelation. Reduced CL and EW correlated with larger and smaller amplitudes of T21 and T22 water pools, respectively, measured by time-domain nuclear magnetic resonance (TD-NMR).}, number={40}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={Stevenson, Clinton D. and Liu, Wenjie and Lanier, Tyre C.}, year={2012}, month={Oct}, pages={10111–10117} }
 @article{lombardand_lanier_2011, title={Marinade Composition and Vacuum Effects on Liquid Uptake and Retention in Tumbled Fish Portions}, volume={20}, ISSN={["1547-0636"]}, DOI={10.1080/10498850.2010.549605}, abstractNote={A combination of higher pH (pH 8 vs. pH 6 or 7), higher NaCl content (6% vs. 2%), and shorter chain polyphosphates (sodium tripoly- or pyro-phosphate vs. hexametaphosphate, all at 1.6% in the marinade) during tumbling of halibut pieces (uniform size, shape) resulted in greatest marinade uptake and yields following subsequent purge and cook losses. Surface slime formation noted in optimum treatments, likely the result of increased surface extraction of protein, could dictate moderating ionic strength and solution pH as a marketing consideration. Unfrozen (fresh) fish exhibited a greater uptake of marinade than previously frozen fish, but also higher subsequent purge and cook losses such that yields after cooking for the two treatments were similar. Contrary to conventional industry belief, vacuum (9.2 kPa) during tumbling did not affect uptake of marinade.}, number={2}, journal={JOURNAL OF AQUATIC FOOD PRODUCT TECHNOLOGY}, author={Lombardand, R. and Lanier, T.}, year={2011}, pages={117–128} }
 @article{carvajal-rondanelli_lanier_2010, title={Diffusion of Active Proteins into Fish Meat To Minimize Proteolytic Degradation}, volume={58}, ISSN={["1520-5118"]}, DOI={10.1021/jf903580t}, abstractNote={Proteases in fish muscle often cause undesired softening of intact meat pieces during refrigerated storage or slow cooking. Several food-grade proteinaceous inhibitors can overcome this softening if properly delivered to the intracellular sites where proteases are located. Fluorescence recovery after photobleaching (FRAP) and laser scanning confocal microscopy (LSCM) were used to measure the translational diffusion of fluorescein isothiocyanate (FITC)-labeled protease inhibitors into intact muscle fibers of halibut. Diffusion coefficients (D) of alpha-2-macroglobulin (720 kDa), soybean trypsin inhibitor (21 kDa), and cystatin (12 kDa) were measured in both muscle fibers and dilute aqueous solutions. On the time scale of the observation (35 min), cystatin and soybean trypsin inhibitor diffused through the cell membrane (sarcolemma) and sarcoplasm, but at a considerably slower rate (>10-fold difference) than in dilute aqueous solution. alpha-2-Macroglobulin did not diffuse into muscle cells within the time frame of the experiment, but did completely penetrate the cell during overnight exposure. The present study thus shows a clear dependence of D on protein inhibitor size when moving within intact skeletal muscle fibers. Low molecular weight protease inhibitors such as cystatin can be effectively diffused into intact fish muscle cells to minimize proteolytic activity and meat softening.}, number={9}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={Carvajal-Rondanelli, Patricio A. and Lanier, Tyre C.}, year={2010}, month={May}, pages={5300–5307} }
 @article{rawdkuen_benjakul_visessanguan_lanier_2008, title={Rheological and Textural Properties of Pacific Whiting Surimi Gels As Influenced by Chicken Plasma}, volume={11}, ISSN={["1532-2386"]}, DOI={10.1080/10942910701624744}, abstractNote={Rheological properties of Pacific whiting surimi, in the absence and presence of chicken plasma (CP) at different levels (0.3–3.0%, w/w), were studied by dynamic rheological (small strain) and torsion fracture measurements, respectively. The surimi paste exhibited two major distinctive rheological transitions during heating (1°C/min) from 20 to 90°C with peaks observed at 33 and 56°C. The abrupt loss of G′ upon heating from 47 to 57°C, and the occurrence of small peak of phase angle at the same temperature range were prevented by the addition of CP. Nevertheless, the final G′ of the surimi paste added with CP was lower than that of the control. But shear fracture stress of both kamaboko and modori gels increased as the CP levels increased and shear strain increased with the addition of CP up to 2% (P < 0.05). CP inhibited the degradation of myosin heavy chains (MHC) caused by endogenous proteinases as indicated by more retained MHC and lowered TCA-soluble peptide content. Whiteness of gels decreased somewhat with increasing CP levels. CP, thus, could be a helpful additive for improving gelling properties of Pacific whiting surimi}, number={4}, journal={INTERNATIONAL JOURNAL OF FOOD PROPERTIES}, author={Rawdkuen, Saroat and Benjakul, Soottawat and Visessanguan, Wonnop and Lanier, Tyre C.}, year={2008}, pages={820–832} }
 @article{fort_lanier_amato_carretero_saguer_2008, title={Simultaneous application of microbial transglutaminase and high hydrostatic pressure to improve heat induced gelation of pork plasma}, volume={80}, ISSN={["0309-1740"]}, DOI={10.1016/j.meatsci.2008.02.009}, abstractNote={The effects of treating porcine plasma with microbial tranglutaminase (MTGase) under high hydrostatic pressure (HHP) were studied as a means of improving its gel-forming properties when subsequently heated at pH 5.5, near the pH of meats. Plasma containing varying levels of commercial MTGase was pressurized (400 MPa, room temperature, pH 7) for different times, and adjusted to pH 5.5 prior to heating to induce gelation. MTGase-treatment under HHP led to greater enhancement of heat-induced plasma gel properties as compared to control samples. The greatest improvements were achieved by pressurising plasma with 43.3 U MTGase/g protein for 30 min, thereby achieving recoveries of 49% and 63% in fracture force (gel strength) and fracture distance (gel deformability) of the subsequently heat-induced gels, respectively, relative to gel properties obtained by heating untreated plasma at physiological conditions (pH 7.5).}, number={3}, journal={MEAT SCIENCE}, author={Fort, N. and Lanier, T. C. and Amato, P. M. and Carretero, C. and Saguer, E.}, year={2008}, month={Nov}, pages={939–943} }
 @article{perez-mateos_lanier_2007, title={Comparison of Atlantic menhaden gels from surimi processed by acid or alkaline solubilization}, volume={101}, ISSN={["1873-7072"]}, DOI={10.1016/j.foodchem.2006.03.026}, abstractNote={Heat-induced gelling abilities of surimis prepared by pH shifting (isoelectric precipitation following acid (AC) or alkaline (AL) solubilization) were compared to that of conventionally washed (CW) surimi. Greater endogenous transglutaminase activity (evidenced as enhanced strength of cooked gels subjected to 30–40 °C preincubation) was measured for CW and AL surimi than for AC surimi (all at pH 7). Upon addition of microbial transglutaminase (MTGase), increased crosslinking of myosin heavy chain and gel strengthening during 30–40 °C preincubation were apparent for all three types of surimi, most markedly in CW and AL surimi. Salt addition improved CW gels most, but seemed to adversely affect MTGase activity in AC and AL surimi. AC and AL surimi gels were of lower whiteness than were CW surimi gels.}, number={3}, journal={FOOD CHEMISTRY}, author={Perez-Mateos, M. and Lanier, T. C.}, year={2007}, pages={1223–1229} }
 @article{rawdkuen_benjakul_visessanguan_lanier_2007, title={Cysteine proteinase inhibitor from chicken plasma: Fractionation, characterization and autolysis inhibition of fish myofibrillar proteins}, volume={101}, ISSN={["1873-7072"]}, DOI={10.1016/j.foodchem.2006.04.035}, abstractNote={Cysteine proteinase inhibitor (CPI) from chicken plasma was fractionated by using polyethylene glycol (PEG-4000) or ammonium sulfate (AS). Addition of PEG, at the level of 200–400 g/l based on the original volume of plasma protein, was more effective to fractionate CPI than was using AS. Highest inhibitory activity and purification-fold were obtained in the PEG precipitate II (CPI fraction). The CPI fraction was stable in the temperature ranges of 40–90 °C for 10 min but extended incubation time at 90 °C markedly decreased the inhibitory activity of the CPI fraction. The fraction was stable in the broad pH ranges tested (3–10). NaCl concentrations of 0.5–3% did not affect the inhibitory activity of the CPI fraction. The CPI fraction effectively prevented the degradation of mince and washed mince from Pacific whiting; however, lower efficacy in inhibiting autolysis of the arrowtooth flounder mince and the washed mince was observed, suggesting differences in initial proteolytic activity between the two species. Therefore, the CPI fraction from chicken plasma could be an alternative food grade inhibitor for the surimi industry.}, number={4}, journal={FOOD CHEMISTRY}, author={Rawdkuen, Saroat and Benjakul, Soottawat and Visessanguan, Wonnop and Lanier, Tyre C.}, year={2007}, pages={1647–1657} }
 @article{rawdkuen_benjakul_visessanguan_lanier_2007, title={Effect of chicken plasma protein and some protein additives on proteolysis and gel-forming ability of sardine (Sardinella gibbosa) surimi}, volume={31}, ISSN={["1745-4549"]}, DOI={10.1111/j.1745-4549.2007.00132.x}, abstractNote={The effect of chicken plasma protein (CPP) and various protein additives on autolysis and gel-forming ability of sardine (Sardinella gibbosa) surimi was investigated. CPP and other protein additives showed inhibitory activity toward autolysis of sardine surimi incubated at 70C in a concentration- dependent manner. Porcine plasma protein (PPP) and egg white (EW) were more effective in proteolysis prevention than CPP and other protein additives. Breaking force and deformation of both modori and kamaboko gels increased when CPP and other protein additives were added at levels up to 2% (P 0.05). Proteolysis of sardine surimi can be retarded by the addition of CPP and protein additives, leading to increased gel-forming ability.}, number={4}, journal={JOURNAL OF FOOD PROCESSING AND PRESERVATION}, author={Rawdkuen, Saroat and Benjakul, Soottawat and Visessanguan, Wonnop and Lanier, Tyre C.}, year={2007}, month={Aug}, pages={492–516} }
 @article{rawdkuen_benjakul_visessanguan_lanier_2007, title={Effect of cysteine proteinase inhibitor containing fraction from chicken plasma on autolysis and gelation of Pacific whiting surimi}, volume={21}, ISSN={["0268-005X"]}, DOI={10.1016/j.foodhyd.2006.10.002}, abstractNote={The effects of cysteine proteinase inhibitor containing fraction (CPI fraction) from chicken plasma on autolysis inhibition and gelling properties of Pacific whiting surimi were investigated. The CPI fraction exhibited the inhibitory activity against autolysis of Pacific whiting surimi in a concentration-dependent manner. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis pattern revealed that the CPI fraction effectively prevented the degradation of myosin heavy chain, tropomyosin and troponin-T in Pacific whiting surimi incubated at 55 °C for 60 min as well as modori gel (55 °C for 30 min/90 °C for 20 min). The breaking force and deformation of modori gels increased as the concentration of CPI fraction increased up to 2.0% with a concomitant decrease in TCA-soluble peptides (p<0.05). However, a decrease in breaking force and deformation was noticeable with the modori gel added with 3% CPI fraction. The addition of CPI fraction had no detrimental effect on whiteness of surimi gels (p>0.05). The result suggested that CPI fraction would be an alternative additive for surimi containing the active cysteine proteinase causing the gel weakening.}, number={7}, journal={FOOD HYDROCOLLOIDS}, author={Rawdkuen, Saroat and Benjakul, Soottawat and Visessanguan, Wonnop and Lanier, Tyre C.}, year={2007}, month={Oct}, pages={1209–1216} }
 @misc{lanier_simunovic_swartzel_drozd_riemann_2007, title={Thermal gelation of foods and biomaterials using rapid heating}, volume={7,270,842}, number={2007 Sept. 18}, publisher={Washington, DC: U.S. Patent and Trademark Office}, author={Lanier, T. and Simunovic, J. and Swartzel, K. R. and Drozd, J. M. and Riemann, A.}, year={2007} }
 @article{perez-mateos_lanier_boyd_2006, title={Effects of rosemary and green tea extracts on frozen surimi gels fortified with omega-3 fatty acids}, volume={86}, ISSN={["1097-0010"]}, DOI={10.1002/jsfa.2388}, abstractNote={Abstract}, number={4}, journal={JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE}, author={Perez-Mateos, M and Lanier, TC and Boyd, LC}, year={2006}, month={Mar}, pages={558–567} }
 @article{rawdkuen_benjakul_visessanguan_lanier_2006, title={Partial purification and characterization of cysteine proteinase inhibitor from chicken plasma}, volume={144}, ISSN={1096-4959}, url={http://dx.doi.org/10.1016/j.cbpb.2006.05.008}, DOI={10.1016/j.cbpb.2006.05.008}, abstractNote={A high-molecular-weight cysteine proteinase inhibitor (CPI) was purified from chicken (Gallus gallus) plasma using polyethylene glycol (PEG) fractionation and affinity chromatography on carboxymethyl–papain–Sepharose-4B. The CPI was purified 96.8-fold with a yield of 28.9%. Based on inhibitory activity staining for papain, CPI was shown to have an apparent molecular mass of 122 kDa. No inhibitory activity was obtained under reducing condition, indicating that CPI from chicken plasma was stabilized by disulfide bonds. CPI was stable in temperature ranges from 40 to 70 °C for 10 min; however, more than 50% of the inhibitory activity towards papain was lost within 30 min of heating at 90 °C. CPI was stable in the presence of salt up to 3%. The purified CPI exhibited the inhibitory activity toward autolysis of arrowtooth flounder (Atheresthes stomias) and Pacific whiting (Merluccius productus) natural actomyosin (NAM) in a concentration-dependent manner.}, number={4}, journal={Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology}, publisher={Elsevier BV}, author={Rawdkuen, Saroat and Benjakul, Soottawat and Visessanguan, Wonnop and Lanier, Tyre C.}, year={2006}, month={Aug}, pages={544–552} }
 @article{rawdkuen_benjakul_visessanguan_lanier_2005, title={Combination effects of chicken plasma protein and setting phenomenon on gel properties and cross-linking of bigeye snapper muscle proteins}, volume={38}, ISSN={["1096-1127"]}, DOI={10.1016/j.lwt.2004.06.016}, abstractNote={Effects of chicken plasma protein (CPP) in combination with setting on surimi gel properties and protein cross-linking were investigated. Addition of CPP (0.5 g/100 g), CaCl2 (10 mmole/kg) and 200 units of thrombin/g CPP in combination with setting at 40 °C for 30 min prior to heating at 90 °C for 20 min resulted in the highest breaking force and deformation (P<0.05). Regardless of CPP addition, myosin heavy chain (MHC) in surimi proteins and natural actomyosin (NAM) underwent polymerization to some extent in the presence of CaCl2 and thrombin. The cross-linking of MHC in surimi proteins were markedly suppressed by the addition of EGTA and NH4Cl, transglutaminase (TGase) inhibitors. No cross-linking of myosin was observed when CPP, CaCl2 and thrombin were added, even with the prolonged incubation time. The result revealed that CPP showed no cross-linking activity and gel strengthening effect of CPP was attributed to its filler effect and proteolytic inhibitory activity.}, number={4}, journal={LWT-FOOD SCIENCE AND TECHNOLOGY}, author={Rawdkuen, S and Benjakul, S and Visessanguan, W and Lanier, TC}, year={2005}, pages={353–362} }
 @article{rawdkuen_benjakul_visessanguan_lanier_2005, title={Fractionation and characterization of cysteine proteinase inhibitor from chicken plasma}, volume={29}, ISSN={["1745-4514"]}, DOI={10.1111/j.1745-4514.2005.00027.x}, abstractNote={The fractionation of cysteine proteinase inhibitor (CPI) from chicken blood plasma was carried out using polyethylene glycol-4000 or ammonium sulfate (AS) precipitation. The addition of PEG at the level of 400 g/L, on the basis of the original volume of plasma protein, was more effective to fraction- ate CPI than using AS. CPI in the PEG fraction had a molecular weight of about 46 kDa with intramolecular disulfide bond. CPI containing fraction was colorless and had no absorbance in the range of 700-360 nm. The fraction was stable in the temperature range of 40-90C for 10 min and still retained high inhibitory activity toward papain after incubation at 90C for 60 min. NaCl, at 0-3.0% concentration, did not affect the inhibitory activity of the CPI containing fraction. The fraction was stable at pH 8.0, and the minimal inhibi- tory activity against papain was found at pH 5-6. Therefore, PEG fraction- ation effectively isolated the CPI from chicken plasma.}, number={5}, journal={JOURNAL OF FOOD BIOCHEMISTRY}, author={Rawdkuen, S and Benjakul, S and Visessanguan, W and Lanier, TC}, year={2005}, month={Oct}, pages={486–503} }
 @article{kang_lanier_2005, title={Inhibition of protease in intact fish fillets by soaking in or injection of recombinant soy cystatin or bovine plasma}, volume={53}, ISSN={["0021-8561"]}, DOI={10.1021/jf051231y}, abstractNote={Arrowtooth flounder (AF) fillets are known to contain a heat-activated cysteine protease similar to that found in Pacific whiting, which results in soft texture upon cooking. A crude recombinant soy cystatin (CRSC) produced by Escherichia coli, which has been shown to inhibit the protease(s) in Pacific whiting, was introduced into AF fillets by immersion or injection at one of three levels of inhibitory activity: 10 times less than, equal to, or 10 times greater than that of a 20% bovine plasma protein (BPP) solution, a known inhibitor of AF protease(s). Fillets treated with CRSC or BPP at equal inhibitory strength subsequently exhibited the same degree of protection against textural degradation during cooking. Fillets treated with CRSC at lesser or greater levels of inhibitory activity than those of BPP exhibited lesser or higher protection, accordingly. As revealed by SDS-PAGE, the outer portion of fillets soaked with inhibitory solutions was more effectively protected than the inner portion. Such differences between the outer and inner portions of the fillets were not evident when inhibitory solutions were injected into the fillets.}, number={25}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={Kang, I and Lanier, TC}, year={2005}, month={Dec}, pages={9795–9799} }
 @article{rawdkuen_benjakul_visessanguan_lanier_2004, title={Chicken plasma protein affects gelation of surimi from bigeye snapper (Priacanthus tayenus)}, volume={18}, ISSN={["1873-7137"]}, DOI={10.1016/S0268-005X(03)00082-1}, abstractNote={Effect of chicken plasma protein (CPP) at different concentrations on gel properties of grade SA and A bigeye snapper surimi was investigated. Addition of 0.5% CPP in combination with setting at 40 °C for 30 min prior to heating at 90 °C for 20 min resulted in the highest breaking force and deformation (P<0.05). However, whiteness decreased to some extent. CPP was able to prevent the degradation of surimi proteins as indicated by the decrease in TCA-soluble peptides (P<0.05). Electrophoretic studies revealed that myosin heavy chain underwent polymerization to a lower extent as CPP concentration increased. Therefore, CPP worked as protease inhibitor rather than protein cross-linker. Microstructure of kamaboko gels, added with 0.5% CPP, had less linkage between protein strands with a coarser fibrillar structure, indicating the interfering effect of CPP on cross-linking of myofibrillar proteins. Thus, at an appropriate amount, CPP possibly worked as a filler in the surimi gel matrix, resulting in gel strengthening.}, number={2}, journal={FOOD HYDROCOLLOIDS}, author={Rawdkuen, S and Benjakul, S and Visessanguan, W and Lanier, TC}, year={2004}, month={Mar}, pages={259–270} }
 @article{rawdkuen_benjakul_visessanguan_lanier_2004, title={Chicken plasma protein: Proteinase inhibitory activity and its effect on surimi gel properties}, volume={37}, ISSN={["1873-7145"]}, DOI={10.1016/j.foodres.2003.09.014}, abstractNote={The inhibitory activity of chicken plasma protein (CPP) at different concentrations on sarcoplasmic proteinases and autolysis of mince and washed mince of bigeye snapper and lizardfish was investigated. CPP (0–2% w/w) exhibited inhibitory activity toward sarcoplasmic proteinases and autolysis, especially when CPP concentration increased. Electrophoretic study revealed that CPP effectively prevented the degradation of myosin heavy chain (MHC) in mince and washed mince incubated at elevated temperature. The breaking force and deformation of modori gels from surimi of both fish species increased as CPP addition increased (P<0.05) with a concomitant decrease in TCA-soluble peptides. MHC was retained more in the presence of CPP, especially when the CPP concentration increased. However, whiteness decreased with increasing CPP concentrations. Microstructure of modori gels with 2% (w/w) CPP added had an ordered fibrillar structure, indicating a preventive effect on hydrolysis of myofibrillar protein. This was accompanied by an increase in surimi gel strength.}, number={2}, journal={FOOD RESEARCH INTERNATIONAL}, author={Rawdkuen, S and Benjakul, S and Visessanguan, W and Lanier, TC}, year={2004}, pages={156–165} }
 @article{kang_wang_shih_lanier_2004, title={Extracellular production of a functional soy cystatin by Bacillus subtilis}, volume={52}, ISSN={["1520-5118"]}, DOI={10.1021/jf049711x}, abstractNote={A recombinant Bacillus subtilis producing soy cystatin was developed by subcloning with a soy cystatin gene cloned in Escherichia coli. An active form of cystatin against the cysteine protease from Pacific whiting fillets contaminated with Myxosporidia parasite was constitutively expressed and secreted extracelluarly into the medium. Two gene fragments of signal peptides from kerA and sacB were introduced and compared for secretion efficiency of cystatin. The secretion level of active cystatin improved with the signal peptide of kerA when compared to that of sacB. Inhibitor activity was reduced rapidly after peak expression of the target protein at 36 h of fermentation. The addition of 1% glucose, a suppressor of protease, into the medium sustained the increase of the cystatin activity during fermentation. This study introduced a potential new method for fermentation production of cystatin.}, number={16}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={Kang, IS and Wang, JJ and Shih, JCH and Lanier, TC}, year={2004}, month={Aug}, pages={5052–5056} }
 @article{perez-mateos_amato_lanier_2004, title={Gelling properties of Atlantic croaker surimi processed by acid or alkaline solubilization}, volume={69}, ISSN={["1750-3841"]}, DOI={10.1111/j.1365-2621.2004.tb06335.x}, abstractNote={Paper No. FSR-03-40 of the Journal Series of the Department of Food Science, North Carolina State University, Raleigh, NC 27695-7624.}, number={4}, journal={JOURNAL OF FOOD SCIENCE}, author={Perez-Mateos, M and Amato, PM and Lanier, TC}, year={2004}, month={May}, pages={C328–C333} }
 @article{goeller_amato_farkas_green_lanier_kong_2004, title={Optimization of incorporation of low-molecular-weight cryoprotectants into intact fish muscle}, volume={69}, ISSN={["1750-3841"]}, DOI={10.1111/j.1365-2621.2004.tb06342.x}, abstractNote={Chanks of freshwater tront muscle were immersed in sorbitol solutions (0% to 60%), under different vacuum conditions, for up to 30 min at 5 °C, Molsture loss, weight change, and sorbitol uptable were measured or calculated by mass balance, and cryoprotection during subsequent freezing and thawing was monitored as change in myosin Ca 3+ ATPase activity. Vacuum treatment had no effect on measured parameters. Initial sorbinal uptake and weight loss were greater at higher sorbitol concentrations, but adequate cryoprotection was achieved by all treatments when diffusion time following immersion was extended sufficiently. Injection of 60% sorbitol was fasier in achieving desired levels of sorbital in flsh ment and induced excellent cryoprotection. diffesion, vacuum, trout, sorbitol, ATPase.}, number={4}, journal={JOURNAL OF FOOD SCIENCE}, author={Goeller, LM and Amato, PM and Farkas, BE and Green, DP and Lanier, TC and Kong, CS}, year={2004}, month={May}, pages={E164–E171} }
 @article{riemann_lanier_swartzel_2004, title={Rapid heating effects on gelation of muscle proteins}, volume={69}, DOI={10.1111/j.1365-2621.2004.tb13635.x}, abstractNote={ABSTRACT:  The hypothesis was tested that total thermal input (combined time and temperature), rather than merely heating rate, is the determining factor in heat‐induced gel formation by muscle proteins. For comminuted pastes of pollock surimi and turkey breast, rapid heating plus a brief holding time at the endpoint temperature produced similar textural properties to gels, which were heated by a slower cook schedule and cooled immediately. These results suggest that the equivalent point method, a tool used to compare and communicate equivalent heat treatments for effecting bacterial reduction and/or enzyme inactivation, can be used to identify other heat processes having similar effects on gelation.}, number={7}, journal={Journal of Food Science}, author={Riemann, A. E. and Lanier, T. C. and Swartzel, K. R.}, year={2004}, pages={E308–314} }
 @article{perez-mateos_boyd_lanier_2004, title={Stability of omega-3 fatty acids in fortified surimi seafoods during chilled storage}, volume={52}, ISSN={["1520-5118"]}, DOI={10.1021/jf049656s}, abstractNote={Physical, chemical, and sensory properties of cooked surimi seafood gels (crab analogue) fortified with omega-3 fatty acids (FA) were monitored during chilled storage. Three sources of stabilized omega-3 FA (fish oil concentrate, menhaden oil, and a purified marine oil) were each incorporated into gels to an omega-3 FA content of 1.5 or 2.5%, w/w. Omega-3 FA stability, development of off-flavors, and changes in color and texture were monitored during chilled storage for 2 months. Gels with fish oil concentrate developed fishy flavor and aroma within 30 days and were eliminated from the study. Gels containing menhaden oil and purified marine oil exhibited little change in sensory properties or oxidation products throughout 2 months of storage. Relative polyene index values (ratio of polyunsaturated to saturated fatty acids) indicated that the omega-3 FA were stable at both levels of addition. Omega-3 fortified gels were whiter than control gels, and gel texture was modified when menhaden and purified oils were added but not significantly affected by the level of omega-3 addition.}, number={26}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={Perez-Mateos, M and Boyd, L and Lanier, T}, year={2004}, month={Dec}, pages={7944–7949} }
 @article{bell_farkas_hale_lanier_2002, title={Effects of retorting and storage on liquid mass transfer in canned skipjack (Katsuwonas pelamis) muscle}, volume={26}, ISSN={["1745-4549"]}, DOI={10.1111/j.1745-4549.2002.tb00484.x}, abstractNote={Mass loss of precooked tuna muscle during retorting and storage in cans impacts cannery yield and throughput. Changes in moisture content and mass of frozen, thawed, precooked tuna muscle chunks, canned in water, were determined after retorting and through five weeks of subsequent storage. Canned tuna pieces were retorted to equivalent lethality (F o -value of four) for different time and temperature processes. Retorting at a lower temperature, longer time resulted in less mass loss than higher temperature, shorter time processes. Canned storage of up to five weeks had no effect on muscle mass or moisture content.}, number={4}, journal={JOURNAL OF FOOD PROCESSING AND PRESERVATION}, author={Bell, JW and Farkas, BE and Hale, SA and Lanier, TC}, year={2002}, month={Oct}, pages={267–278} }
 @article{luck_lanier_daubert_kwanyuen_2002, title={Viscoelastic behavior of commercially processed soy isolate pastes during heating and cooling}, volume={67}, ISSN={["0022-1147"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-0036293043&partnerID=MN8TOARS}, DOI={10.1111/j.1365-2621.2002.tb10293.x}, abstractNote={ABSTRACT}, number={4}, journal={JOURNAL OF FOOD SCIENCE}, author={Luck, PJ and Lanier, TC and Daubert, CR and Kwanyuen, P}, year={2002}, month={May}, pages={1379–1382} }
 @article{bell_farkas_hale_lanier_2001, title={Effect of thermal treatment on moisture transport during steam cooking of skipjack tuna (Katsuwonas pelamis)}, volume={66}, ISSN={["0022-1147"]}, DOI={10.1111/j.1365-2621.2001.tb11337.x}, abstractNote={ABSTRACT:  Moisture and mass loss were determined during atmospheric steam cooking of skipjack tuna by measurement of muscle moisture content in whole fish and on‐line measurement of mass and temperature in fillets. Thermal denaturation temperatures of muscle proteins were measured by differential scanning calorimetry. Muscle moisture content and mass loss were dependent on muscle temperature. Temperature distribution was predicted and mass loss rates were calculated in fillets. A decreasing rate of mass loss was followed by a steady rate period and a resumption of a decreasing rate period. The increased loss of mass during the steady period corresponded to thermal denaturation temperatures of muscle proteins. Changes in mass loss rates resulted from a gradient of muscle changes produced by the temperature gradient created during cooking.}, number={2}, journal={JOURNAL OF FOOD SCIENCE}, author={Bell, JW and Farkas, BE and Hale, SA and Lanier, TC}, year={2001}, month={Mar}, pages={307–313} }
 @article{kang_lanier_1999, title={Bovine plasma protein functions in surimi gelation compared with cysteine protease inhibitors}, volume={64}, ISSN={["0022-1147"]}, DOI={10.1111/j.1365-2621.1999.tb15924.x}, abstractNote={ABSTRACT:}, number={5}, journal={JOURNAL OF FOOD SCIENCE}, author={Kang, IS and Lanier, TC}, year={1999}, pages={842–846} }
 @article{carvajal_macdonald_lanier_1999, title={Cryostabilization mechanism of fish muscle proteins by maltodextrins}, volume={38}, ISSN={["0011-2240"]}, DOI={10.1006/cryo.1998.2142}, abstractNote={Maltodextrins of varying mean molecular weights (MW) were evaluated for cryoprotective ability in Alaska pollock surimi (leached mince) versus sucrose or a sucrose-sorbitol mixture. Treatments were stored either isothermally at -8, -14, or -20 degrees C for 3 months or freeze-thaw (F/T) cycled six times to induce freeze-related protein denaturation, measured as a decrease in myosin Ca+2 ATPase activity and change in heat-induced gel-forming ability. Results indicated good cryoprotection by all maltodextrins at -20 degrees C isothermal storage irrespective of MW, but poor cryoprotection by higher MW maltodextrins at higher isothermal storage temperatures or after F/T cycling. These observations, and surface tension measurements of maltodextrin solutions, indicated that lower MW maltodextrins likely cryoprotect by a preferential solute exclusion mechanism, similar to sucrose and sorbitol. Higher MW maltodextrins presumably cryoprotect at lower storage temperatures via a reduced water mobility mechanism. As the MW of maltodextrins increased the gelling ability of the surimi was increasingly impaired, such that evidence of cryoprotection from gelation data was obscured. Copyright 1999 Academic Press.}, number={1}, journal={CRYOBIOLOGY}, author={Carvajal, PA and MacDonald, GA and Lanier, TC}, year={1999}, month={Feb}, pages={16–26} }
 @article{ashie_lanier_1999, title={High pressure effects on gelation of surimi and turkey breast muscle enhanced by microbial transglutaminase}, volume={64}, ISSN={["0022-1147"]}, DOI={10.1111/j.1365-2621.1999.tb15115.x}, abstractNote={ABSTRACT}, number={4}, journal={JOURNAL OF FOOD SCIENCE}, author={Ashie, INA and Lanier, TC}, year={1999}, pages={704–708} }
 @article{ashie_lanier_macdonald_1999, title={Pressure-induced denaturation of muscle proteins and its prevention by sugars and polyols}, volume={64}, ISSN={["0022-1147"]}, DOI={10.1111/j.1365-2621.1999.tb15919.x}, abstractNote={ABSTRACT:}, number={5}, journal={JOURNAL OF FOOD SCIENCE}, author={Ashie, INA and Lanier, TC and MacDonald, GA}, year={1999}, pages={818–822} }
 @article{choi_lanier_lee_cho_1999, title={Purification and characterization of alkaline proteinase front Atlantic menhaden muscle}, volume={64}, ISSN={["0022-1147"]}, DOI={10.1111/j.1365-2621.1999.tb15908.x}, abstractNote={ABSTRACT:}, number={5}, journal={JOURNAL OF FOOD SCIENCE}, author={Choi, YJ and Lanier, TE and Lee, HG and Cho, YJ}, year={1999}, pages={768–771} }
 @article{choi_cho_lanier_1999, title={Purification and characterization of proteinase from Atlantic menhaden muscle}, volume={64}, ISSN={["0022-1147"]}, DOI={10.1111/j.1365-2621.1999.tb15909.x}, abstractNote={ABSTRACT:}, number={5}, journal={JOURNAL OF FOOD SCIENCE}, author={Choi, YJ and Cho, YJ and Lanier, TC}, year={1999}, pages={772–775} }
 @inbook{lanier_1998, title={High pressure processing effects on fish proteins}, volume={434}, DOI={10.1007/978-1-4899-1925-0_5}, abstractNote={Salted pastes of surimi, a myofibrillar concentrate of fish muscle, gel at pressures near 300 MPa. High pressure processing has been thought to induce de-naturation and gelation of myofibrillar proteins mainly by disruption of protein intramolecular hydrophobic interactions which subsequently reform intennolecularly. We have shown that pressure-induced surimi gels evidence disulfide bonding as well. Endogenous transglutaminase (TGase) evidently survives the pressure treatment, and subsequent TGase-mediated setting of Alaska pollock surimi pastes at 25°C results in very strong gels as compared to those prepared without prior pressurization. High pressure during freezing or thawing greatly accelerates these operations and can reduce ice crystal size and associated tissue damage. Yet pressure treatment can destabilize proteins which might lower fish quality. Infusion of certain carbohydrates into muscle prior to pressure-assisted freezing/thawing can achieve both baroprotection and cryoprotection of the muscle proteins. Pressure treatment has not proven useful for inactivation of proteolytic enzymes that degrade fish quality.}, booktitle={Process-induced chemical changes in food (Advances in experimental medicine and biology ;  v. 434)}, publisher={New York: Plenum Press}, author={Lanier, T. C.}, editor={F. Shahidi, C.-T. Ho and Chuyen, N.Editors}, year={1998}, pages={45–55} }
 @article{gilleland_lanier_hamann_1997, title={Covalent bonding in pressure-induced fish protein gels}, volume={62}, ISSN={["1750-3841"]}, DOI={10.1111/j.1365-2621.1997.tb15442.x}, abstractNote={ABSTRACT}, number={4}, journal={JOURNAL OF FOOD SCIENCE}, author={Gilleland, GM and Lanier, TC and Hamann, DD}, year={1997}, pages={713-+} }
 @misc{lanier_akahane_1986, title={Method of retarding denaturation of meat products}, volume={4,572,838}, number={1986 Feb. 25}, publisher={Washington, DC: U.S. Patent and Trademark Office}, author={Lanier, T. C. and Akahane, T.}, year={1986} }