@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{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{clare_lillard_ramsey_amato_daubert_2007, title={Calcium effects on the functionality of a modified whey protein ingredient}, volume={55}, ISSN={["1520-5118"]}, DOI={10.1021/jf071613z}, abstractNote={The primary objective for this study addressed the effects of supplemental calcium on the functional properties of a modified whey protein ingredient (mWPC), prepared by acidification to pH 3.35, followed by extended heat treatment, gelation, and spray drying. In the presence of added calcium (mWPC-Ca2+), protein solutions showed increased thickening capacity, especially under refrigeration temperatures, compared to dispersions made with mWPC alone. A rheological assessment included the determination of (i) power law parameters, (ii) viscoelastic properties, and (iii) the effects of heating and cooling on these protein systems. The sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) banding profile suggested that various disulfide-linked molecular forms of beta-lactoglobulin, bovine serum albumin, and immunoglobulin were likely formed during manufacturing of the mWPC ingredient based on the patterns obtained when electrophoresis was performed in the absence of beta-mercaptoethanol compared to those observed with commercial WPC samples. An enhanced water-holding capacity was measured in mWPC-Ca2+ dispersions. Differential scanning calorimetry established that the addition of calcium salts caused a 2-fold increase in the amount of bound or unfreezeable water compared to mWPC controls. The physical appearance of the network structure varied significantly upon visualization with scanning electron microscopy, in which case the formation of large, rounded, spherical structures was noted in mWPC-Ca2+ samples, ascribed to an increased surface tension caused by the higher salt content. Ultimately, such attributes may afford distinct advantages for whey-based ingredients intended for application within food systems, especially under cold processing conditions.}, number={26}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={Clare, Debra A. and Lillard, S. John and Ramsey, Sharon R. and Amato, Penny M. and Daubert, Christopher R.}, year={2007}, month={Dec}, pages={10932–10940} }
 @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} }