Xiaolin L. Huang

Works (8)

Updated: July 5th, 2023 16:04

2014 journal article

Evaluation and comparison of sustainability performance and visual preference of residential landscape elements

HortTechnology, 24(3), 318–324.

By: X. Huang & J. Sherk

Source: NC State University Libraries
Added: August 6, 2018

1999 journal article

Modification of rheological properties of whey protein isolates by limited proteolysis

NAHRUNG-FOOD, 43(2), 79–85.

By: X. Huang n, G. Catignani n & H. Swaisgood*

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Source: Web Of Science
Added: August 6, 2018

1997 journal article

Comparison of the properties of trypsin immobilized on 2 Celite(TM) derivatives

JOURNAL OF BIOTECHNOLOGY, 53(1), 21–27.

By: X. Huang n, G. Catignani n & H. Swaisgood n

author keywords: immobilized trypsin; succinamidopropyl-Celite; aminopropyl-Celite; beta-lactoglobulin
MeSH headings : Diatomaceous Earth / chemistry; Enzymes, Immobilized / chemistry; Enzymes, Immobilized / metabolism; Hydrogen-Ion Concentration; Kinetics; Trypsin / chemistry; Trypsin / metabolism
TL;DR: The two methods of immobilization on Celite gave biocataysts with similar kinetic properties but immobilized on SAPC yielded slightly higher loadings and higher specific activities. (via Semantic Scholar)
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Source: Web Of Science
Added: August 6, 2018

1997 journal article

Micro-scale method for determining foaming properties of protein

JOURNAL OF FOOD SCIENCE, 62(5), 1028-&.

By: X. Huang n, G. Catignani n & H. Swaisgood n

author keywords: microscale whipping method; foam properties; protein
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Source: Web Of Science
Added: August 6, 2018

1996 journal article

Improved emulsifying properties of beta-barrel domain peptides obtained by membrane-fractionation of a limited tryptic hydrolysate of beta-lactoglobulin

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 44(11), 3437–3443.

By: X. Huang  n, G. Catignani n & H. Swaisgood n

author keywords: beta-lactoglobulin; tryptic hydrolysate; limited proteolysis; immobilized trypsin; emulsifying properties; beta-barrel domain
TL;DR: Comparison of the surface and emulsifying properties of the peptide fraction with those of intact β-lactoglobulin indicated that the domain peptides have a lower surface hydrophobicity and a slightly higher surface and interfacial tension. (via Semantic Scholar)
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Source: Web Of Science
Added: August 6, 2018

1995 journal article

IMMOBILIZATION OF BIOTINYLATED TRANSGLUTAMINASE BY BIOSELECTIVE ADSORPTION TO IMMOBILIZED AVIDIN AND CHARACTERIZATION OF THE IMMOBILIZED ACTIVITY

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 43(4), 895–901.

By: X. Huang*, G. Catignani & H. Swaisgood

author keywords: IMMOBILIZED TRANSGLUTAMINASE; BIOTINYLATED TRANSGLUTAMINASE; BIOSELECTIVE ADSORPTION; IMMOBILIZED AVIDIN; CROSS-LINKED ALPHA(S)-CASEIN
TL;DR: The pH optima and temperature dependences of enzyme catalysis were similar for both the soluble and immobilized enzyme, although the slight differences observed for the immobilized form were also indicative of mass transfer effects. (via Semantic Scholar)
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6. Clean Water and Sanitation (OpenAlex)
Source: Web Of Science
Added: August 6, 2018

1994 journal article

COMPARISON OF THE SIZE AND RATE OF FORMATION OF PEPTIDES RELEASED BY LIMITED PROTEOLYSIS OF BETA-LACTOGLOBULIN-A AND BETA-LACTOGLOBULIN-B WITH IMMOBILIZED TRYPSIN

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 42(6), 1281–1284.

By: X. Huang*, G. Catignani & H. Swaisgood

TL;DR: Proteolytic susceptibility of β-lactoglobulin (β-Lg) genetic variants A and B was determined by subjection to immobilized trypsin by fractionation with anion-exchange chromatography and by denaturing gel electrophoresis of the isolated fractions. (via Semantic Scholar)
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Source: Web Of Science
Added: August 6, 2018

1994 journal article

RELATIVE STRUCTURAL STABILITIES OF BETA-LACTOGLOBULIN-A AND BETA-LACTOGLOBULIN-B AS DETERMINED BY PROTEOLYTIC SUSCEPTIBILITY AND DIFFERENTIAL SCANNING CALORIMETRY

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 42(6), 1276–1280.

By: X. Huang*, G. Catignani & H. Swaisgood

TL;DR: Lower structural stability of variant A is indicated by a 5 o C lower thermal denaturation temperature observed for β-Lg A by DSC, and a more rapid disappearance of intact β- Lg A during proteolysis of equimolar mixtures of the two variants. (via Semantic Scholar)
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Source: Web Of Science
Added: August 6, 2018

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