The Effects of Grass Carp Skin Gelatin and Whey Protein Interactions on Rheological and Textural Properties and Nanostructure

2017 ◽  
Vol 26 (7) ◽  
pp. 790-800
Author(s):  
Luyun Cai ◽  
Liping Leng ◽  
Jianrong Li ◽  
Xiaoqiang Chen ◽  
Joe M. Regenstein ◽  
...  
Keyword(s):  
Whey Protein ◽  
Protein Interactions ◽  
Grass Carp ◽  
Textural Properties

scholarly journals Effect of casein to whey protein ratios on the protein interactions and coagulation properties of low-fat yogurt

2016 ◽  
Vol 99 (10) ◽  
pp. 7768-7775 ◽  
Author(s):  
L.L. Zhao ◽  
X.L. Wang ◽  
Q. Tian ◽  
X.Y. Mao
Keyword(s):  
Whey Protein ◽  
Protein Interactions ◽  
Low Fat

The use of high hydrostatic pressure to modulate milk protein interactions for the production of an alpha-lactalbumin enriched-fraction

2018 ◽  
Vol 20 (2) ◽  
pp. 515-524 ◽  
Author(s):  
Alice Marciniak ◽  
Shyam Suwal ◽  
Michel Britten ◽  
Yves Pouliot ◽  
Alain Doyen
Keyword(s):  
Hydrostatic Pressure ◽  
Whey Protein ◽  
Protein Interactions ◽  
High Hydrostatic Pressure ◽  
Milk Protein ◽  
Protein Solution ◽  
Green Method ◽  
Alpha Lactalbumin

An innovative and green method for the fractionation of α-lactalbumin with 86% purity from whey protein solution was developed using high hydrostatic pressure as a pretreatment.

The cheesemaking potential of milk concentrated up to four-fold by ultrafiltration and heated in the range 90–97 °C

1990 ◽  
Vol 57 (4) ◽  
pp. 549-557 ◽  
Author(s):  
Margaret L. Green
Keyword(s):  
Electron Microscopy ◽  
Heat Treatment ◽  
Whey Protein ◽  
Protein Interactions ◽  
Heat Denaturation ◽  
The Difference

SummaryProperties of interest to cheesemaking were investigated with milks concentrated by ultrafiltration and heated at 90 °C or 95–97 °C for 15 s. The effects of light homogenization before concentration and of addition of CaCl2 after heating were assessed. No changes in casein–fat or casein–whey protein interactions were detected by electron microscopy. The heat denaturation of whey protein increased linearly as the milk became more concentrated. Coagulability by rennet after heat treatment increased with concentration to close to the unheated value in 3·5 to 4-fold concentrates. The decrease in curd firming rate by heat treatment was slightly affected by concentration and addition of CaCl2 restored some of the difference. Heat treatment reduced the rate of whey loss and slightly improved the curd structure but did not affect fat losses. Light homogenization slightly reduced heat denaturation of whey protein and whey loss.

scholarly journals Improved Gel Properties of Whey Protein-Stabilized Emulsions by Ultrasound and Enzymatic Cross-Linking

Gels ◽  
2021 ◽  
Vol 7 (3) ◽  
pp. 135
Author(s):  
Yanli Zhao ◽  
Shiqi Xue ◽  
Xinyue Zhang ◽  
Tiehua Zhang ◽  
Xue Shen
Keyword(s):  
Whey Protein ◽  
Disulfide Bonds ◽  
Noncovalent Interactions ◽  
Textural Properties ◽  
Industrial Applications ◽  
Cross Linking ◽  
Similar Frequency ◽  
Soluble Aggregate ◽  
Gelation Behavior ◽  
Cross Links

This study investigated the effects of high-intensity ultrasound (HUS) and transglutaminase pretreatment on the gelation behavior of whey protein soluble aggregate (WPISA) emulsions. HUS pretreatment and TGase-mediated cross-linking delayed the onset of gelation but significantly increased (p < 0.05) the gel firmness (G′) both after gel formation at 25 °C and during storage at 4 °C. The frequency sweep test indicated that all gels had a similar frequency dependence at 4 and 25 °C, and the elasticity and viscosity of the WPISA-stabilized emulsion gel were significantly enhanced by HUS pretreatment and TGase-mediated cross-linking (p < 0.05). HUS and TGase-mediated cross-linking greatly improved the textural properties of WPISA-stabilized emulsion gels, as revealed by their increases in gel hardness, cohesiveness, resilience, and chewiness. HUS pretreatment and TGase-mediated cross-linking significantly increased the water-holding capacity but decreased the swelling ratios of the gels (p < 0.05). Interactive force analysis confirmed that noncovalent interactions, disulfide bonds, and TGase-induced covalent cross-links were all involved in the formation of gel networks. In conclusion, the combination of HUS and TGase-mediated cross-linking were beneficial for improving the gelation properties of WPISA-stabilized emulsion as a controlled release vehicle for potential food industrial applications.

Whey protein interactions in acidic cold-set gels at different pH values

2007 ◽  
Vol 87 (6) ◽  
pp. 535-554 ◽  
Author(s):  
Angelo Luiz Fazani Cavallieri ◽  
Antonio Paulino Costa-Netto ◽  
Marcelo Menossi ◽  
Rosiane Lopes Da Cunha
Keyword(s):  
Whey Protein ◽  
Protein Interactions ◽  
Ph Values

scholarly journals Effects of Boswellia Serrata and Whey Protein Powders on Physicochemical Properties of Pork Patties

Foods ◽  
2020 ◽  
Vol 9 (3) ◽  
pp. 334 ◽  
Author(s):  
Fengqi Yang ◽  
Won-Young Cho ◽  
Nayeon Lee ◽  
Da-Hee Kim ◽  
Jihye Lee ◽  
...  
Keyword(s):  
Lipid Oxidation ◽  
Whey Protein ◽  
Meat Products ◽  
Textural Properties ◽  
Thiobarbituric Acid ◽  
Control Group ◽  
Processed Meat ◽  
Boswellia Serrata ◽  
Bacterial Colony ◽  
Pork Patties

Processed meat products are prone to oxidative damage and quality decline during storage; however, these problems can be mitigated by the proper formulation of meat productions. This study evaluated the effects of natural anti-oxidants found in Boswellia serrata (B), whey protein powder (W), and their combination on pork patties during storage, exploring changes in textural properties and lipid oxidation susceptibility. The 2% whey-added group exhibited a higher crude protein content than the untreated control group. The highest water-holding capacity and lowest cooking losses were observed in mixed-additive groups (WB1 (2% W/0.5% B) and WB2 (2% W/1.0% B), and the highest sensory scores for overall acceptability were obtained for WB1. Adding B. serrata can neutralize the hardness caused by whey powder, thereby improving palatability. From 7 d (days 7), the extents of lipid oxidation, determined using 2-thiobarbituric acid-reactive substances (TBARS) analysis, for the WB1 and WB2 groups were significantly lower than that of the control group. The WB1 and WB2 groups exhibited substantially suppressed total bacterial colony and Escherichia coli counts relative to the control group. Our findings suggest that the additive combination of B. serrata and whey protein powders can suppress lipid oxidation, improve storage stability, and enhance textural properties in the production of functional pork patties.

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