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Crosslinking of milk whey proteins by transglutaminase

Paper ID Volume ID Publish Year Pages File Format Full-Text
35581 45096 2008 7 PDF Available
Title
Crosslinking of milk whey proteins by transglutaminase
Abstract

Milk whey powder was used to evaluate the polymerization reaction of the proteins α-lactalbumin and β-lactoglobulin by the enzyme transglutaminase. Measurement of the flow behavior was carried out as a parameter to monitor the viscosity changes of the solutions after the enzymatic reaction. Through an experimental design the optimum reaction conditions were evaluated as a function of the enzyme concentration, temperature and reaction time. The protein polymerization was favored when the solutions were kept at a temperature of 36 °C for 4 h. The formation of polymers increased proportionally with an increase in transglutaminase up to a maximum point of substrate exhaustion, reaching an ideal enzymatic concentration of 50 U of transglutaminase/g of protein. An increase in the content of high molecular weight polymers in the milk whey solutions resulted in an increase in the consistency index of the solutions, favoring non-Newtonian behavior.

Keywords
α-Lactalbumin; β-Lactoglobulin; Transglutaminase; Crosslinking; Rheology; Electrophoresis
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 43, Issue 7, July 2008, Pages 788–794
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us