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Engineering of caseins and modulation of their structures and interactions

Paper ID Volume ID Publish Year Pages File Format Full-Text
14682 1237 2009 8 PDF Available
Title
Engineering of caseins and modulation of their structures and interactions
Abstract

β-Casein (β-CN) is a milk protein widely used in food industries because of its mild emulsifying properties due to its amphiphilicity. However, the elements determining its micellization behavior in solution and interfacial behavior at the air–water interface are not well known. In order to study how the forced dimerisation influences functional properties of β-CN, recombinant wild-type β-CN was produced and distal cysteinylated forms of recombinant β-CN were engineered. We show that 1) cysteinylated β-CN formed mainly dimers bridged by disulfide bonds; 2) the process of dimerization adds to the micellization process with temperature and is poorly reversible; 3) covalent disulfide linkage forms at the air–water interface at a lower temperature than in bulk. In conclusion, the location of the cysteinylation in the C-terminus or N-terminus or both is of importance for the properties of β-CN.

Keywords
Casein; Polymerization; Disulfide bond; Micellization; Interfacial properties
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biotechnology Advances - Volume 27, Issue 6, November–December 2009, Pages 1124–1131
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