Cross-Linking of Whey Proteins by Enzymatic Oxidation

The applicability of enzymatic oxidation for polymerization of whey proteins [in whey protein isolate (WPI)] has been investigated, using three different oxidoreductases with different specificities (microbial peroxidase, fungal laccase, and bovine plasma monoamine oxidase) to induce oxidation. All...

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Bibliographic Details
Published in:Journal of agricultural and food chemistry Vol. 46; no. 4; pp. 1326 - 1333
Main Authors: Otte, Jeanette, Qvist, Karsten Bruun
Format: Journal Article
Language:English
Published: Washington, DC American Chemical Society 01-04-1998
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Summary:The applicability of enzymatic oxidation for polymerization of whey proteins [in whey protein isolate (WPI)] has been investigated, using three different oxidoreductases with different specificities (microbial peroxidase, fungal laccase, and bovine plasma monoamine oxidase) to induce oxidation. All three enzymes were able to induce formation of oligomers and polymers of whey proteins under various conditions, but their modes of action seemed to diverge, as they affected the two main whey proteins β-lactoglobulin and α-lactalbumin differently:  for example, peroxidase (in the presence of hydrogen peroxide) mainly acted on β-lactoglobulin, laccase (in the presence of chlorogenic acid) mainly worked on α-lactalbumin, and monoamine oxidase acted somewhat on both proteins. None of the oxidoreductases induced full polymerization of WPI, as opposed to cross-linking with microbial transglutaminase with a reductant present, which polymerizes the whey proteins fully. None of the oxidoreductases could induce gelling of WPI solutions with 10−20% protein. Keywords: Enzymatic; oxidation; whey proteins; cross-linking; polymerization
Bibliography:Q04
Q02
1997089512
istex:C072A80F69331DB74FE743B884FC1C31184DBE8B
ark:/67375/TPS-7BRTH56B-2
ISSN:0021-8561
1520-5118
DOI:10.1021/jf970743c