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- Title
Properties of casein micelles cross-linked by transglutaminase.
- Authors
JEONG-HAN MOON; YOUN-HO HONG; HUPPERTZ, THOM; FOX, PATRICK F; KELLY, ALAN L
- Abstract
Factors affecting the cross-linking of milk proteins by transglutaminase (TGase) were studied. Cross-linking of caseins in bovine skim milk was optimal over a very wide pH range. The role of micellar calcium phosphate (MCP) in maintaining the integrity of TGase-treated casein micelles was studied by incubating skim milk with 0.01% (w/v) TGase at 30°C for 1–24 h, followed by removal of MCP from untreated or TGase-treated milk by acidification and dialysis. The protein content and profile of the samples were determined by Kjeldahl and SDS-PAGE, respectively. Whey proteins in unheated milk were not susceptible to TGase-induced cross-linking. The higher level of sedimentable protein in MCP-free TGase-treated milk than in MCP-free control milk indicated that TGase treatment partially prevented disintegration of the micelle on removal of MCP, probably due to extensive intramicellar TGase-induced cross-linking of casein molecules which led to the formation of sedimentable covalently bonded casein aggregates.
- Subjects
MILK; MILK proteins; COMPOSITION of milk; CASEINS; SKIM milk
- Publication
International Journal of Dairy Technology, 2009, Vol 62, Issue 1, p27
- ISSN
1364-727X
- Publication type
Article
- DOI
10.1111/j.1471-0307.2008.00442.x