Crosslinking of casein by microbial transglutaminase and its resulting influence on the stability of micelle structure.
The influence of enzymatic crosslinking by microbial transglutaminase (mTG) on the stability of casein micelles of ultrahigh temperature (UHT)-treated milk in the presence of EDTA (0-0.45 mM) or ethanol (0-74 vol%) as well as under high hydrostatic pressures up to 400 MPa was investigated. Disintegration of micelles and changes in micelle size were monitored by the measurement of turbidity as well as by dynamic light scattering. The results show that the incubation of UHTtreated milk with mTG resulted in an improved micelle stability toward disintegration on addition of EDTA, ethanol, or pressure treatment. Intramicellar formed isopetides significantly enhanced the stability of casein micelles. It is supposed that net-like crosslinks are formed within the external region of the micelles and they adopt the stabilizing role of colloidal calcium phosphate within the micelles, thus making the micelles less contestable for disrupting influences.
Partschefeld
Claudia
C
Institute of Food Chemistry, Technische Universität Dresden, Dresden, Germany.
Schwarzenbolz
Uwe
U
Richter
Sven
S
Henle
Thomas
T
D000818:Animals; D002364:Caseins / Q000737:chemistry*; D002417:Cattle; D003102:Colloids / Q000737:chemistry*; D003432:Cross-Linking Reagents / Q000737:chemistry; D005511:Food Handling / Q000379:methods*; D006358:Hot Temperature; D008823:Micelles; D008892:Milk / Q000737:chemistry*; D011503:Transglutaminases / Q000378:metabolism*
D002364:Caseins; D003102:Colloids; D003432:Cross-Linking Reagents; D008823:Micelles; D011503:Transglutaminases