The re-association of disintegrated casein micelles was investigated using a combined high pressure and enzymatic treatment with chymosin at 20 C and 150 or 200 MPa. The amphiphilic, growth-limiting character of k-casein was altered in the pressure-disintegrated state of the casein micelle. With increasing amounts of k-casein being hydrolysed, less micellar surface can be covered with intact k-casein after high pressure treatment. Therefore, larger particles with shifted surface-to-volume ratio were expected to occur with increasing degree of hydrolysis (DH) of k-casein. Higher DH values led to larger reformed casein micelles. As compared with a control sample, the relative particle diameter showed a strong correlation to DH. This could be attributed to the re-association of caseins or micellar fragments forming micelles similar in structure as compared with native ones. Gelling similar to that in standard renneting, only occurred at DH levels above 0.80.
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The re-association of disintegrated casein micelles was investigated using a combined high pressure and enzymatic treatment with chymosin at 20 C and 150 or 200 MPa. The amphiphilic, growth-limiting character of k-casein was altered in the pressure-disintegrated state of the casein micelle. With increasing amounts of k-casein being hydrolysed, less micellar surface can be covered with intact k-casein after high pressure treatment. Therefore, larger particles with shifted surface-to-volume ratio...
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