The rennet and acid coagulation properties of reconstituted micellar casein concentrate prepared using cold or warm microfiltration (MF), at similar casein contents, were investigated, with low-heat skim milk powder (LHSMP) as a control. The MF retentates had higher casein content (as % of total protein) compared with LHSMP, and heat-induced whey protein-casein aggregates were only present in LHSMP. All MF retentates showed shorter rennet coagulation times and higher gel strengths than LHSMP, which may be linked to lower levels of whey protein (either native or denatured). At similar casein contents, longer rennet coagulation times were evident for cold MF retentates compared with warm MF retentates, as the ratio of κ-CN as a function of total increased with the depletion of β-CN. In terms of acid-induced coagulation, all MF retentates coagulated at a pH >5, higher than the gelation pH of LHSMP (4.7-4.9), which was confirmed by microscopic and textural analysis. An inflection point (increase, followed by a decrease) in the storage modulus value was seen during the acidification of warm MF retentates, but not cold MF retentates; this may be related to structural rearrangements of the gel initiated by release of colloidal calcium phosphate and compacting of the structure of warm MF retentate gels as pH decreased. Both warm and cold MF retentates exhibited shorter rennet coagulation times, stronger rennet-induced gels and higher acid-induced gelation pH compared with LHSMP, which might influence their use for the manufacture of cheese or yogurt with tailored functionalities.
原文链接
分享
引用
