![]() ![]() The values for milk-clotting and proteolytic activity of the kiwifruit pulp extract were evaluated at different temperatures and pH parameters in order to obtain a high value of the MCA/PA ratio we found that a temperature of 40 ☌ in combination with a pH value of 5.5 allowed us to obtain the best performance. The aqueous extract obtained from the pulp showed a hydrolytic activity toward both κ-casein and semi-skimmed milk. ![]() Although the aqueous extract obtained from the kiwifruit peel was able to hydrolyze semi-skimmed milk, it did not break down κ-casein. Data revealed the presence of the enzyme both in the peel and in the pulp of the fruit. In detail, polyacrylamide gel electrophoresis (SDS-PAGE) was used to investigate the presence of actinidin, the kiwifruit enzyme involved in κ-casein hydrolysis, in different tissues (pulp, peel, and whole fruit) of ripe and unripe kiwifruits. In the present study, a kiwifruit aqueous extract was developed and used as a coagulant enzyme in cheesemaking. ![]()
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