chymosin

Request TOC of this Report- https://www.factmr.com/connectus/sample?flag=T&rep_id=2651 The casein glycomacropeptide is mainly derived from whey during cheese making by the action of chymosin. The casein glycomacropeptide provides a complete source of protein and an excellent dietary supplement for children and adults.

DZIUBA & MINKIEWICZ (1996) reported that a higher level of [kappa]-CN glycosylation, associated with smaller and more hydrophobic micelles, favors firmer rennet gels, reflecting increased [kappa]-CN hydrolysis through chymosin and a closer packing arrangement (and aggregation between) of para-CN micelles forming the basic building blocks (para-CN aggregates) of the gel matrix.

bulgaricus) and enzyme chymosin (Double strength Chy-max, 500000 MCU/mL, Pifzer Inc, Milwaukee, WI, USA) were used for Mozzarella cheese manufacturing.

The protein chymosin, produced in the stomach, turned liquid milk into a semisolid form.

Glycomacropeptide is a 64-amino acid glycophosphopeptide (7-11 kDa) and is part of the K-casein micelle in bovine milk that is cleaved by chymosin during the cheese-making process [5].

Traditional calf rennet and fermentation-produced camel chymosin (FPCC), which has ratio between milk clotting activity and general proteolytic activity 7 times higher than calf chymosin [22] , were used as rennet formulations in order to obtain different body texture between formulations.

Fermentation of a skim milk concentrate with Streptococcus thermophilus and chymosin: structure, viscoelasticity and syneresis of gels.

Hansen Ireland Ltd.) and chymosin (CHY-MAX(r), Chr.

Glycomacropeptide (GMP) is an active biopeptide derived from milk K-casein that is released to the whey during cheese-making process by the action of chymosin [13].

The chymosin cleavage site of camel milk k-CN was found at the [Phe.sup.9]-[Ile.sup.9]8 amino-acid sequence site, whereas the hydrolysis site in bovine milk is [Phe.sup.105]-[Met.sup.106] [12].

They justified the findings by reasoning that during storage, the degradation of [sup.2]-casein due to the action of chymosin and plasmin, results in the formation of smaller peptides that may be responsible for bitterness in dahi.