Specific viscosity during hydrolysis

Figure 4. Decrease in specific viscosity during the hydrolysis of CMC solution by E-3-1, E-3-2, E-3-3, E-3-4, and E-3-5. Reaction mixture consists of 3.0 mL 1% CMC, 7.0 mL 0.1M sodium acetate buffer, pH 4.0, and 2.0 mL enzyme solution containing an amount of protein equivalent to an optical density of 0.05 at 280 nm. The reaction mixture was carried out at 30°C in an Ostwald viscometer.

Figure 19. Decrease in specific viscosity during the hydrolysis of CMC solution by En-1. Reaction conditions are the same as in Figure 18 final enzyme concentration 2.2 X 10 4%.

Enzymatic gelation of partially heat-denatured whey proteins by trypsin, papain, pronase, pepsin, and a preparation of Streptomyces griseus has been studied (Sato et al., 1995). Only peptic hydrolysate did not form a gel. The strength of the gel depended on the enzyme used and increased with increasing DH. Hydrolysis of whey protein concentrate with a glutamic acid specific protease from Bacillus licheniformis at pH 8 and 8% protein concentration has been shown to produce plastein aggregates (Budtz and Nielsen, 1992). The viscosity of the solution increased dramatically during hydrolysis and reached a maximum at 6% DH. Incubation of sodium caseinate with pepsin or papain resulted in a 55-77% reduction in the apparent viscosity (Hooker et al., 1982). 

Effects of the solvent, polymerization time, intrinsic viscosity and pH on the degree of the specific rotation of polyhexamethylene-c -tartaramide were investigated. From the results of hydrolysis of the polymer, it was found that c/-tartaric acid is not racemized during condensation polymerization. Interfacial polycondensation of diamines with r/-tartaric acid derivatives failed. 

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