Degradation of soluble and insoluble proteins by Bacteroides amylophilus protease and by rumen microorganisms.
Various soluble and insoluble proteins (6.25 mg) were incubated at 37 C with partially purified protease from Bacteroides amylophilus (156 micrograms) in 2.0 ml of .1 M potassium phosphate buffer, pH 7.6, for 2, 4, 6 and 18 hr, and the liberated amino acids were determined by the ninhydrin method. Results showed that (1) although soluble, serum albumin and ribonuclease A were resistant to hydrolysis; (2) soluble and insoluble proteins of soybean meal were hydrolyzed at almost identical rates; (3) soluble proteins from soybean meal, rapeseed meal and casein were hydrolyzed at different rates, and (4) treatment of resistant proteins (serum albumin, ribonuclease A and insoluble fish meal and rapeseed meal proteins) with mercaptoethanol in 8 M urea or oxidation with performic acid rendered these proteins susceptible to hydrolysis. It is concluded that (1) solubility or insolubility of a protein is not by itself an indication of the protein's resistance or susceptibility to hydrolysis by rumen bacterial protease; (2) structural characteristics of the properties which renders feed protein resistant to degradation is the presence of crosslinking disulfide bonds.
D000818:Animals; D001439:Bacteroides / Q000378:metabolism*; D002364:Caseins / Q000378:metabolism; D002417:Cattle / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism*; D012417:Rumen / Q000378:metabolism* / Q000382:microbiology; D012995:Solubility; D013025:Glycine max
D002364:Caseins; D011506:Proteins; D010447:Peptide Hydrolases