Enzymatic Solubilization of Heat-denatured Cheese Whey Protein Export

@article{citeulike:6080093, abstract = {Resolubilization of heat-denatured cheese whey protein was achieved by partial enzymatic hydrolysis of the protein with food-grade proteases. The efficiency with which porcine, trypsin, papain, and neutral protease from Bacillus subtilis solubilized the water-insoluble protein was compared by measuring the percentage of water-soluble nitrogen of the corresponding digests. The tryptic digest was completely soluble at neutral pH and was over 90\% water-soluble at pH 6.0. This digest had a pronounced solubility minimum of 65\% at pH 4.5. Neutral protease gave a digest with similar pH dependence of the solubility, but the percents of water-soluble nitrogen were all below those of the tryptic digest. Papain gave a digest with maximum solubility at pH 3.0 and approximately 80\% solubility at neutral pH. The solubility minimum was again at pH 4.5. Trypsin proved the most potent protease for solubilizing heat-denatured whey protein. With this enzyme, a water-soluble whey protein preparation was obtained which contained 13.2\% nitrogen, 4.5 3\% fat, 2.6\% moisture, .23\% lactose, and 2.9\% ash.}, author = {Monti, J. C. and Jost, R.}, citeulike-article-id = {6080093}, citeulike-linkout-0 = {http://jds.fass.org/content/61/9/1233.abstract}, citeulike-linkout-1 = {http://jds.fass.org/content/61/9/1233.full.pdf}, day = {1}, journal = {J. Dairy Sci.}, keywords = {enzymatic\_hydrolysis, heat, protein, solubility, whey}, month = {September}, number = {9}, pages = {1233--1237}, posted-at = {2009-11-06 07:40:16}, priority = {2}, title = {Enzymatic Solubilization of Heat-denatured Cheese Whey Protein}, url = {http://jds.fass.org/content/61/9/1233.abstract}, volume = {61}, year = {1978} }

TY - JOUR ID - citeulike:6080093 L3 - citeulike-article-id:6080093 N2 - Resolubilization of heat-denatured cheese whey protein was achieved by partial enzymatic hydrolysis of the protein with food-grade proteases. The efficiency with which porcine, trypsin, papain, and neutral protease from Bacillus subtilis solubilized the water-insoluble protein was compared by measuring the percentage of water-soluble nitrogen of the corresponding digests. The tryptic digest was completely soluble at neutral pH and was over 90% water-soluble at pH 6.0. This digest had a pronounced solubility minimum of 65% at pH 4.5. Neutral protease gave a digest with similar pH dependence of the solubility, but the percents of water-soluble nitrogen were all below those of the tryptic digest. Papain gave a digest with maximum solubility at pH 3.0 and approximately 80% solubility at neutral pH. The solubility minimum was again at pH 4.5. Trypsin proved the most potent protease for solubilizing heat-denatured whey protein. With this enzyme, a water-soluble whey protein preparation was obtained which contained 13.2% nitrogen, 4.5 3% fat, 2.6% moisture, .23% lactose, and 2.9% ash. IS - 9 JF - J. Dairy Sci. EP - 1237 TI - Enzymatic Solubilization of Heat-denatured Cheese Whey Protein VL - 61 SP - 1233 KW - enzymatic_hydrolysis KW - heat KW - protein KW - solubility KW - whey AU - Monti, JC AU - Jost, R PY - 1978/09/01/ UR - http://jds.fass.org/content/61/9/1233.abstract ER -