Enzymatic Solubilization of Heat-denatured Cheese Whey Protein

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Abstract
Rosolubilization 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 N 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 N 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% N, 4.53% fat, 2.6% moisture, .23% lactose and 2.9% ash.

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