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Enzymatic Solubilization of Heat-denatured Cheese Whey Protein

Research Department, Nestle Products Technical Assistance Co., Ltd., Case Postale 1009, CH-1001 Lausanne, Switzerland

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.