Relationship between some characteristics of WPC hydrolysates and the enzyme complement in commercially available proteinase preparations

Endoproteinase and exopeptidase activities were determined in nine commerci ally available enzyme preparations using synthetic fluorogenic substrates a t pH 7.0 and 8.0 and at 37 and 50 degrees C. Four Bacillus (i.e. Protamex, Alcalase 0.6 L, Neutrase and Neutral Protease), three Aspergillus (i.e. Cor olase 7092, Fungal Protease and Flavourzyme) and two porcine pancreatic (i. e., PTN 3.0S powder and PTN 3.0S granulated) preparations were analysed. Co nsiderable variations in the endoproteinase, elastase-like, chymotryptic an d tryptic activities were observed. Flavourzyme contained high aminopeptida se, while Fungal Protease had high X-prolyl-dipeptidyl-aminopeptidase activ ity. Significant differences were observed in the characteristics of the WP C hydrolysates generated with the above preparations. Some trends were obse rved between enzyme complement and hydrolysate characteristics, e.g. enzyme preparations with high exopeptidase activities resulted in hydrolysates ha ving high DH values and low levels of hydrophobic peptides. However, in gen eral it was not possible to directly predict the characteristics of WPC hyd rolysates from the endoproteinase and exopeptidase complement in the crude enzyme preparations. (C) 1999 Elsevier Science Ltd. All rights reserved.