Abstract

Casein hydrolysates were obtained using enzyme preparations (EPs) of bacterial proteases, Alcalase, Protamex, Neutrase, and Protosubtilin. The dependence of the hydrolysate bitterness on the decrease of the EP proteolytic activity in the presence of PMSF, an inhibitor of serine proteases, was observed. It was found that the use of Neutrase provided non-bitter hydrolysates, while the proteolytic activity of Neutrase decreased by 44% in the presence of PMSF. A domestic EP of Protosubtilin lost 59% activity in the presence of PMSF and formed bitter hydrolysates. Casein hydrolysates obtained using Alcalase were characterized by the most severe bitterness, probably due to the fact that almost all proteolytic activity in this preparation is represented by a serine protease. The Bacillus subtilis 359 strain with a ratio of neutral and serine protease activities of 52 to 48% was selected from the VNIIPBT Collection of Bacterial Producers of Proteases. The concentrated preparation was obtained from the culture liquid of B. subtilis 359 strain by spray-drying. The preparation obtained hydrolyzed casein similarly to Neutrase and ensured the absence of bitterness in hydrolysates. neutral protease, serine protease, bitterness of hydrolysates, Bacillus subtilis This work was financially supported by a Grant of the Basic Research Program of the Russian Academy of Sciences for 2019-2021 (Project no. 0529-2019-0066).

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