Multivariate strategy in screening of enzymes to be used for whey protein hydrolysis in an enzymatic membrane reactor

作者：Cheison Seronei Chelulei; Wang Zhang^*; Xu Shi Ying

来源：International Dairy Journal, 2007, 17(4): 393-402.

DOI：10.1016/j.idairyj.2006.05.006

• enzyme selection
• residual enzyme activity
• free amino acids
• enzymatic membrane reactor
• protease N

Proteinase activities for Alcalase (R) 2.4L (EC 3.4.21.62), Flavourzyme (R) (EC 3.4.11.1), Protease A (EC 3.4.24.39) and Protease N (IUB 3.4.24.28) were determined using 2% whey protein isolate (WPI) and 2% casein. The optimum substrate and enzyme concentrations and temperature were determined by the pH-stat method. Residual enzyme activity, hydrolysate molecular weight and free amino acid (FAA) content were determined. Protease N and Alcalase (R) 2.4L had the highest proteinase activities on casein and WPI, respectively. Alcalase (R) 2.4L was more stable in the presence of WPI while Protease N was inhibited by hydrolysates, and like Protease A which released high FAAs, they produced shorter peptides. Flavourzyme (R) hydrolysed WPI poorly and released the highest FAAs. Short peptides were removed by 5% trichloroacetic acid (TCA) and 3.5% 5-sulphosalicylic acid before FAA analysis by reversed phase high-performance liquid chromatography (RP-HPLC) of Flavourzyme (R) and Protease A hydrolysates, but were detected in Alcalase (R) 2.4L and Protease N hydrolysates. The enzyme activities for WPI hydrolysis in an enzymatic membrane reactor were Flavourzyme (R) < Protease A < Alcalase (R) 2.4L <= Protease N.

• 出版日期2007-4
• 单位江南大学