Characterization of hydrolysates produced by mild-acid treatment and enzymatic hydrolysis of defatted soybean flour |
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| Affiliation: | 1. Department of Product Development, Faculty of Agro-Industry, Kasetsart University, 50 Ngam Wong Wan Road, Chatuchak, Bangkok 10900, Thailand;2. Department of Biotechnology, Faculty of Agro-Industry, Kasetsart University, 50 Ngam Wong Wan Road, Chatuchak, Bangkok 10900, Thailand;3. Food Science Program, College of Agriculture, Food and Natural Resources, University of Missouri, Columbia, MO 65211, USA;1. CBQF – Centro de Biotecnologia e Química Fina – Laboratório Associado, Escola Superior de Biotecnologia, Universidade Católica Portuguesa/Porto, Rua Arquiteto Lobão Vital, Apartado 2511, 4200 Porto, Portugal;2. IPROBYQ (Institute of Bio-technological and Chemical Processes) – College of Biochemical and Pharmaceutical Sciences, National University of Rosario, Suipacha 570, S2002LRK Rosario, Argentina;1. School of Food Science and Engineering, South China University of Technology, Guangzhou 510640, China;2. College of Tropical Agriculture and Forestry, Guangdong Agriculture Industry Business Polytechnic College, Guangzhou 510507, China;3. School of Chemical Sciences, University of Auckland, Auckland 1142, New Zealand;4. Guangdong Tianqi Biological Technology Co., Ltd, Foshan 528000, China;5. Shanghai Totole Food Ltd, Shanghai 201812, China |
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| Abstract: | Acid (0.05–0.2 N HCl) pre-treatments and subsequent enzymatic hydrolysis (Alcalase? and Flavourzyme?) of defatted soybean flour (DSF) were performed under aseptic conditions. The acid pre-treatment facilitated enzymatic hydrolysis of the protein in DSF by increasing the nitrogen solubility index. Protein was hydrolyzed primarily during the first 5 h of enzymatic hydrolysis. The degree of hydrolysis and α-amino nitrogen contents of the hydrolysates increased after acid pretreatment. The average peptide chain lengths were estimated at 7～8 amino acid units after 3 h hydrolyzation by Alcalase, and 3–5 amino acid units after 21 h by Flavourzyme/Alcalase mixture. Gel permeation chromatography provided molecular size distribution to determine the molecular weights of the corresponding hydrolysates. At the end of 24 h enzymatic hydrolysis, the amounts of free amino acid, dipeptide and tripeptide accounted for almost half of the proteins in the hydrolysate, while the oligopeptides constituted 40%. |
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