期刊
LWT-FOOD SCIENCE AND TECHNOLOGY
卷 42, 期 10, 页码 1717-1721出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.lwt.2009.04.005
关键词
Alcalase; Hydrolysis; Defatted peanut flour; Pepsin-pancreatin; Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE)
资金
- US Agency for International Development (USAID) [GDG-G-00-02-00012-00]
In vitro protein digestion studies were carried out on raw and roasted peanut flour as the starting material in the production of peanut protein hydrolysate. Peanut flour was hydrolyzed with alcalase and alternately in a sequential digestion with pepsin-pancreatin, both for up to 24 h. The degree of hydrolysis (DH) at different times of hydrolysis was determined using the trinitrobenzenesulfonic acid (TNBS) method. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was used to indicate destruction of native protein units in the enzymatic digests. Hydrolysis with alcalase was very rapid for the first 6 h after which a plateau was reached, whereas that with pepsin-pancreatin was more gradual reaching a plateau after 12 h of hydrolysis. Raw peanut hydrolyzed with alcalase and pepsin-pancreatin had 23% and 21% DH after 24 h respectively, whilst roasted peanut hydrolyzed with alcalase had 21% DH, with the pepsin-pancreatin hydrolysate recording the highest value of 25% after 24 h of hydrolysis. SDS-PAGE results showed that raw peanut samples behaved differently from the roasted samples; increasing hydrolysis time reduced larger peanut protein subunits, with only peptides of <20 kDa visible after hydrolysis for raw peanut, and virtually no distinct visible bands for the roasted peanut after 3 h of hydrolysis. (C) 2009 Elsevier Ltd. All rights reserved.
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