期刊名称：Journal of Nutritional Science and Vitaminology
印刷版ISSN：0301-4800
电子版ISSN：1881-7742
出版年度：1996
卷号：42
期号：4
页码：367-376
DOI：10.3177/jnsv.42.367
出版社：Center for Academic Publications Japan
摘要：Rice bran trypsin inhibitor (RBTI) was digested by pepsin alone or by pepsin and pancreatin with or without bovine serum albumin (BSA) to clarify the changes in trypsin inhibitory activity, apparent antigenicity, and molecular size of RBTI. In vitro pepsin digestion of RBTI in the absence of BSA caused the gradual loss of the trypsin inhibitory activity and antigenicity. This was mostly due to a progressive degradation of the native 14.5-kDa RBTI molecule to small molecular mass products. The presence of BSA in the digestion mixture prevented the RBTI degradation and was accompanied with a considerable protection of the activity and antigenicity. Similar results were also given by in vitro pepsin-pancreatin digestion. These findings suggest that RBTI may be present in its active form in the gastrointestinal tract when fed to animals, especially with a dietary protein.
