食品科学2012，Vol.33Issue(7)：163-167,5.
毛霉亮氨酸氨肽酶的纯化及性质研究
Purification and Characterization of Leucine Aminopeptidase from Mucor
摘要
Abstract
An aminopeptidase was purified and characterized from crude extracellular protease extract from wheat bran koji of Mucor through ammonium sulfate precipitation, ion exchange chromatography, hydrophobic chromatography, gel filtration chromatography and ultra-filtration. The purified aminopeptidase was identified as leucine aminopeptidase, which was very active in hydrolyzing N-terminal leucine of peptides. Its maximum activity was observed at pH 6.5 and 40 ℃. In addition, the leucine aminopeptidase was stable in the pH range of 5.0-8.0 and at temperatures below 40 ℃. However, it could be completely inhibited by the metal protease inhibitor EDTA, indicating that it belongs to the metal protease family. Ca^2＋ had an activating effect on it, while Zn^2＋, Cu^2＋ and Mn^2＋ were very active in inhibiting it. The enzyme was effective in removing bitter taste from soybean ploypeptides and basic elimination of bitter taste was achieved after 4 h of treatment with it.关键词
毛霉/亮氨酸氨肽酶/纯化/性质/脱苦Key words
Mucor/leucine aminopeptidase/purification/properties/debittering分类
生物科学引用本文复制引用
潘进权..毛霉亮氨酸氨肽酶的纯化及性质研究[J].食品科学,2012,33(7):163-167,5.基金项目
广东省自然科学基金项目 （）
湛江师范学院基金项目 （）
