食品与发酵工业2011，Vol.37Issue(4)：26-31,6.
毛霉AS3.2778脯氨酸氨肽酶的部分纯化及性质研究
Partial Purification and Properties of One Prolyl-aminopeptidase from Mucor AS3.2778
摘要
Abstract
Proteases from Mucor had a good application prospect in the production of soy-polypeptides for their high hydrolysis efficiency to soy protein and debittering effect to hydrolysate.To explore these proteases, this study used ammonium sulfate precipitation, ion exchange chromatography, hydrophobic chromatography and gel filtration chromatography, and investigated the properties of one aminopeptidase purified from the fermented wheat bran by Actinomucor elegans AS3.2778.The purified aminopeptidase was a particular prolyl-aminopeptidase, which had a very high hydrolysis activity to N-terminal proline of peptides.It had the maximum activity at pH6.5 40 ～ 45 ℃, was stable in the pH range of 5.0 ～ 8.0 at ＜ 30℃, and could be inhibited by the serine protease inhibitor, PMSF, indicated that it may belong to the serine protease family.The effect of debittering for bitter peptides among SPI hydrolysate with Alcalase was clearly found by proly-aminopeptidase treatment for 3 h.关键词
雅致放射毛霉/脯氨酸氨肽酶/纯化/性质.脱苦Key words
Actinomucor elegans/ prolyl-aminopeptidase/ purification/ properties/ debittering引用本文复制引用
潘进权..毛霉AS3.2778脯氨酸氨肽酶的部分纯化及性质研究[J].食品与发酵工业,2011,37(4):26-31,6.基金项目
广东省自然科学基金项目(9452404801001943) （9452404801001943）
湛江师范学院基金项目(ZL0912) （ZL0912）
