摘要
目的从牡蛎蛋白质的酶解物中分离制备活性肽并对其理化性质进行初步研究。方法采用胰蛋白酶对牡蛎蛋白质进行酶解,使其释放出具备特殊活性的活性肽,将含有活性肽的粗提物分别用Sephadex G25凝胶柱层析,DEAE-Sepharose FF离子交换柱层析和C18反相柱进行分离和纯化。结果牡蛎活性肽粗提物经过分离纯化制备出3个组分F31,F32,F41。组分F32,F41的等电点分别是7.12和7.08;组分F31,F32,F41的相对分子质量分别为885,810及409;其蛋白含量分别为51.9%,80.2%及99.8%;其糖含量分别为19.2%,4.3%及0%。结论以胰蛋白酶作用的最佳条件采用一步酶解的工艺,牡蛎蛋白质可以得到良好的酶解,同时得到的牡蛎活性肽粗提物活性较高。
Objective To study the preparation and the physicochemical characteristics of bioactire peptides from the oyster. Methods The oyster protein was hydrolyzed with trypsin. Hydrolysates were purified using Sephadex G25 gel chromatography, DEAE-Sepharose FF ion exchange chromatography, reversed-phase HPLC on C18 column. Results Three peptides F31,F32,F41 were finally isolated from the oyster hydrolysates . The pI values of F32 and F41 were 7.12,7.08, respectively ; the molecular weights of F31, F32, F41 were 885,810 and 409; the protein contents of F31,F32,F41 were 51.9%,80.2% and 99.8%;the saccharide contents of F31,F32, F41 were 19.2 %, 4.3 % and 0 %, respectively. Conclusion The oyster protein was hydrolyzed better in the optimum condition of trypsin one-step technology, and the bioactivity of the oyster hvdrolvsates obtained by this way was high.
出处
《中国海洋药物》
CAS
CSCD
2006年第2期22-25,共4页
Chinese Journal of Marine Drugs
基金
山东省科技攻关计划项目(021100102)
关键词
太平洋牡蛎
活性肽
酶解
理化性质
Crassostrea gigas Thunberg
bioactive peptides
hydrolysis
physicochemical characteristics
