CHARACTERIZATION OF RECOMBINANT CHICKEN AMINOPEPTIDASE H FROM ESCHERICHIA COLI EXPRESSION SYSTEM

来源 :第十四届世界食品科技大会 | 被引量 : 0次 | 上传用户:lqwhappy
下载到本地 , 更方便阅读
声明 : 本文档内容版权归属内容提供方 , 如果您对本文有版权争议 , 可与客服联系进行内容授权或下架
论文部分内容阅读
  Chicken Aminopeptidase H (APH) is an peptidase in the chicken sckeletal muscle,partially in charge of the production of flavor peptides and free amino acids after death stiffening.In this work,the gene of APH from chicken liver was expressed in E coli Rosetta(DE3),and the obtained recombinant APH (rAPH) was charaterized by SDS-PAGE,gel filtration chromatography and enzymatical analysis.The molecular weight of rAPH was found to be 52 KD and 369 KD by SDS-PAGE and gel filtration chromatography,indicating rAPH contains 8 or 7 subunits.
其他文献
会议
Rice dregs(RD),a cheap resource of protein of by-product from rice syrup production,retains nearly all rice protein (RP) being considered hypoallergenic.But 80% its insoluble glutelin and their disulf
会议
会议
会议
Both of Laccase and Manganese Peroxidase from Coriolus Versicolor were co-immobilized by chitosan microspheres in this paper.Firstly,the chitosan microspheres formed condition was investigated.Then,th
会议
会议
会议
It is believed that food allergens are proteins resistant to digestion.Digestibility tests have been accepted as an appropriate method for evaluating the allergenicity of newly introduced proteins.In
会议
The effective utilization of the byproducts during the processing of aquatic products is important to the fisheries industry.So far,very little information about trypsins from byproducts of freshwater
会议
会议