无花果蛋白酶的分离纯化及其理化性质研究  

A STUDY ON THE SEPERATION AND PURIFICATFICATION OF FIG PROTEOLYTIC ENZYME AND ITS PHYSICAL AND CHEMICAL PROPERTIES

作　　者：邱业先[1] 刘勇[1] 周群[1] 陈金印[1] 李钟渤[1] 罗来水[1] 

机构地区：[1]江西农业大学林学院,江西农业大学农学院,江西农业联合开发总公司

出　　处：《江西农业大学学报》1996年第1期46-50,共5页Acta Agriculturae Universitatis Jiangxiensis

基　　金：江西省科委"八.五"重点攻关课题

摘　　要：以无花果良种布兰瑞克和紫果１号为材料，其匀浆滤汁经有机溶剂沉淀、超滤等方法处理。得到无花果蛋白酶粉。酶比活力为１５．３４ｕ／ｍｇ·ｐｒｏｔｅｉｎ，纯化倍数为１１．６８％，酶产率为１．５％，酶活力回收率为２７．４％，酶最适ｐＨ为８．０，在ｐＨ５～１０范围内处理０．５ｈ活性稳定，酶最适温度为４０℃，在温度５０℃以内活性稳定。酶具有琉基蛋白酶特性，能被半胱氨酸和ＥＤＴＡ激活，而被ＨｇＣｌ２抑制。Uaing fine figs-Buran Ruiki and purple-fruit-1 as the material,treating its scattered pulp and filtered juice through preipitation in organic solvent,ultra-filtration,etc,we got the powder of fig proteolyfic enzyme.Its specific activity was 15.34 u/mg,protein,its purifioat-ion ploidy reached 11.68 percent.The nate of enzyme production was 1.5 percent,and therecovery ratio of enzytne activity was 27.4 percent.The enzyme exhibited stable activity atpH5～10 for haif an hour with the optimum pH of 8.0.It had stable activity at the tempera-ture below 50℃with the optimum of 40℃.The enzyme had the properties of lnercapto-proteinase.It could be activated by cysteine and EDTA,but inactivated by Hgcl2.

关 键 词：无花果 蛋白酶 分离纯化 比活力 理化性质 

分 类 号：S663.301[农业科学—果树学]