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无花果蛋白酶的分离纯化及其理化性质研究 被引量:17

A STUDY ON THE SEPERATION AND PURIFICATFICATION OF FIG PROTEOLYTIC ENZYME AND ITS PHYSICAL AND CHEMICAL PROPERTIES
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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.
出处 《江西农业大学学报》 CAS CSCD 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
关键词 无花果 蛋白酶 分离纯化 比活力 理化性质 fig pmteolytic enzyme purification specific activity
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