Purification and Characterization of a Thermostable Caseinolytic Serine Protease from the Latex of Euphorbia heterophylla L.

被引：3

作者：

Singh, Sorokhaibam J. ^{[1
]}

Singh, Laishram R. ^{[1
]}

Devi, Sanjenbam K. ^{[1
]}

Singh, Senjam S. ^{[1
]}

Devi, Chingsubam B. ^{[2
]}

Rully, Huidrom ^{[1
]}

机构：

[1] Manipur Univ, Dept Biochem, Lab Prot Biochem, Imphal 795003, Manipur, India

[2] Imphal Coll, Dept Chem, Imphal 795001, Manipur, India

来源：

PROTEIN AND PEPTIDE LETTERS | 2015年 / 22卷 / 09期

关键词：

Euphorbia heterophylla; plant latex; protease; serine protease; CHYMOTRYPSIN; ENZYMES; MEROPS;

D O I：

10.2174/0929866522666150707114548

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A new thermostable caseinolytic serine protease was purified from the latex of Euphorbia heterophylla L. to electrophoretic homogeneity by a procedure involving successive steps of pretreatment of the latex, PEG fractionation, CM-cellulose chromatography and DEAE-cellulose chromatography. The purified protease was found to be a monomeric protein of molecular weight 77.2 kDa. It exhibited caseinolytic activity with hyperbolic azocasein saturation with V-max and K-m values of 0.11 units.mL(-1) and 0.55 mg.mL(-1) respectively. Specific inhibitory studies revealed the enzyme to be a serine protease. The protease was characterized by pH optimum of 8.0 and high thermostability with T-1/2 of 75 degrees C. Based on the results of peptide mass fingerprinting analysis, the protease was shown to be a new protein not characterized earlier.

引用

页码：828 / 835

页数：8

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