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
收藏
页码：828 / 835
页数：8
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