Purification and characterization of a serine protease (CESP) from mature coconut endosperm.

ABSTRACT:

Background

In plants, proteases execute an important role in the overall process of protein turnover during seed development, germination and senescence. The limited knowledge on the proteolytic machinery that operates during seed development in coconut (Cocos nucifera L.) prompted us to search for proteases in the coconut endosperm.

Findings

We have identified and purified a coconut endosperm protease (CESP) to apparent homogeneity. CESP is a single polypeptide enzyme of approximate molecular mass of 68 kDa and possesses pH optimum of 8.5 for the hydrolysis of BAPNA. Studies relating to substrate specificity and pattern of inhibition by various protease inhibitors indicated that CESP is a serine protease with cleavage specificity to peptide bonds after arginine. Purified CE

SUBMITTER: Panicker LM 

PROVIDER: S-EPMC2689245 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature