Purification and characterization of a serine protease (CESP) from mature coconut endosperm
2009
Mandal Chhabinath | Roy Samir | Usha Rajamma | Panicker Leelamma M
<p>Abstract</p> <p>Background</p> <p>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 (<it>Cocos nucifera </it>L.) prompted us to search for proteases in the coconut endosperm.</p> <p>Findings</p> <p>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 CESP was often autolysed to two polypeptides of 41.6 kDa (CESP1) and 26.7 kDa (CESP2) and is confirmed by immunochemistry. We have shown the expression of CESP in all varieties of coconut and in all stages of coconut endosperm development with maximum amount in fully matured coconut.</p> <p>Conclusion</p> <p>Since the involvement of proteases in the processing of pre-proteins and maintenance of intracellular protein levels in seeds are well known, we suspect this CESP might play an important role in the coconut endosperm development. However this need to be confirmed using further studies.</p>
Show more [+] Less [-]Bibliographic information
This bibliographic record has been provided by Directory of Open Access Journals