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BMC Research Notes

, 2:81

First Online: 09 May 2009Received: 18 September 2008Accepted: 09 May 2009DOI: 10.1186-1756-0500-2-81

Cite this article as: Panicker, L.M., Usha, R., Roy, S. et al. BMC Res Notes 2009 2: 81. doi:10.1186-1756-0500-2-81

Abstract

BackgroundIn 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.

FindingsWe 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.

ConclusionSince 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.

List of abbreviations usedBAPNA N∞-Benzoyl DL-arginine p-nitroanilide

TLCK N∞-p-Tosyl-L-Lysine chloromethyl ketone

TPCK N∞-p-Tosyl-L-Phenylalanine chloromethyl ketone

SBTI Soybean trypsin inhibitor.

Electronic supplementary materialThe online version of this article doi:10.1186-1756-0500-2-81 contains supplementary material, which is available to authorized users.

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Autor: Leelamma M Panicker - Rajamma Usha - Samir Roy - Chhabinath Mandal

Fuente: https://link.springer.com/







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