Purification and characterization of β-amylase from Curculigo pilosa View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1999-11

AUTHORS

M. H. Dicko, M. J. F. Searle-van Leeuwen, G. Beldman, O. G. Ouedraogo, R. Hilhorst, A. S. Traoré

ABSTRACT

Curculigo pilosa is traditionally used in the manufacture of sorghum beer in West Africa. β-Amylase was purified 100-fold with 38% yield from a crude extract, giving final specific activities of 4850 U/mg and 5650 U/mg using soluble starch and p-nitrophenyl maltopentaoside, respectively, as substrates. The molecular mass of the monomeric enzyme was 64 kDa and its pI 4.2. Both activity and thermostability are higher than reported for other plant β-amylases. The catalytic efficiency was lower for amylose than for starches and amylopectin. In contrast to other plant amylases, the β-amylase from C. pilosa is able to degrade raw starches from wheat, corn, potato and rice. In this respect, it resembles β-amylases from microbial origin. This property, and its high activity and stability, explain its traditional use in the manufacture of infant food and sorghum beer in Burkina Faso and could make it applicable for other biotechnological purposes. More... »

PAGES

802-805

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s002530051595

DOI

http://dx.doi.org/10.1007/s002530051595

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1019793171


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