Journal of Applied Glycoscience
Online ISSN : 1880-7291
Print ISSN : 1344-7882
ISSN-L : 1344-7882
Notes
Purification and Characterization of Alkali-stable β-Amylase from Chinese Yam (Nagaimo) Tuber
Yogo ChibaTakahiro Kuwashima
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2006 Volume 53 Issue 4 Pages 273-275

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Abstract

An alkali-stable β-amylase was purified from Nagaimo, a cultivar of yam (Dioscorea opposita Thunb.) by hexadecyltrimethylammonium bromide treatment, ammonium sulfate fractionation, and two-step column chromatographic procedures on α-CD-Sepharose CL-4B and DEAE-Sephacel. Analysis by SDS-PAGE revealed the enzyme to be a monomeric protein with a 56 kDa molecular mass. This enzyme was stable for pH 4.0-12.0 at 4°C for 24 h. During two months, its activity remained about 40% at pH 9.5, but it fell below 20% at pH 5.0. Other properties such as optimum pH (5.6), and molecular mass resembled those of previously reported β-amylases. Thermal stability of this enzyme was not very high, either. From these results, this enzyme appears to be a good model for studying β-amylase stability.

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© 2006 by The Japanese Society of Applied Glycoscience
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