Purification and partial characterization of beta-glucosidase from fresh leaves of tea plants (Camellia sinensis (L.) O. Kuntze).

Abstract:

:beta-Glucosidases are important in the formation of floral tea aroma and the development of resistance to pathogens and herbivores in tea plants. A novel beta-glucosidase was purified 117-fold to homogeneity, with a yield of 1.26%, from tea leaves by chilled acetone and ammonium sulfate precipitation, ion exchange chromatography (CM-Sephadex C-50) and fast protein liquid chromatography (FPLC; Superdex 75, Resource S). The enzyme was a monomeric protein with specific activity of 2.57 U/mg. The molecular mass of the enzyme was estimated to be about 41 kDa and 34 kDa by SDS-PAGE and FPLC gel filtration on Superdex 200, respectively. The enzyme showed optimum activity at 50 deg;C and was stable at temperatures lower than 40 degrees C. It was active between pH 4.0 and pH 7.0, with an optimum activity at pH 5.5, and was fairly stable from pH 4.5 to pH 8.0. The enzyme showed maximum activity towards pNPG, low activity towards pNP-Galacto, and no activity towards pNP-Xylo.

authors

Li YY,Jiang CJ,Wan XC,Zhang ZZ,Li DX

doi

10.1111/j.1745-7270.2005.00053.x

subject

Has Abstract

pub_date

2005-06-01 00:00:00

pages

363-70

issue

6

eissn

1672-9145

issn

1745-7270

journal_volume

37

pub_type

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