| Purification and Partial Characterization of β-Glucosidase from Fresh Leaves of Tea Plants （Camellia sinensis （L.） O. Kuntze） |
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| 作者姓名： | Li YY Jiang CJ Wan XC Zhang ZZ Li DX |
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| 作者单位： | KeyLaboratoryofTeaBiochemistryandBiotechnology,MinistryofEducation,AnhuiAgriculturalUniversity,Hefei230036,China |
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| 基金项目： | This work was supported by grants from the Key Natural Science Research Program of the Department of Education of Anhui Province(No.2004kj137zd),the Key Program of Science and Technique Research of the Ministry of Education of China(No.00182) |
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| 摘 要： | β-Glucosidases are important in the formation of floral tea aroma and the development of resistance to pathogens and herbivores in tea plants. A novel β-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℃ and was stable at temperatures lower than 40℃. 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.
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| 关 键 词： | β-葡糖苷酶 茶树 叶片 分离 提纯 理化性质 Camellia sinensis |
Purification and partial characterization of beta-glucosidase from fresh leaves of tea plants (Camellia sinensis (L.) O. Kuntze) |
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| Li YY,Jiang CJ,Wan XC,Zhang ZZ,Li DX.Purification and partial characterization of beta-glucosidase from fresh leaves of tea plants (Camellia sinensis (L.) O. Kuntze)[J].Acta Biochimica et Biophysica Sinica,2005,37(6):363-370. |
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| Authors: | Li Ye-Yun Jiang Chang-Jun Wan Xiao-Chun Zhang Zheng-Zhu Li Da-Xiang |
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| Institution: | Key Laboratory of Tea Biochemistry and Biotechnology, Ministry of Education, Anhui Agricultural University, Hefei 230036, China. |
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| 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. |
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| Keywords: | Camellia sinensis β-glucosidase purification characterization |
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