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首页> 外文期刊>International Journal of Biological Macromolecules: Structure, Function and Interactions >Purification and characterization of a novel tannase produced by Kluyveromyces marxianus using olive pomace as solid support, and its promising role in gallic acid production
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Purification and characterization of a novel tannase produced by Kluyveromyces marxianus using olive pomace as solid support, and its promising role in gallic acid production

机译：用橄榄渣作为固体载体的Kluyveromyce Marxianus生产的新鞣酸序列的纯化与表征，其在加酸生产中的有前途作用

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摘要

Tannase is considered one of the most important industrial enzymes that find great applications in various sectors. Production of tannases through solid state fermentation (SSF) using agro-industrial wastes is an eco-friendly and cheap technology. Tannase was produced by the yeast Kluyveromyces marxianus using olive pomace as a solid support under SSF. It was purified using ammonium sulfate fractional precipitation followed by Sephadex G-200 gel filtration resulting in 64.6% enzyme yield with 1026.12 U/mg specific activity and 24.21 purification fold. Pure tannase had molecular weight of 65 KDa and 66.62 KDa by SDS-PAGE and gel filtration, respectively. It showed a maximal activity at 35 degrees C having two different pH optima, one of which is acidic (4.5) and the other one is alkaline (8.5). The enzyme was stable in the acidic range of pH (4.0-5.5) for 30min, and thermostable within the temperature range 30-70 degrees C. Using tannic acid, the enzyme had a Km value of 0.77 mM and Vmax of 263.20 mu mole min(-1) ml(-1). The effect of different metal ions on enzymatic activity was evaluated. HPLC analysis data indicated that the purified enzyme could carry out 24.65% tannic acid conversion with 5.25 folds increase in gallic acid concentration within 30 min only. (C) 2017 Elsevier B.V. All rights reserved.
机译：鞣酶被认为是最重要的工业酶之一，在各个部门中找到了伟大的应用。通过使用农业工业废物的固态发酵（SSF）生产鞣制品是一种环保和廉价的技术。甘蔗由酵母kluyveromyces Marxianus使用橄榄渣作为SSF的固体载体产生。使用硫酸铵分数沉淀纯化，然后由Sephadex G-200凝胶过滤，得到64.6％的酶产率，1026.12 U / Mg特异性活性和24.21纯化折叠。通过SDS-PAGE和凝胶过滤分子量为65kDa和66.62kDa的分子量。它显示出35摄氏度的最大活性，其具有两种不同的pH值，其中一种是酸性（4.5），另一个是碱性（8.5）。酶在30分钟的酸性pH（4.0-5.5）的酸性范围内稳定，并在温度范围内热稳定在30-70℃下。使用单宁酸，酶的KM值为0.77mm，Vmax为263.20μmmin （-1）ml（-1）。评价不同金属离子对酶活性的影响。 HPLC分析数据表明，纯化的酶可以进行24.65％的单宁酸转化，只有5.25倍的倍数，仅在30分钟内增加了无碱酸浓度。 （c）2017年Elsevier B.V.保留所有权利。

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