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首页> 外文期刊>Applied Microbiology >Processivity and Enzymatic Mode of a Glycoside Hydrolase Family 5 Endoglucanase from Volvariella volvacea
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Processivity and Enzymatic Mode of a Glycoside Hydrolase Family 5 Endoglucanase from Volvariella volvacea

机译：Volvolvella volvacea的糖苷水解酶家族5内切葡聚糖酶的生产能力和酶促模式。

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EG1 is a modular glycoside hydrolase family 5 endoglucanase from Volvariella volvacea consisting of an N-terminal carbohydrate-binding module (CBM1) and a catalytic domain (CD). The ratios of soluble to insoluble reducing sugar produced from filter paper after 8 and 24 h of exposure to EG1 were 6.66 and 8.56, respectively, suggesting that it is a processive endoglucanase. Three derivatives of EG1 containing a core domain only or additional CBMs were constructed in order to evaluate the contribution of the CBM to the processivity and enzymatic mode of EG1 under stationary and agitated conditions. All four enzymatic forms exhibited the same mode of action on both soluble and insoluble cellulosic substrates with cellobiose as a main end product. An additional CBM fused at either the N or C terminus reduced specific activity toward soluble and insoluble celluloses under stationary reaction conditions. Deletion of the CBM significantly decreased enzyme processivity. Insertion of an additional CBM also resulted in a dramatic decrease in processivity in enzyme-substrate reaction mixtures incubated for 0.5 h, but this effect was reversed when reactions were allowed to proceed for longer periods (24 h). Further significant differences were observed in the substrate adsorption/desorption patterns of EG1 and enzyme derivatives equipped with an additional CBM under agitated reaction conditions. An additional family 1 CBM improved EG1 processivity on insoluble cellulose under highly agitated conditions. Our data indicate a strong link between high adsorption levels and low desorption levels in the processivity of EG1 and possibly other processive endoglucanses.
机译：EG1是来自Volvariella volvacea的模块化糖苷水解酶5家族内切葡聚糖酶，由N末端碳水化合物结合模块（CBM1）和催化域（CD）组成。滤纸接触EG1 8和24小时后产生的可溶性还原糖与不溶性还原糖之比分别为6.66和8.56，表明这是一种进行性内切葡聚糖酶。构建了仅包含核心结构域或其他CBM的EG1的三个衍生物，以评估在稳定和搅拌条件下CBM对EG1的合成能力和酶促模式的贡献。以纤维二糖为主要终产物，所有四种酶形式对可溶性和不溶性纤维素底物均表现出相同的作用方式。在固定反应条件下，在N或C末端稠合的其他CBM降低了对可溶性和不溶性纤维素的比活。删除CBM会大大降低酶的合成能力。插入额外的CBM还会导致孵育0.5小时的酶-底物反应混合物的合成能力显着降低，但是当允许反应进行更长的时间（24小时）时，这种作用会逆转。在搅拌的反应条件下，EG1和配备了额外CBM的酶衍生物的底物吸附/解吸模式还观察到了进一步的显着差异。另一族1 CBM在高度搅拌条件下提高了对不溶性纤维素的EG1合成能力。我们的数据表明，EG1和其他可能的内生葡聚糖的合成能力在高吸附水平和低解吸水平之间有很强的联系。

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