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The Chemical Modification of Cellulase from Locale Bacteria Isolate Bacillus subtilis ITBCCB148 with Glyoxylic Acid

机译:乙醛酸对局域细菌分离枯草芽孢杆菌ITBCCB148纤维素酶的化学修饰

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摘要

This research aims to increase the stability of cellulase obtained from Bacillus subtilis ITBCCB148 using glyoxylic acid as modifier. To achieve this aim, the research phases performed were production, isolation, purification and chemical modificationon cellulase and were followed by characterization of the purified (native) and modified enzyme to know the stability increase of the enzyme. The result showed that the purified enzyme has optimum pH 6, temperature optimum 60°C; k. = 0,066 min.~(-1); t_(1/2) = 10.50 min.; and AG. = 100.7330 kj/mol, while the modified enzymes with glyoxylic acid with modification degree of 70.54; 78.68; 86.43% have similar optimum pH and temperature with the native enzyme, but the thermal stability of the three modified enzymes were k. = 0.031; 0.033; and 0.037 min.t_(1/2) = 22.35; 21.00; and 18.72 minutes, and AG. = 102.8253; 102.6522; and 102.3354 kj mol '. respectively. The chemical modification has been able to increase the thermal stability of the modified enzymes 1.8 - 2.1 times more than the native one.
机译:这项研究旨在提高使用乙醛酸作为修饰剂的枯草芽孢杆菌ITBCCB148获得的纤维素酶的稳定性。为了达到这个目的,进行的研究阶段是纤维素酶的生产,分离,纯化和化学修饰,然后对纯化的(天然)和修饰的酶进行表征,以了解酶的稳定性。结果表明,纯化后的酶的最适pH值为6,最适温度为60°C; k。 = 0,066分钟〜(-1); t_(1/2)= 10.50分钟;和AG。 = 100.7330kj / mol,而用乙醛酸修饰的酶的修饰度为70.54; 78.68; 86.43%的最佳pH和温度与天然酶相似,但三种修饰酶的热稳定性为k。 = 0.031; 0.033;和0.037分钟t_(1/2)= 22.35; 21.00; 18.72分钟,以及AG。 = 102.8253; 102.6522;和102.3354 kj mol'。分别。化学修饰能够将修饰酶的热稳定性提高到天然酶的1.8-2.1倍。

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