KMID : 1094720200250010104
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Biotechnology and Bioprocess Engineering 2020 Volume.25 No. 1 p.104 ~ p.116
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Endoglucanase Produced by Bacillus subtilis Strain CBS31: Biochemical Characterization, Thermodynamic Study, Enzymatic Hydrolysis, and Bio-industrial Applications
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Regmi Sudip
Choi Yoon-Seok Kim Young-Kyun Khan Md Maruf Lee Sang-Hun Cho Seung-Sik Jin Ying-Yu Lee Dae-Young Yoo Jin-Cheol Suh Joo-Won
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Abstract
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Microbial cellulases have become the mainstream biocatalysts due to their complex nature and widespread industrial applications. Here, homogeneous endoglucanase GluCB31 from Bacillus subtilis subsp. inaquosorum CBS31 was studied. GluCB31 was purified to 17.68-fold with an 8.33% yield and a specific activity of 1066.37 U/mg. Biochemical properties of GluCB31 were performed and the results are as follows; molecular mass of 35 kDa with an optimum pH at 7.5 and temperature at 50¡ÆC. GluCB31 was immobilized in calcium alginate gel and it exhibited the highest activity at 10¡ÆC higher temperature than soluble enzyme, as the entrapment in alginate gel made GluCB31 more stable. Kinetic studies showed the Vmax of 1293.33 ¡¾ 2.51 U/mg and Km of 0.0183 mg/mL. Enzymatic activity was activated by Tween-20 (106.7%), Tween-80 (111.6%), Triton X-100 (142.3%), SDS (135.5%), Mg++ (185.7%), Cu++ (167.6%), Zn++ (153.7%), Mn++ (106.3%), Ba++ (181.9%), Ni++ (107.2%) while inhibited by Fe++ (15.8%), ¥â-mercaptoethanol (46.8%), EDTA (54.5%). Enthalpy, free energy, and entropy of activation were calculated to be 38.526 kJmol-1, 44.187 kJmol-1, and -17.518 Jmol-1K-1 respectively. Also, ¥ÄGE-S and ¥ÄGE-T were found to be -10.75 kJmol-1 and -45.92 kJmol-1 respectively. A low ¥ÄS, ¥ÄGE-S, and ¥ÄGE-T values were signified enzyme-catalyzed reaction occurs at a fast rate and the existence of the enzyme in its stable state. Cellobiose was the major end product of hydrolysis. These attributes of GluCB31 demonstrated the diversity of catalytic activities and serve in various biotechnological processes, thus deserve to be developed as a bio-industrial agent.
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KEYWORD
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endoglucanase, thermodynamic, bio-industrial, enzymatic hydrolysis
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