Heterologous Expression of a Thermostable α-Galactosidase from Parageobacillus thermoglucosidasius Isolated from the Lignocellulolytic Microbial Consortium TMC7

Wang Yi; Wang Chen; Chen Yonglun; Cui MingYu; Wang Qiong; Guo Peng

doi:10.4014/jmb.2201.01022

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자료유형: 학술저널

저자정보: Wang Yi (Institute of Agricultural Products Processing and Nuclear Agriculture Technology Research Hubei Aca) Wang Chen (Institute of Agricultural Products Processing and Nuclear Agriculture Technology Research Hubei Aca) Chen Yonglun (Institute of Agricultural Products Processing and Nuclear Agriculture Technology Research Hubei Aca) Cui MingYu (Institute of Agricultural Products Processing and Nuclear Agriculture Technology Research Hubei Aca) Wang Qiong (Institute of Agricultural Products Processing and Nuclear Agriculture Technology Research Hubei Aca) Guo Peng (Institute of Agricultural Products Processing and Nuclear Agriculture Technology Research Hubei Aca)

저널정보: 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제32권 제6호

발행연도: 2022.6

수록면: 749 - 760 (12page)

DOI: 10.4014/jmb.2201.01022

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α-Galactosidase is a debranching enzyme widely used in the food, feed, paper, and pharmaceuticals industries and plays an important role in hemicellulose degradation. Here, T26, an aerobic bacterial strain with thermostable α-galactosidase activity, was isolated from laboratory-preserved lignocellulolytic microbial consortium TMC7, and identified as Parageobacillus thermoglucosidasius. The α-galactosidase, called T26GAL and derived from the T26 culture supernatant, exhibited a maximum enzyme activity of 0.4976 IU/ml when cultured at 60oC and 180 rpm for 2 days. Bioinformatics analysis revealed that the α-galactosidase T26GAL belongs to the GH36 family. Subsequently, the pET-26 vector was used for the heterologous expression of the T26 α-galactosidase gene in Escherichia coli BL21 (DE3). The optimum pH for α-galactosidase T26GAL was determined to be 8.0, while the optimum temperature was 60oC. In addition, T26GAL demonstrated a remarkable thermostability with more than 93% enzyme activity, even at a high temperature of 90oC. Furthermore, Ca2+ and Mg2+ promoted the activity of T26GAL while Zn2+ and Cu2+ inhibited it. The substrate specificity studies revealed that T26GAL efficiently degraded raffinose, stachyose, and guar gum, but not locust bean gum. This study thus facilitated the discovery of an effective heatresistant α-galactosidase with potent industrial application. Meanwhile, as part of our research on lignocellulose degradation by a microbial consortium, the present work provides an important basis for encouraging further investigation into this enzyme complex.

#α-Galactosidase #thermophilic enzyme #enzymatic properties #GH36 #heterologous expression

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Wang Yi

소속기관 Department of Biosystems Engineering Auburn University Auburn Alabama Alabama 36849 USA

주요연구분야 자연과학 > 생물학

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Wang Chen