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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2022.12
- 수록면
- 184 - 189 (6page)
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β-Glucosidase producing microorganism was isolated from Doenjang due to its ability of forming black zone on esculin MRS agar plate containing esculin with ferric ammonium citrate. In the analysis of 16S rRNA gene sequence, this strain showed 99% of identity with Leuconostoc mesenteroides (GenBank OK513090.1). A recombinant β- glucosidase from L. mesenteroides was cloned and expressed in Escherichia coli BL21, and the enzyme was purified as a soluble protein with a 14-fold of purification and a final yield of 15%. The recombinant β-glucosidase was determined tobe a homodimer by analyses of SDS-PAGE and gel-filtration chromatography. Optimum pH and temperature of β-glucosidase from L. mesenteroides was pH 6.0 and 40oC, respectively. At the optimum temperature of 40oC, the residual enzyme activity decreased to 50% in only 30 min. Nevertheless, it showed a high thermal stability with a half-life of 4 h at 35oC, where a relative activity of 85% was shown. In the substrate specificity study, specific activity was the highest for pNP-β-D-glucopyranoside, and the enzyme showed hydrolytic activity for substrates such as pNP-β-D-fucopyranoside, pNP-β-D-galactopyranoside, oNP-β-D-glucopyranoside, oNP-β-D-galactopyranoside, pNP-α-L-arabinopyranoside, pNP-β- D-xylopyranoside, and oNP-β-D-xylopyranoside. On the other hand, the enzyme showed no activity for pNP-α-D glucopyranoside, pNP-α-D-galactopyranoside, pNP-α-L-arabinofuranoside. β-Glucosidase from L. mesenteroides had a higher hydrolytic activity on β-1,4 glycosidic linkage than on β-1,2 linkage.
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