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Gene cloning, expression and biochemical characterization of a glucose- and xylose-stimulated β-glucosidase from Humicola insolens RP86

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    • 바이오플라스틱
      1. 플라스틱
    • 바이오정밀화학
      1. 용매
      2. 화학제품
      3. 연료
      4. 기타
    • 화장품용 기능성소재
      1. 계면활성제⁄증점제
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논문

Gene cloning, expression and biochemical characterization of a glucose- and xylose-stimulated β-glucosidase from Humicola insolens RP86

학술지

Journal of molecular catalysis. B, Enzymatic

저자명

Souza, F.H.M.; Meleiro, L.P.; Machado, C.B.; Zimbardi, A.L.R.L.; Maldonado, R.F.; Souza, T.A.C.B.; Masui, D.C.; Murakami, M.T.; Jorge, J.A.; Ward, R.J.; Furriel, R.P.M.

초록

Efficient cellulose saccharification is crucial for the cost-effective production of ethanol from lignocellulosic biomass. Most &beta;-glucosidases are inhibited by glucose, and high enzyme loads are needed to attain acceptable hydrolysis yields, increasing the process costs. Therefore, glucose-stimulated &beta;-glucosidases with high catalytic efficiency for cellobiose hydrolysis are highly interesting, particularly those produced at low cost using convenient expression systems. The bglhi gene from Humicola insolens RP86, which encodes a glucose- and xylose-stimulated &beta;-glucosidase (Bglhi), was cloned and expressed in E. coli. The recombinant Bglhi was expressed in soluble form and dynamic light scattering showed that the protein was monomeric (56.1kDa). The enzyme showed broad substrate specificity, with optima of pH and temperature of 5.0-7.0 and 60<SUP>o</SUP>C, and was stable from pH 4.5 to 8.0, and for 1h at 50<SUP>o</SUP>C in water. The recombinant Bglhi was highly stimulated by glucose and xylose. About 2-fold stimulation of pNP-glucosidase activity occurred at 50mmolL<SUP>-1</SUP> glucose or 100mmolL<SUP>-1</SUP> xylose. In addition, stimulation was observed over 50-370mmolL<SUP>-1</SUP> glucose or 100-1000mmolL<SUP>-1</SUP> xylose. Xylose maximally stimulated (2.3-fold) the cellobiase activity of the enzyme at 80mmolL<SUP>-1</SUP> concentration. The V<SUB>max</SUB> for cellobiose hydrolysis (183.4+/-12.0Umg<SUP>-1</SUP>) was 5-fold higher than that for pNP-Glc (36.4+/-1.4Umg<SUP>-1</SUP>), but a lower K<SUB>M</SUB> for pNP-Glc (0.20+/-0.01mmolL<SUP>-1</SUP>), compared to cellobiose (0.38+/-0.01mmolL<SUP>-1</SUP>), was estimated. More importantly, the recombinant Bglhi presented the highest catalytic efficiency for cellobiose hydrolysis (k<SUB>cat</SUB>/K<SUB>M</SUB>=453.0+/-29.6s<SUP>-1</SUP>mmol<SUP>-1</SUP>L) among all glucose-stimulated and glucose-tolerant &beta;-glucosidases known to date. Together, these properties indicate that the recombinant Bglhi is an attractive candidate to include in enzymatic cocktails for application in industrial processes for the saccharification of lignocellulosic materials.

발행연도

2014

발행기관

Elsevier

ISSN

1381-1177

ISSN

1873-3158

106

페이지

pp.1-10

주제어

Cellobiase; Humicola insolens; Cellulose saccharification; Cellulosic ethanol; Recombinant β-glucosidase; Product stimulation; Glucose stimulation

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1 2023-12-11
2 2023-12-11

논문; 2014-08-01

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