Addition of expansin to cellulase enhanced bioethanol production
메타 데이터
바이오화학분류
바이오플라스틱
플라스틱
바이오정밀화학
용매
화학제품
연료
화장품용 기능성소재
계면활성제⁄증점제
의료용 화학소재
식품첨가제
논문
Addition of expansin to cellulase enhanced bioethanol production
학술지
Process biochemistry
저자명
Kumar, M.; Singh, P.; Sukla, L.B.
초록
A metagenomic clone (pUC-189) that exhibited clear zone on CMC agar plate showed homology with glycosyl hydrolase (GH) family 12 endoglucanase. Purified recombinant cellulase (C18) exhibited the highest activity towards CMC followed by Avicel PH101 and waste paper which was confirmed by chromatography. Role of expansin (E11CB) was investigated to address the poor activity of C18 towards waste paper. The Langmuir isotherm for binding of the purified E11CB to waste paper showed a good fit (R<SUP>2</SUP>=0.97). Recombinant E11CB protein bound to waste paper was detected in situ by UV fluorescence of [Ln(DPA)<SUB>3</SUB>]<SUP>3-</SUP> complex. Scanning electron microscopy confirmed that binding of E11CB transformed smooth microfibrils into rough and amorphic surface. Improvement in the enzymatic hydrolysis of pure cellulose and lignocelluloses was observed after treatment with purified E11CB at low cellulase loading. The enzymatic hydrolysate of waste cellulose paper was then used as the substrate for bioethanol production by Saccharomyces cerevisiae.