Purification and characterisation of processive-type endoglucanase and β-glucosidase from Aspergillus ochraceus MTCC 1810 through saccharification of delignified coir pith to glucose
메타 데이터
바이오화학분류
바이오플라스틱
기타
바이오정밀화학
기타
화장품용 기능성소재
기타
의료용 화학소재
식품첨가제
논문
Purification and characterisation of processive-type endoglucanase and β-glucosidase from Aspergillus ochraceus MTCC 1810 through saccharification of delignified coir pith to glucose
<P><B>Abstract</B></P> <P>The study describes purification and characterisation of processive-type endoglucanase and β-glucosidase from <I>Aspergillus ochraceus</I> MTCC 1810 through bioconversion of delignified coir pith to fermentable glucose. The purified processive endoglucanase (AS-HT-Celuz A) and β-glucosidase (AS-HT-Celuz B) were found to have molecular mass of ≈78-kDa and 43-kDa respectively with optimum endoglucanase (35.63U/ml), total cellulase (28.15FPU/ml) and β-glucosidase (15.19U/ml) activities at 40°C/pH 6. The unique feature of AS-HT-Celuz A is the multiple substrate specificity and processivity towards both amorphous and crystalline cellulose. Zymogram indicated both endo and exoglucanase activities residing in different binding sites of a single protein exhibiting sequential synergy with its own β-glucosidase. Accordingly, the identified enzymes could be implemented as synergistic cellulases for complete cellulose saccharification which still considered an unresolved issue in bio-refineries.</P> <P><B>Highlights</B></P> <P> <UL> <LI> Purification of a new processive-type endoglucanase and β-glucosidase from <I>A. ochraceus.</I> </LI> <LI> Cellulases displayed multiple-substrate specificity, processivity and sequential synergy. </LI> <LI> Offers a novel and cost effective bioprocess for bioconversion of delignified coir pith to glucose. </LI> </UL> </P>