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Production and Characterization of Multi-Polysaccharide Degrading Enzymes from Aspergillus aculeatus BCC199 for Saccharification of Agricultural Residues
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  • Production and Characterization of Multi-Polysaccharide Degrading Enzymes from Aspergillus aculeatus BCC199 for Saccharification of Agricultural Residues
  • Production and Characterization of Multi-Polysaccharide Degrading Enzymes from Aspergillus aculeatus BCC199 for Saccharification of Agricultural Residues
저자명
Suwannarangsee. Surisa,Arnthong. Jantima,Eurwilaichitr. Lily,Champreda. Verawat
간행물명
Journal of microbiology and biotechnology
권/호정보
2014년|24권 10호|pp.1427-1437 (11 pages)
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한국미생물생명공학회
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정기간행물|ENG|
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이 논문은 한국과학기술정보연구원과 논문 연계를 통해 무료로 제공되는 원문입니다.
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기타언어초록

Enzymatic hydrolysis of lignocellulosic biomass into fermentable sugars is a key step in the conversion of agricultural by-products to biofuels and value-added chemicals. Utilization of a robust microorganism for on-site production of biomass-degrading enzymes has gained increasing interest as an economical approach for supplying enzymes to biorefinery processes. In this study, production of multi-polysaccharide-degrading enzymes from Aspergillus aculeatus BCC199 by solid-state fermentation was improved through the statistical design approach. Among the operational parameters, yeast extract and soybean meal as well as the nonionic surfactant Tween 20 and initial pH were found as key parameters for maximizing production of cellulolytic and hemicellulolytic enzymes. Under the optimized condition, the production of FPase, endoglucanase, ${eta}$-glucosidase, xylanase, and ${eta}$-xylosidase was achieved at 23, 663, 88, 1,633, and 90 units/g of dry substrate, respectively. The multi-enzyme extract was highly efficient in the saccharification of alkaline-pretreated rice straw, corn cob, and corn stover. In comparison with commercial cellulase preparations, the BCC199 enzyme mixture was able to produce remarkable yields of glucose and xylose, as it contained higher relative activities of ${eta}$-glucosidase and core hemicellulases (xylanase and ${eta}$-xylosidase). These results suggested that the crude enzyme extract from A. aculeatus BCC199 possesses balanced cellulolytic and xylanolytic activities required for the efficient saccharification of lignocellulosic biomass feedstocks, and supplementation of external ${eta}$-glucosidase or xylanase was dispensable. The work thus demonstrates the high potential of A. aculeatus BCC199 as a promising producer of lignocellulose-degrading enzymes for the biomass conversion industry.