Document Detail


Enhanced enzymatic hydrolysis of lignocellulose by optimizing enzyme complexes.
MedLine Citation:
PMID:  19288067     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
To enhance the conversion of the cellulose and hemicellulose, the corncob pretreated by aqueous ammonia soaking was hydrolyzed by enzyme complexes. The saturation limit for cellulase (Spezyme CP) was determined as 15 mg protein/g glucan (50 filter paper unit (FPU)/g glucan). The accessory enzymes (beta-glucosidase, xylanase, and pectinase) were supplemented to hydrolyze cellobiose (cellulase-inhibiting product), hemicellulose, and pectin (the component covering the fiber surfaces), respectively. It was found that beta-glucosidase (Novozyme 188) loading of 1.45 mg protein/g glucan [30 cellobiase units (CBU)/g glucan] was enough to eliminate the cellobiose inhibitor, and 2.9 mg protein/g glucan (60 CBU/g glucan) was the saturation limit. The supplementation of xylanase and pectinase can increase the conversion of cellulose and hemicellulose significantly. The yields of glucose and xylose enhanced with the increasing enzyme loading, but the increasing trend became low at high loading. Compared with xylanase, pectinase was more effective to promote the hydrolysis of cellulose and hemicellulose. The supplementation of pectinase with 0.12 mg protein/g glucan could increase the yields of glucose and xylose by 7.5% and 29.3%, respectively.
Authors:
Mingjia Zhang; Rongxin Su; Wei Qi; Zhimin He
Related Documents :
20371297 - Changes in oxidative enzyme activity during interspecific mycelial interactions involvi...
11996227 - Fenton's reagent-mediated degradation of residual kraft black liquor.
22064917 - Aminobenzoates as building blocks for natural product assembly lines.
23325357 - Structure-based design and analysis of mao-b inhibitors for parkinson's disease: using ...
2709007 - Alterations in protective enzymes against peroxidation in the central and peripheral ne...
1608967 - Crystallization and preliminary x-ray diffraction analysis of p450terp and the hemoprot...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2009-03-14
Journal Detail:
Title:  Applied biochemistry and biotechnology     Volume:  160     ISSN:  1559-0291     ISO Abbreviation:  Appl. Biochem. Biotechnol.     Publication Date:  2010 Mar 
Date Detail:
Created Date:  2010-02-10     Completed Date:  2010-05-03     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8208561     Medline TA:  Appl Biochem Biotechnol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1407-14     Citation Subset:  IM    
Affiliation:
State Key Laboratory of Chemical Engineering, School of Chemical Engineering and Technology, Tianjin University, 92 Weijin Road, Nankai District, Tianjin 300072, China.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Cellobiose / metabolism
Cellulase / metabolism
Endo-1,4-beta Xylanases / metabolism
Enzymes / metabolism*
Glucose / metabolism
Hydrolysis
Lignin / metabolism*
Polygalacturonase / metabolism
Substrate Specificity
Xylose / metabolism
Zea mays / metabolism
beta-Glucosidase / metabolism
Chemical
Reg. No./Substance:
0/Enzymes; 0/Xylose; 11132-73-3/lignocellulose; 16462-44-5/Cellobiose; 50-99-7/Glucose; 9005-53-2/Lignin; EC 3.2.1.15/Polygalacturonase; EC 3.2.1.21/beta-Glucosidase; EC 3.2.1.4/Cellulase; EC 3.2.1.8/Endo-1,4-beta Xylanases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Selective backbone labelling of ILV methyl labelled proteins.
Next Document:  Immobilization of beta-Galactosidase onto Magnetic Beads.