Please use this identifier to cite or link to this item: http://hdl.handle.net/1822/37151

TitleCelluclast and Cellic® CTec2: Saccharification / fermentation of wheat straw, solid-liquid partition and potential of enzyme recycling by alkaline washing
Author(s)Rodrigues, Ana Cristina Costa
Haven, Mai Østergaard
Lindedam, Jane
Felby, Claus
Gama, F. M.
KeywordsCellulases
Enzyme activity stability
Adsorption/Desorption
Enzyme recycling
Issue dateNov-2015
PublisherElsevier B.V.
JournalEnzyme and Microbial Technology
CitationRodrigues, A.; Haven, Mai Østergaard; Lindedam, Jane; Felby, Claus; Gama, F. M., Celluclast and Cellic® CTec2: Saccharification / fermentation of wheat straw, solid-liquid partition and potential of enzyme recycling by alkaline washing. Enzyme and Microbial Technology, 79-80, 70-77, 2015
Abstract(s)The hydrolysis/fermentation of wheat straw and the adsorption/desorption/deactivation of cellulases were studied using Cellic® CTec2 (Cellic) and Celluclast mixed with Novozyme 188. The distribution of enzymes cellobiohydrolase I (Cel7A), endoglucanase I (Cel7B) and -glucosidase of the two formulations between the residual substrate and supernatant during the course of enzymatic hydrolysis and fermentation was investigated. The potential of recyclability using alkaline wash was also studied. The efficiency of hydrolysis with an enzyme load of 10 FPU/g cellulose reached >98 % using Cellic® CTec2, while for Celluclast a conversion of 52 % and 81 %, was observed without and with -glucosidase supplementation, respectively. The decrease of Cellic® CTec2 activity observed along the process was related to deactivation of Cel7A rather than of Cel7B and -glucosidase. The adsorption/desorption profiles during hydrolysis/fermentation revealed that a large fraction of active enzymes remained adsorbed to the solid residue throughout the process. Surprisingly, this was the case of Cel7A and -glucosidase from Cellic, which remained adsorbed to the solid fraction along the entire process. Alkaline washing was used to recover the enzymes from the solid residue. This method allowed efficient recovery of Celluclast enzymes; however, this may be achieved only when minor amounts of cellulose remain present. Regarding the Cellic formulation, neither the presence of cellulose nor lignin restricted an efficient desorption of the enzymes at alkaline pH. This work shows that the recycling strategy must be customized for each particular formulation, since the enzymes found e.g.in Cellic and Celluclast bear quite different behaviour regarding the solid-liquid distribution, stability and cellulose and lignin affinity.
TypeArticle
URIhttp://hdl.handle.net/1822/37151
DOI10.1016/j.enzmictec.2015.06.019
ISSN0141-0229
e-ISSN0141-0229
Publisher versionhttp://www.sciencedirect.com/science/article/pii/S0141022915300211
Peer-Reviewedyes
AccessOpen access
Appears in Collections:CEB - Publicações em Revistas/Séries Internacionais / Publications in International Journals/Series

Files in This Item:
File Description SizeFormat 
document_22253_1.pdf1,78 MBAdobe PDFView/Open

Partilhe no FacebookPartilhe no TwitterPartilhe no DeliciousPartilhe no LinkedInPartilhe no DiggAdicionar ao Google BookmarksPartilhe no MySpacePartilhe no Orkut
Exporte no formato BibTex mendeley Exporte no formato Endnote Adicione ao seu ORCID