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dc.contributor.authorC.M. Bosire
dc.contributor.authorLaila Abubakar
dc.contributor.authorJames Ochanda
dc.contributor.authorJ.O. Bosire
dc.date.accessioned2015-11-03T08:53:25Z
dc.date.available2015-11-03T08:53:25Z
dc.date.issued2013
dc.identifier.issn2220 - 6655
dc.identifier.urihttp://hdl.handle.net/123456789/5593
dc.descriptionThe original publication is available at http://www.innspub.net/wp-content/uploads/2013/12/IJB-V3No12-p134-144.pdfen_US
dc.description.abstractMarine woodborers have a close association with tropical mangrove plants whereby they voraciously consume lignocellulose and play a role in nutrient cycling. They represent a rich source of potential lignocellulolytic enzymes that can be harnessed for conversion of biomass into simple sugars and other monomers for a variety of uses. Ligninolytic enzymes find applications in bio bleaching of pulp and decolouration of textile dyes, whereas cellulolytic and hemicellulolytic enzymes find applications in animal feed, manufacture of bread, bioethanol production and xylitol production among other uses. In this study, we obtained crude gut extracts from two marine woodborers, Dicyathifer mannii (Wright, 1866) and Sphaeroma terebrans (Bate, 1866), from three sampling sites along the Kenyan coast. Lignocellulolytic activities of the gut extracts were investigated in an effort to seek the species with the most lignocellulolytic efficacious extracts. Ligninolytic activities investigated were lignin peroxidase (LiP), manganese-dependent peroxidase (MnP) and laccase (Lac) or monophenol oxidase. Cellulolytic enzymes investigated were glucanases endoglucanase (endo-1-4-β-D-glucanase), exoglucanase (1,4-β-D-glucan-cellobiohydrolase), and β-D-glucosidase or cellobiase (β-D-glucoside glucanohydrolase). Endo-1-4-β-xylanase was investigated in the hydrolysis of xylan, the chief type of hemicellulose. D. mannii crude extracts showed an appreciable Lip activity of up to 34.65±0.116 U/L and endoglucanase (CMCase) activity of up to 50.7 U/ml (1 U represents the amount of enzyme which catalyzed the transformation of 1 micromol of substrate min-1). D. mannii is implicated as a source of these enzymes for industrial use.en_US
dc.description.sponsorshipTechnical University of Mombasaen_US
dc.language.isoenen_US
dc.publisherInternational Journal of Biosciencesen_US
dc.subjectLignocellulolytic enzymeen_US
dc.subjectgut extracten_US
dc.subjectwoodboreren_US
dc.titleLignocellulolytic activities of crude gut extracts of marine woodborers Dicyathifer mannii and Sphaeroma terebransen_US
dc.typeArticleen_US


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