Please use this identifier to cite or link to this item: http://hdl.handle.net/123456789/385
Title: Lignocellulolytic activities of crude gut extracts of marme woodborers Dicyathifer msnnii and Sphaeroma terebrans
Authors: Bosire, C.
Abubakar, L.
Ochanda, J.
Bosire, J.
Keywords: Lignocellulolytic enzyme
gut extract
woodborer
Issue Date: 2013
Publisher: Innspub
Series/Report no.: International Journal of Biosciences;Vol. 3, No. 12, p. 134-144
Abstract: Marine woodborers have a close association with tropical mangrove plants whereby they voraciously consume lignocellulose and playa 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 endoglucanaS! (endo-i-q-f-Dvglucanase), exoglucanase (l,4-P-D-glucan-cellobiohydrolase), and P-D-glucosidase or cellobiase (P-D-glucoside •• glucanohydrolase). Endo-r-q-B-xylanase was i1l.vestigated in the hydrolysis of xylan, the chief type of hemicellulose. D. mtiiinii: C!'tudeextracts showed an appreciable .Lip activity of up to 34.65±O.1l6 U/L and endoglucanase (CMCase) activity of up to 50.7 U/rnl (1U represents the amount of enzyme which catalyzed thtransformation of 1 micromol of substrate min"). D. mannii is implicated as a so~urce of these enzymes fc. industrial use
URI: http://hdl.handle.net/123456789/385
ISSN: 2222-5234
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