Lignocellulolytic Activities Of Crude Gut Extracts Of Marine Woodborers Dicyathifer Mannii And Sphaeroma Terebrans
Abubakar, L aila
Bosire, J O
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Marine woodborers have a close association with tropical mangrove plants whereby they voraciously consume lignocellulose and play a role in nutrient cycling. T hey represent a rich source of potential lignocellulo lytic 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 hemicellu lolytic 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 inv estigated were lignin peroxidase (LiP), manganese - dependent peroxidase (MnP) and laccase (Lac) or monophenol oxidase. Cellulolytic enzymes investigated were gluc anases endoglucanase (endo - 1 - 4 - β - D - glucanase), exoglucanase (1,4 - β - D - glucan - cellobiohydrolase), and β - D - gl ucosidase or cellobiase ( β - D - glucosid e 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. 1 16 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 sourc e of these enzymes for industrial use.
CitationAbubakar, L. U., Bulimo, W. D., Mulaa, F. J., & Osir, E. O. (2006). Molecular characterization of a tsetse fly midgut proteolytic lectin that mediates differentiation of African trypanosomes. Insect biochemistry and molecular biology, 36(4), 344-352.
University of Nairobi