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Utility of Enzymes from Fibrobacter Succinogenes and Prevotella Ruminicola As Detergent Additives

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Specialty Biotechnology
Date 2008 May 9
PMID 18463911
Citations 5
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Abstract

In this study, we investigated the application of cellulase and protease purified from rumen bacteria as detergent additives. Cellulase and protease were purified from the rumen cellulytic bacteria Fibrobacter succinogenes S85, and Prevotella ruminicola 23, respectively. An inhibitor test indicated that the purified protease belongs to the category of serine proteases and metalloproteases. Both the enzymes were effective at a high temperature (50 degrees C) and neutral pH (pH 7-8), but the protease activity increased with the increase in temperature and pH. The purified protease was treated with ten types of surfactants/detergents; it was found to retain over 60% of its activity in the presence of anionic and nonionic detergents. The cellulose plus protease combination was still effective after treatment with Triton X-100 and Tween 80, but the residual activity was low after treatment with Tween 20 than that after treatment with other nonionic detergents. Washing tests indicated that enzyme addition produced no significant improvement in the removal of grass stains, but individual enzyme addition in surfactants/detergents, especially in nonionic detergents, could improve the washing performance of the detergents by improving its ability to remove blood stains. This suggested that the surfactant/detergent class, enzyme properties, and the mixing ratio of ingredients should be considered simultaneously to enhance the washing performance.

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References
1.
Mawadza C, Hatti-Kaul R, Zvauya R, Mattiasson B . Purification and characterization of cellulases produced by two Bacillus strains. J Biotechnol. 2000; 83(3):177-87. DOI: 10.1016/s0168-1656(00)00305-9. View

2.
McGavin M, Forsberg C . Isolation and characterization of endoglucanases 1 and 2 from Bacteroides succinogenes S85. J Bacteriol. 1988; 170(7):2914-22. PMC: 211229. DOI: 10.1128/jb.170.7.2914-2922.1988. View

3.
Laemmli U . Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970; 227(5259):680-5. DOI: 10.1038/227680a0. View

4.
Maurer K . Detergent proteases. Curr Opin Biotechnol. 2004; 15(4):330-4. DOI: 10.1016/j.copbio.2004.06.005. View

5.
Bradford M . A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976; 72:248-54. DOI: 10.1016/0003-2697(76)90527-3. View