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Enzyme Research
Volume 2017, Article ID 7686904, 7 pages
Research Article

Characterization of Pectinase from Bacillus subtilis Strain Btk 27 and Its Potential Application in Removal of Mucilage from Coffee Beans

1Department of Biology, Ambo University, P.O. Box 19, Ambo, Ethiopia
2College of Natural Science, Addis Ababa University, P.O. Box 1176, Addis Ababa, Ethiopia

Correspondence should be addressed to Oliyad Jeilu Oumer; te.ude.uobma@uliej.dayilo

Received 10 May 2017; Accepted 6 August 2017; Published 11 September 2017

Academic Editor: Toshihisa Ohshima

Copyright © 2017 Oliyad Jeilu Oumer and Dawit Abate. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


The demand for enzymes in the global market is projected to rise at a fast pace in recent years. There has been a great increase in industrial applications of pectinase owing to their significant biotechnological uses. For applying enzymes at industrial scale primary it is important to know the features of the enzyme. Thus, this study was undertaken with aims of characterizing the pectinase enzyme from Bacillus subtilis strain Btk27 and proving its potential application in demucilisation of coffee. In this study, the maximum pectinase activity was achieved at pH 7.5 and 50°C. Also, the enzyme activity was found stimulated with Mg2+ and Ca2+ metal ions. Moreover, it was stable on EDTA, Trixton-100, Tween 80, and Tween 20. Since Bacillus subtilis strain Btk27 was stable in most surfactants and inhibitors it could be applicable in various industries whenever pectin degradation is needed. The enzyme m and max values were identified as 1.879 mg/ml and 149.6 U, respectively. The potential application of the enzyme for coffee processing was studied, and it is found that complete removal of mucilage from coffee beans within 24 hours of treatment indicates the potential application in coffee processing.