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Title: | Isolation and characterization of different strains of Bacillus licheniformis for the production of commercially significant enzymes |
Authors: | Maria Ghani Asma Ansari Afsheen Aman Rashida Rahmat Zohra Nadir Naveed Siddiqui Shah Ali Ul Qader |
Keywords: | B. licheniformis commercial enzymes amylolytic enzyme protease pectinase |
Issue Date: | 6-Jul-2013 |
Publisher: | Karachi: Faculty of Pharmacy & Pharmaceutical Sciences University of Karachi |
Citation: | Ghani, M., Ansari, A., Aman, A., Zohra, R. R., Siddiqui, N. N., & Qader, S. A. U. (2013). Isolation and characterization of different strains of Bacillus licheniformis for the production of commercially significant enzymes. Pak J Pharm Sci, 26(4), 691-697. |
Abstract: | Utilization of highly specific enzymes for various industrial processes and applications has gained huge momentum in the field of white biotechnology. Selection of a strain by efficient plate-screening method for a specific purpose has also favored and boosted the isolation of several industrially feasible microorganisms and screening of a large number of microorganisms is an important step in selecting a potent culture for multipurpose usage. Five new bacterial isolates of Bacillus licheniformis were discovered from indigenous sources and characterized on the basis of phylogeny using 16S rDNA gene analysis. Studies on morphological and physiological characteristics showed that these isolates can easily be cultivated at different temperatures ranging from 30ºC to 55ºC with a wide pH values from 3.0 to 11.0 All these 05 isolates are salt tolerant and can grow even in the presences of high salt concentration ranging from 7.0 to 12.0%. All these predominant isolates of B. licheniformis strains showed significant capability of producing some of the major industrially important extracellular hydrolytic enzymes including α-amylase, glucoamylase, protease, pectinase and cellulase in varying titers. All these isolates hold great potential as commercial strains when provided with optimum fermentation conditions. |
URI: | http://142.54.178.187:9060/xmlui/handle/123456789/16084 |
ISSN: | 1011-601X |
Appears in Collections: | Issue 04 |
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Paper-6.htm | 142 B | HTML | View/Open |
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