Production, purification, and characterization of lipase from thermophilic and alkaliphilic Bacillus coagulans BTS-3

2005 ◽  
Vol 41 (1) ◽  
pp. 38-44 ◽  
Author(s):  
Satyendra Kumar ◽  
Khyodano Kikon ◽  
Ashutosh Upadhyay ◽  
Shamsher S. Kanwar ◽  
Reena Gupta
2002 ◽  
Vol 30 (5) ◽  
pp. 590-595 ◽  
Author(s):  
Min-Jen Tseng ◽  
Mee-Nagan Yap ◽  
Khanok Ratanakhanokchai ◽  
Khin Lay Kyu ◽  
Shui-Tein Chen

2021 ◽  
Vol 26 (5) ◽  
pp. 2994-3001
Author(s):  
ABDULLAH A. AL-GHANAYEM ◽  

Thermo-alkaline stable lipase producing B. coagulans was isolated and identified by 16S rRNA sequencing. The lipase production was optimized using different growth parameters. The enzyme was purified and characterized in terms of pH, temperature, solvents, heavy metal ions and inhibitors. Compatibility with commercially available detergents was also studied. The isolate showed maximum lipase production at 37 ⁰C; pH of 9 within 48 h. Addition of magnesium chloride increased lipase production. Sephadex G-100 chromatography was used to purify lipase. The enzyme showed maximum activity at pH 8 of 30 ⁰C. Lipase form B. coagulans was active at a wide range of temperature between 30-70 ⁰C. It was stable in most of the solvents at a concentration 5 and 10%, except dimethyl sulfoxide (DMSO) and methanol. Iodoacetic acid (IAA) and p-chloromercuribenzoic acid (pCMB) had an inhibitory effect on lipase. The lipase was compatible with commercially available detergents that increased the brightness and whiteness of the tested cotton fabrics. Lipase from B. coagulans with alkaline stability at a wide range of temperature has potential application in the detergent industry.


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