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<span style="font-size:11.0pt;mso-bidi-font-size: 10.0pt;font-family:"Times New Roman";mso-fareast-font-family:"Times New Roman"; mso-bidi-font-family:"Times New Roman";mso-ansi-language:EN-GB;mso-fareast-language: EN-US;mso-bidi-language:AR-SA" lang="EN-GB">Thermostable, alkaline and detergent-tolerant lipase from a newly isolated thermophilic <i>Bacillus</i> <i>stearothermophilus</i> </span>

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Title Thermostable, alkaline and detergent-tolerant lipase from a newly isolated thermophilic Bacillus stearothermophilus
 
Creator Bacha, Abir Ben
Moubayed, Nadine M S
Abid, Islam
 
Subject Bacillus stearothermophilus
Optimization
Thermo-alkaline lipase
Purification
Detergent
Formulation
 
Description 179-188
Lipases are the
enzymes of choice for laundry detergent industries, owing to their triglyceride
removing ability from the soiled fabric, which eventually reduces the usage of
phosphate-based chemical cleansers in the detergent formulation. In this study,
a novel thermo-alkaline lipase-producing strain identified as Bacillus
stearothermophilus was isolated from the soil samples of olive oil mill.
Enhanced lipase production was observed at 55°C, pH 11 and after 48 h of
incubation. Among the substrates tested, xylose (a carbon source), peptone (a
nitrogen source) and olive oil at a concentration of 1% were suitable
substrates for enhancing lipase production. MgSO4 and Tween-80 were
suitable substrates for maximizing lipase production. The enzyme was purified
to homogeneity by a single CM-Sephadex column chromatography and revealed
molecular mass of 67 kDa. The enzyme (BL1) was active over a wide range of pH
from 9.0 to 13.0, with an optimum at pH 11.0, exhibited maximal activity at
55°C and retained more than 70% of its activity after incubation at 70°C or pH
13 for 0.5 h or 24 h, respectively. The enzyme hydrolyzed both short and
long-chain triacylglycerols at comparable rates. BL1 was studied in a
preliminary evaluation for use in detergent formulation solutions. This novel
lipase showed extreme stability towards non-ionic and anionic surfactants after
pre-incubation for 1 h at 40°C, and good stability towards oxidizing agents.
Additionally, the enzyme showed excellent stability and compatibility with
various commercial detergents, suggesting its potential as an additive in
detergent formulations.
 
Date 2015-05-14T11:38:43Z
2015-05-14T11:38:43Z
2015-04
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/31529
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.52(2) [April 2015]