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Purification, characterization and potential detergent industry application of a thermostable α-amylase from Bacillus licheniformis RA31

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Title Purification, characterization and potential detergent industry application of a thermostable α-amylase from Bacillus licheniformis RA31
 
Creator Sharma, Himanshu
Batra, Navneet
Sing, Jagtar
 
Subject Laundry
Stain removal
 
Description 331-342
α-Amylase is an endoamylase catalysing the degradation of starch into maltose, maltotriose and glucose. The enzyme
isolated from microbial sources possess unique properties of thermostability thus making it a useful tool in the detergent
industry. Here, we explored a strain of thermophilic bacteria Bacillus licheniformis for its potential application in detergent
industry. The B. licheniformis RA31 was isolated from soil samples of hot spring in Rampur district of Himachal Pradesh,
India and grown on optimized media to produce thermostable α-amylase. The enzyme was ethanol precipitated, purified
(12.93 fold, 55.52% yield and 621.93 U/mg specific activity) to homogeneity with a single band on SDS-PAGE (66 kDa)
and native-PAGE (68 kDa). Purified enzyme displayed best activity in pH 8 buffer and 80% activity was retained in
pH 7 and 10. It showed temperature optima at 70°C. Its activity was decreased at 70°C (70% after 4 h), 80°C (65% after 4 h)
and 90°C (50% after 1 h). The enzyme was stimulated (126%; 5 mM) by barium chloride. It was relatively stable in the
presence of commercial detergents (109-125%), SDS (84%), Tween 20 (88%), EDTA (72%) and β-ME (70% at 10 mM).
Km and Vmax for the enzymatic hydrolysis of starch were 0.339 mg/mL and 1.450 mg/min, respectively. The enzyme
revealed the highest specificity towards wheat starch granule (140% after 1 h) and SEM analysis displayed its
biodegradation (2-10 h). Improved cleaning efficiency of potato curry stained fine cotton clothes were observed with
enzyme assisted detergent advance treatment (0.02% w/v). The enzyme showed potential applications in detergent industry.
 
Date 2022-05-02T11:17:14Z
2022-05-02T11:17:14Z
2022-05
 
Type Article
 
Identifier 0975-1009 (Online); 0019-5189 (Print)
http://nopr.niscair.res.in/handle/123456789/59638
 
Language en
 
Publisher NIScPR-CSIR, India
 
Source IJEB Vol.60(05) [May 2022]