Purification and characterisation of a thermostable alkaline lipase from a new thermophilic Bacillus sp. RSJ-1

Sharma, Rohit K.; Soni, Sanjeev Kumar; Vohra, Rakesh M.; Gupta, Lalita; Gupta, Jancy

doi:10.1016/s0032-9592(01)00316-8

Cited by 148 publications

(134 citation statements)

References 21 publications

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“…The gradual decrease in enzyme production after 7 days might be due to the accumulation of toxic end products of metabolism or exhaustion of available nutrients in medium. Kumar et al (2012) have found that Bacillus sp gave the maximum yield of (1.2 Eu mLG 1 ) lipase after 72 h of incubation whereas Sharma et al (2002) showed the lipase production was highest after 12 h of incubation.…”

Section: Optimization Of Process Variables Effect Of Incubation Periodmentioning

confidence: 99%

Optimization of Lipase Production by Thermo-Alkalophilic Bacillus sp. 8C

Bhosale¹,

Uzma²,

Bismile³

2015

Research J. of Microbiology

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Microbial lipases catalyzing the hydrolysis and synthesis of esters from glycerol and fatty acids are commercially important in food, dairy, detergent and leather industries. In the present study, 15 thermo-alkalophilic bacterial strains isolated from a compost soil sample were screened for lipase production in beef extract nitrate medium containing 1% tributyrin. The strain 8C, giving maximum lipolytic activity was morphologically and biochemically identified as Bacillus sp. Lipase production from strain 8C was optimized by studying effects of incubation period, initial pH of medium, carbon and nitrogen sources, metals, substrates and thiols under static conditions. Lipase production was maximum after 7 days of incubation at 50°C and pH 9.0 and when sesame oil was used as a substrate. Supplementation of ribose or raffinose and ammonium sulphate (1%) as sole sources of carbon and nitrogen also stimulated lipase production over control. Of the different thiols tested, methionine greatly increased lipase production (175 Eu mLG 1 ) whereas, FeCl 3 (50 mM) found to be most suitable metal salt for optimal lipase production (300 Eu mLG 1 ). Under optimized conditions, lipase production by thermo-alkalophilic Bacillus sp. 8C was increased by 6.36 fold compared to unoptimized conditions. Key words: Thermophilic, alkaline, ribose, FeCl 3 , methionine, sesame oil INTRODUCTIONLipases (triglycerol hydrolases (EC 3.1.1.3) are the hydrolytic enzymes belonging to serine hydrolase family and catalyze conversion and synthesis of esters from glycerol and fatty acids. Lipolytic reactions are highly chemo-, regio and or enantioselective and operate at the interface of oil and water (Nguyen et al., 2010). High quality and low energy consumption of lipase catalyzed reactions make them superior over conventional steam splitting methods operating at high temperature and pressure (Treichel et al., 2010). These characteristics of lipases increased their demand in different industries including food and dairy, detergent, cosmetics, leather, paper and pulp, biodiesel and pharmaceutical (Hasan et al., 2007).Thermophilic lipases are of special interest for industrial applications due to their stability and high activity at higher temperatures and being stable in presence of chemicals (Messias et al., 2009;Uttatree et al., 2010). Lipases being third largest selling group of enzymes with more than 1000 t of annual production and approaching to a billion dollar business. Lipases active at alkaline pH are of great importance in detergent industry where these enzymes are used for removal of fat stains and dirt (Bora and Bora, 2012). The use of alkaline lipases in detergent formulation substantially

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Section: Optimization Of Process Variables Effect Of Incubation Periodmentioning

confidence: 99%

Optimization of Lipase Production by Thermo-Alkalophilic Bacillus sp. 8C

Bhosale¹,

Uzma²,

Bismile³

2015

Research J. of Microbiology

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“…However, the biggest market of their use is in the detergent formulation (7,16). Regarding detergents applications, new challenges for lipases producers can be pointed (7,18,19): (1) the high variation in the triglyceride content of fat stains, requiring lipases with low substrate specificity; (2) the relatively harsh washing conditions (pH 10-11 and 30-60ºC), requiring stable enzymes; and (3) the effects of chemical denaturation and/or proteolytic degradation caused by detergents additives such as surfactant linear alkyl benzene sulfonate (LAS) and proteases. The functional importance of lipases in the detergent industry is related to the removal of fatty residues in laundry, dishwashers as well as for cleaning of clogged drains.…”

Section: Introductionmentioning

confidence: 99%

Characterization of alkaline lipase from Fusarium oxysporum and the effect of different surfactants and detergents on the enzyme activity

Prazeres¹,

Cruz²,

Pastore³

2006

Braz. J. Microbiol.

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Nowadays, there is a tendency of use of low temperature in laundry cleaning for both environmental and economical reasons, which makes the use of enzymes in detergent products indispensable. Since lipases are efficient catalyst both in solution and at the water-liquid interface, they are potentially suitable for lipid stain removal applications in industrial laundry and household detergents. The effect of different commercial detergents and surfactants on enzymatic activity of lipase from Fusarium oxysporum was observed through p-nitrophenylpalmitate (pNPP) assay. The enzyme was compatible with various ionic and non-ionic surfactants as well as commercial detergents. Lipase activity was strongly inhibited by Sodium Dodecyl Sulphate (SDS), but not by Triton X-100 and Triton X-114. The best assay conditions observed for this lipase were pH 8.0 and 50ºC. The enzyme was stable at alkaline pH and remained 93% of residual activity during 1 h incubation at 60ºC. The highest lipase activity was measured with triglycerides of middle and long chain fatty acids (C8-C18). This enzyme showed a variable specifity/hydrolytic activity towards various fats and oils. All these properties and its resistance towards various surfactants and tolerance to commercial detergents make this lipase a potential additive for detergent formulation.

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“…These enzymes are effective catalysts of various inter-esterification and trans-esterification reactions (Gupta et al, 2004;Romdhane et al 2012) in the presence of decreasing amounts of water and often in the presence of organic solvents (Ogino et al, 2004;Palacios et al, 2014). Because of their versatility, lipases are the enzymes of choice for multiple applications in different fields: food, pharmaceutical, chemical, detergent, leather, textile, cosmetics and paper industries, for organic synthesis, biodiesel production or even environmental management (Pandey et al, 1999;Sharma et al, 2002;Barros et al, 2010;Foresti and Ferreira, 2010).…”

Section: Reverse Transcription (Rt)-pcrmentioning

confidence: 99%

Cloning, Sequence Analysis and Expression Patterns during Seed Germination of a Rapeseed (Brassica napus L.) G-x-S-x-G-motif Lipase Gene

Ghram

Belguith

Mustapha

et al. 2016

Not Bot Horti Agrobo

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Lipases catalyze the hydrolysis of ester bonds in triacylglycerides, generating glycerol and free fatty acids. These enzymes are encoded by extremely complex gene families, and appear to fulfil many different biological functions. Although they are present in all types of organisms, available information on plant lipases is still very limited, as compared to their bacterial and animal counterparts. A full-length clone, BnLIP, encoding a putative lipase, has been isolated by PCR amplification of Brassica napus genomic DNA, with oligonucleotide primers derived from the sequence of an Arabidopsis thaliana homologue. The clone included an open reading frame of 1581 bp encoding a polypeptide of 526 amino acids, with a calculated molecular mass of 59.5 kDa. Analysis of the deduced protein sequence, sequence alignment with homologous proteins from related plant species, and a phylogenetic analysis revealed that the BnLIP protein belongs to the 'classical' GxSxG-motif lipase family. RT-PCR assays indicated that the BnLIP gene is expressed specifically, but only transiently, during seed germination: the lipase mRNA was not present at detectable levels in ungerminated seeds, was detected only three days after seed imbibition, but its levels decreased rapidly afterwards. No expression was observed in roots, stems or leaves of adult plants. This expression pattern suggests that BnLIP is one of the lipases involved in the hydrolysis of triacylglycerides stored in rapeseed seeds, ultimately providing nutrients and energy to sustain seedling growth until photosynthesis is activated.

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Purification and characterisation of a thermostable alkaline lipase from a new thermophilic Bacillus sp. RSJ-1

Cited by 148 publications

References 21 publications

Optimization of Lipase Production by Thermo-Alkalophilic Bacillus sp. 8C

Optimization of Lipase Production by Thermo-Alkalophilic Bacillus sp. 8C

Characterization of alkaline lipase from Fusarium oxysporum and the effect of different surfactants and detergents on the enzyme activity

Cloning, Sequence Analysis and Expression Patterns during Seed Germination of a Rapeseed (Brassica napus L.) G-x-S-x-G-motif Lipase Gene

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