Industrial applications of microbial lipases

Hasan, Fariha; Shah, Aamer Ali; Hameed, Abdul

doi:10.1016/j.enzmictec.2005.10.016

Cited by 1,683 publications

(1,132 citation statements)

References 139 publications

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“…They are considered as the third largest enzyme group, after proteases and carbohydrases, based on their market value. There is a large potential for lipases in industrial applications such as additives in foods, pharmaceuticals (naproxen, ibuprofen), medical assay, cosmetics, leather, dairy industry (cheese ripening, flavour development, EMC technology), fine chemicals, detergents, paper manufacture and waste-water treatment (Hasan et al 2006). The enantioselective and regioselective nature of lipases have been utilized for the resolution of chiral drugs, fat modification, synthesis of cocoa butter substituent, biofuels, and for synthesis of personal care products and flavor enhancers (Hasan et al 2006;Treichel et al 2010).…”

Section: Introductionmentioning

confidence: 99%

Detergent compatible alkaline lipase produced by marine Bacillus smithii BTMS 11

Lailaja

Chandrasekaran

2013

World J Microbiol Biotechnol

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Bacillus smithii BTMS 11, isolated from marine sediment, produced alkaline and thermostable lipase. The enzyme was purified to homogeneity by ammonium sulfate precipitation and ion exchange chromatography which resulted in 0.51 % final yield and a 4.33 fold of purification. The purified enzyme was found to have a specific activity of 360 IU/mg protein. SDS-PAGE analyses, under non-reducing and reducing conditions, yielded a single band of 45 kDa indicating the single polypeptide nature of the enzyme and zymogram analysis using methylumbelliferyl butyrate as substrate confirmed the lipolytic activity of the protein band. The enzyme was found to have 50°C and pH 8.0 as optimum conditions for maximal activity. However, the enzyme was active over wide range of temperatures (30-80°C) and pH (7.0-10.0). Effect of a number of metal salts, solvents, surfactants, and other typical enzyme inhibitors on lipase activity was studied to determine the novel characteristics of the enzyme. More than 90 % of the enzyme activity was observed even after 3 h of incubation in the presence of commercial detergents Surf, Sunlight, Ariel, Henko, Tide and Ujala indicating the detergent compatibility of B. smithii lipase. The enzyme was also found to be efficient in stain removal from cotton cloths. Further it was observed that the enzyme could catalyse ester synthesis between fatty acids of varying carbon chain lengths and methanol with high preference for medium to long chain fatty acids showing 70 % of esterification. Results of the study indicated scope for application of this marine bacterial lipase in various industries.

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Section: Introductionmentioning

confidence: 99%

Detergent compatible alkaline lipase produced by marine Bacillus smithii BTMS 11

Lailaja

Chandrasekaran

2013

World J Microbiol Biotechnol

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“…Novel biotechnological applications have been successfully established using lipase for the synthesis of biopolymers and biodiesel, the production of enantiopure pharmaceuticals, agro-chemicals and fl avor compounds [1][2][3][4][5][6]. The advantages of enzymatic hydrolysis over a chemical process are less energy requirement and higher quality of obtained product.…”

Section: Introductionmentioning

confidence: 99%

Extracellular lipase of Aspergillus niger NRRL3; production, partial purification and properties

Adham

Ahmed

2009

Indian J Microbiol

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Four strains of Aspergillus niger were screened for lipase production. Each was cultivated on four different media differing in their contents of mineral components and sources of carbon and nitrogen. Aspergillus niger NRRL3 produced maximal activity (325U/ml) when grown in 3% peptone , 0.05% MgSO 4 .7H 2 O, 0.05% KCl, 0.2% K 2 HPO 4 and 1% olive oil:glucose (0.5:0.5). A. niger NRRL3 lipase was partially purifi ed by ammonium sulphate precipitation. The majority of lipase activity (48%) was located in fraction IV precipitated at 50-60% of saturation with a 18-fold enzyme purifi cation. The optimal pH of the partial purifi ed lipase preparation for the hydrolysis of emulsifi ed olive oil was 7.2 and the optimum temperature was 60°C. At 70°C, the enzyme retained more than 90% of its activity. Enzyme activity was inhibited by Hg 2+ and K + , whereas Ca 2+ and Mn 2+ greatly stimulated its activity. Additionally, the formed lipase was stored for one month without any loss in the activity.

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“…The large applicability in this area is due to certain properties such as stability, selectivity, large substrate specificity and because they do not need cofactors (Castro et al 2004), beyond different catalytic activities, genetic manipulation facility and the faster growth of microorganisms in low cost culture media (Hasan et al 2006). Many microorganisms are lipase producers as well as the main part of commercial lipases is from microbial origin (Veerabagu et al 2013).…”

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confidence: 99%

Bioprospecting of lipolytic microorganisms obtained from industrial effluents

Peil

Kuss

Rave

et al. 2016

An. Acad. Bras. Ciênc.

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The lipases have ability to catalyze diverse reactions and are important in different biotechnological applications. The aim of this work was to isolate and characterize microorganisms that produce lipases, from different food industry effluents localized in Pelotas, RS/Brazil. Bacteria were identified using Gram stain and biochemical tests (Vitek 2®). Fungi were identified according to macro and micromorphology characteristics. The extracellular lipase production was evaluated using the Rhodamine B test and the enzymatic activity by titration. Twenty-one bacteria were isolated and identified as Klebsiella pneumoniae ssp. pneumoniae, Serratia marcescens, Enterobacter aerogenes, Raoultella ornithinolytica and Raoultella planticola. Were characterized isolated filamentous fungi by the following genera: Alternaria sp., Fusarium sp., Geotrichum sp., Gliocladium sp., Mucor sp., Paecilomyces sp. and Trichoderma sp. Extracellular lipase production was observed in 71.43% of the bacteria and 57.14% of the fungi. The bacterium that presented better promising enzymatic activity was E. aerogenes (1.54 U/ml) however between fungi there was not significant difference between the four isolates. This study indicated that microorganisms lipase producers are present in the industrial effluents, as well as these enzymes have potential of biodegradation of lipid compounds.

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Industrial applications of microbial lipases

Cited by 1,683 publications

References 139 publications

Detergent compatible alkaline lipase produced by marine Bacillus smithii BTMS 11

Detergent compatible alkaline lipase produced by marine Bacillus smithii BTMS 11

Extracellular lipase of Aspergillus niger NRRL3; production, partial purification and properties

Bioprospecting of lipolytic microorganisms obtained from industrial effluents

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