Presence Of Commercial Detergents Research Articles

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

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.

Truncation of C-terminal amino acids of GH26 endo-mannanase (ManB-1601) affects biochemical properties and stability against anionic surfactants

Hitherto, the contribution of C-terminal amino acids in structure, stability and function of GH26 endo-mannanases has not been demonstrated. Semi-logarithmic plot of endo-mannanase activity showed a progressive decline with increase in the number of truncated amino acids [ManB-CΔ5 (129 U/mL), ManB-CΔ10 (47 U/mL), ManB-CΔ15 (0.05 U/mL) and ManB-CΔ20 (0.02 U/mL)]. ManB-CΔ5 and ManB-CΔ10 exhibited similar temperature and pH optima and product profile but biochemical properties (kinetic constants, mannan hydrolysis, response to metal ions and enzyme inhibitors) and stability (in presence of commercial detergents, anionic surfactants and organic solvents and half-life) were markedly affected. Interaction of truncated proteins with anionic surfactants was probed using intrinsic, Nile red, acrylamide quenching, resonance light scattering and synchronous fluorescence spectroscopy studies. Truncation of ten amino acids increased vulnerability to anionic surfactants as conformational changes, exposure of the hydrophobic core and susceptibility to unfolding process were observed. The microenvironment around Trp residues was affected more with surfactants as compared to Tyr residues in truncated proteins. Zn2+ coordination might not play a role in providing stability against SDS. MD simulation studies corroborated that C-terminal amino acids (327−336) helps in structure stabilization, regulating flexibility of loops around the active site and preventing denaturation in the presence of SDS.

Characterization of a novel lipase from Bacillus licheniformis NCU CS-5 for applications in detergent industry and biodegradation of 2,4-D butyl ester

Enzymatic degradation has become the most promising approach to degrading organic ester compounds. In this study, Bacillus licheniformis NCU CS-5 was isolated from the spoilage of Cinnamomum camphora seed kernel, and its extracellular lipase was purified, with a specific activity of 192.98 U/mg. The lipase was found to be a trimeric protein as it showed a single band of 27 kDa in SDS-PAGE and 81 kDa in Native-PAGE. It was active in a wide range of temperatures (5–55 °C) and pH values (6.0–9.0), and the optimal temperature and pH value were 40 °C and 8.0, respectively. The enzyme was active in the presence of various organic solvents, metal ions, inhibitors and surfactants. Both crude and purified lipase retained more than 80% activity after 5 h in the presence of commercial detergents, suggesting its great application potential in detergent industry. The highest activity was found to be towards medium- and long-chain fatty acids (C6-C18). Peptide mass spectrometric analysis of the purified lipase showed similarity to the lipase family of B. licheniformis. Furthermore, it degraded more than 90% 2,4-D butyl ester to its hydrolysate 2,4-D within 24 h, indicating that the novel lipase may be applied to degrade organic ester pesticides.

Purification and characterization of a novel high molecular weight alkaline protease produced by an endophytic Bacillus halotolerans strain CT2

A protease-producing strain CT2 isolated from Tunisian potatoes, exhibiting a potent protease activity (prot CT2), was identified as Bacillus halotolerans according to 16S ribosomal DNA sequence analysis. Maximum prot CT2 production was obtained in medium supplemented with bean seed proteins. Proteolytic activity was purified by ammonium sulphate precipitation, Sephacryl S-200 gel filtration and SP-sepharose cation-exchange chromatography. Optimal enzyme activity was reached at pH 9 and temperature of 50 °C. Proteolytic activity was enhanced by Ca2+ and Mn2+ ions, completely inhibited by PMSF suggesting a serine protease nature and exhibited high stability in the presence of commercial detergents. Prot CT2 showed broad substrate specificity towards both synthetic and natural substrates, with a high capacity to hydrolyze legume seed proteins. Using electrophoretic analysis, its molecular weight was around 250 kDa with two major subunit showing important homologies with serine proteases belonging to the subtilisin-like serine proteases. Based on the Lineweaver–Burk plots Km and Vmax values were 10 mg/ml and 50,000 U/mg respectively. This newly described prot CT2 displays relevant properties which highlight its potential use in various industrial and biotechnological applications.

Protease production by Brevundimonas sp. and Trabulsiella guamensis isolated from contaminated soil

Microorganisms have ability to produce protease enzyme which predominates 40% of the international enzyme market. In present study, three strains of protease producing bacteria were isolated from soil using Gelatin agar media and named as G9, R8 and R5. The isolates were identified as Brevundimonas sp. (R8) and Trabulsiella guamensis (G9 and R5) according to morphological, biochemical and 16S rRNA gene sequencing data. The maximum protease production was found to be at 37 °C and pH 7. These proteases are very stable in the presence of commercial detergents that indicates the promising usage in detergent industry. Maximum protease yield (94%) was found when wheat bran was used as the sole carbon source. All selected bacterial strains showed maximum protease production with 2% Inoculum concentration. These rarely reported protease producers Brevundimonas sp. and T. guamensis can be suitable candidates for detergent industry and biotechnological applications.

A novel esterase from Paenibacillus sp. PBS-2 is a new member of the β-lactamase belonging to the family VIII lipases/esterases.

Screening of a gene library from Paenibacillus sp. PBS-2 generated in Escherichia coli led to the identification of a clone with lipolytic activity. Sequence analysis showed an open reading frame encoding a polypeptide of 378 amino acid residues with a predicted molecular mass of 42 kDa. The esterase displayed 69% and 42% identity with the putative β-lactamases from Paenibacillus sp. JDR-2 and Clostridium sp. BNL1100, respectively. The esterase contained a Serx- x-Lys motif that is conserved among all β-lactamases found to date. The protein PBS-2 was produced in both soluble and insoluble forms when E. coli cells harboring the gene were cultured at 18°C. The enzyme is a serine protein and was active against p-nitrophenyl esters of C2, C4, C8, and C10. The optimum pH and temperature for enzyme activity were pH 9.0 and 30°C, respectively. Relative activity of 55% remained at up to 5°C with an activation energy of 5.84 kcal/mol, which indicates that the enzyme is cold-adapted. Enzyme activity was inhibited by Cd(2+), Cu(2+), and Hg(2+) ions. As expected for a serine esterase, activity was inhibited by phenylmethylsulfonyl fluoride. The enzyme was remarkably active and stable in the presence of commercial detergents and organic solvents. This cold-adapted esterase has potential as a biocatalyst and detergent additive for use at low temperatures.

A statistical approach for the enhanced production of thermostable alkaline protease showing detergent compatibility activity from Bacillus circulans

Response surface methodology (RSM) was employed to enhance the production of a thermostable alkaline protease from Bacillus circulans. Significant influences of peptone, yeast extract, and glucose on protease production were noted with a one-variable-at-a-time optimization strategy. Then, a full factorial central composite design (CCD) was applied to study the effects of glucose, peptone, and yeast extract to determine the optimal concentrations of these compounds for protease production by B. circulans under shake flask fermentation conditions. The statistical reliability and significance of the model was validated by an F-test for analysis of variance (ANOVA); enzyme production was improved significantly under optimized conditions. The enzyme was purified by ammonium sulphate fractionation, and gel filtration chromatography. Maximum enzyme activity was observed at 60°C temperature, and at pH 10. Alkaline protease from B. circulans showed excellent compatibility and stability in the presence of commercial detergents like Ariel, Surf Excel, Tide, Rin, Nirma, Wheel, and Doctor and showed excellent blood destaining effectiveness with commercial detergents.

Purification and Characterization of Highly Alkaline Lipase from Bacillus licheniformis MTCC 2465: and Study of its Detergent Compatibility and Applicability

AbstractAn extracellular alkaline lipase from Bacillus licheniformis MTCC 2465 has been studied and analyzed for its applicability as a detergent additive. The lipase obtained from Bacillus licheniformis MTCC 2465 was purified by ammonium sulfate fractionation and gel filtration chromatography. The enzyme was precipitated with a 60 % saturated ammonium sulfate fraction showed 6.73 fold purification with the fold purification of 10.4 and specific activity of 398 U/mg of protein with gel filtration chromatography. The optimal pH and temperature for activity were 10 and 60 °C respectively. The enzyme was found to be stable in the pH range of 8–11 with 90 % retention of activity at pH 11. The enzyme retained 90 % activity at 60 °C and 70 % of activity at 70 °C for 1 h. The enzyme activity was maximally enhanced by Hg2+ followed by Co2+ and Fe2+. The lipase was found to be stable in organic solvents with maximum stability in acetone followed by ethanol. The lipase exhibited remarkable stability in the presence of commercial detergents and found to be stable in bleaching agents. Wash performance analysis resulted in improvement of 10 % more grease removal ability of the present lipase in comparison to commercially available lipase.

Production, characterization and applications of organic solvent tolerant lipase by Pseudomonas aeruginosa AAU2

Abstract Jatropha seedcake (JSC) represents an important environmental problem owing to its toxicity for the biodiesel producing sectors where they are generated in bulk as a major by-product. The aim of the present work was to study the feasibility of JSC as a substrate for lipase production under submerged condition. Pseudomonas aeruginosa AAU2 isolated from dumped rotting JSC was found to produce extracellular solvent tolerant lipase (0.432 U ml −1 ). A 11.4-fold increase in enzyme yield was obtained in an optimized medium containing 20 g JSC/l, 2.5 g potassium nitrate/l and 0.1 v/v% Tween 80 after 60 h of incubation at 30 °C under shake flask conditions (150 rpm). The pH and temperature optima of the partially purified AAU2 lipase were 7.5 and 40 °C, respectively. The AAU2 lipase was found to be a cysteine hydrolase and exhibited preference towards longer carbon chain fatty acid ester substrates over the shorter ones. The enzyme exhibited significant stability in the presence of commercial detergents namely, Ezee ® and Wheel ® . The AAU2 lipase efficiently catalyzed biodiesel production using Jatropha oil. In addition, the enzyme also hydrolyzed 86.49% of commercially available phorbol ester (phorbol 12-myristate 13-acetate) within 12 h of incubation at 37 °C, suggesting its application in detoxification of phorbol ester from JSC. These results demonstrate viable approach for utilization of JSC biomass and degradation of phorbol esters by P. aeruginosa AAU2.

Gene Cloning and Characterization of a Cold-Adapted Esterase from Acinetobacter venetianus V28

Acinetobacter venetians V28 was isolated from the intestine of righteye flounder, Poecilopsetta plinthus caught in Vietnam seawater, and the esterase gene was cloned using a shotgun method. The amino acid sequence deduced from the nucleotide sequence (1,017 bp) corresponded to a protein of 338 amino acid residues with a molecular weight of 37,186. The esterase had 87% and 72% identities with the lipases of A. junii SH205 and A. calcoaceticus RUH2202, respectively. The esterase contained a putative leader sequence, as well as the conserved catalytic triad (Ser, His, Asp), consensus pentapeptide GXSXG, and oxyanion hole sequence (HG). The protein from the strain V28 was produced in both a soluble and an insoluble form when the Escherichia coli cells harboring the gene were cultured at 18 degrees C. The maximal activity of the purified enzyme was observed at a temperature of 40 degrees C and pH 9.0 using p-NP-caprylate as substrate; however, relative activity still reached to 70% even at 5 degrees C with an activation energy of 3.36 kcal/mol, which indicated that it was a cold-adapted enzyme. The enzyme was a nonmetalloprotein and was active against p-nitrophenyl esters of C4, C8, and C14. Remarkably, this enzyme retained much of its activity in the presence of commercial detergents and organic solvents. This cold-adapted esterase will be applicable as catalysts for reaction in the presence of organic solvents and detergents.

Isolation and Molecular Characterisation of Alkaline Protease Producing Bacillus thuringiensis

Proteases are of particular interest because of their action on insoluble keratin substrates and generally on a broad range of protein substrates. Proteases are one of the most important groups of industrial enzymes used in detergent, protein, brewing, meat, photographic, leather, dairy, pharmaceutical and food industry. In the present study, the organism isolated from the protein rich soil sample was identified by biochemical and molecular characterisation as Bacillus thuringiensis and further optimum conditions for alkaline protease synthesis were determined. The growth conditions for B. thuringiensis was optimised by inoculating into yeast extract casein medium at different pH and incubating at different temperatures. The maximum protease production occurred at pH 8 and at 37 °C. B. thuringiensis showed proteolytic activity at various culture conditions. Optimum conditions for the protease activity were found to be 47 °C and pH 8. In the later stage, the blood removing action of crude and partially purified protease was found to be effective within 25 min in the presence of commercial detergents indicating the possible use of this enzyme in detergent industry. Enzyme also showed good activity against hair substrate keratin and can be used for dehairing.

Biochemical characterization of a novel thermostable xyloglucanase from an alkalothermophilic Thermomonospora sp.

Xyloglucanase from an extracellular culture filtrate of alkalothermophilic Thermomonospora sp. was purified to homogeneity with a molecular weight of 144kDa as determined by SDS-PAGE and exhibited specificity towards xyloglucan with apparent K (m) of 1.67mg/ml. The enzyme was active at a broad range of pH (5-8) and temperatures (40-80°C). The optimum pH and temperature were 7 and 70°C, respectively. The enzyme retained 100% activity at 50°C for 60h with half-lives of 14h, 6h and 7min at 60, 70 and 80°C, respectively. The kinetics of thermal denaturation revealed that the inactivation at 80°C is due to unfolding of the enzyme as evidenced by the distinct red shift in the wavelength maximum of the fluorescence profile. Xyloglucanase activity was positively modulated in the presence of Zn(2+), K(+), cysteine, β-mercaptoethanol and polyols. Thermostability was enhanced in the presence of additives (polyols and glycine) at 80°C. A hydrolysis of 55% for galactoxyloglucan (GXG) from tamarind kernel powder (TKP) was obtained in 12h at 60°C and 6h at 70°C using thermostable xyloglucanases, favouring a reduction in process time and enzyme dosage. The enzyme was stable in the presence of commercial detergents (Ariel), indicating its potential as an additive to laundry detergents.

A Novel Cold-Adapted Lipase from Sorangium cellulosum Strain So0157-2: Gene Cloning, Expression, and Enzymatic Characterization

Genome sequencing of cellulolytic myxobacterium Sorangium cellulosum reveals many open-reading frames (ORFs) encoding various degradation enzymes with low sequence similarity to those reported, but none of them has been characterized. In this paper, a predicted lipase gene (lipA) was cloned from S. cellulosum strain So0157-2 and characterized. lipA is 981-bp in size, encoding a polypeptide of 326 amino acids that contains the pentapeptide (GHSMG) and catalytic triad residues (Ser114, Asp250 and His284). Searching in the GenBank database shows that the LipA protein has only the 30% maximal identity to a human monoglyceride lipase. The novel lipA gene was expressed in Escherichia coli BL21 and the recombinant protein (r-LipA) was purified using Ni-NTA affinity chromatography. The enzyme hydrolyzed the p-nitrophenyl (pNP) esters of short or medium chain fatty acids (≤C10), and the maximal activity was on pNP acetate. The r- LipA is a cold-adapted lipase, with high enzymatic activity in a wide range of temperature and pH values. At 4 °C and 30 °C, the Km values of r-LipA on pNP acetate are 0.037 ± 0.001 and 0.174 ± 0.006 mM, respectively. Higher pH and temperature conditions promoted hydrolytic activity toward the pNP esters with longer chain fatty acids. Remarkably, this lipase retained much of its activity in the presence of commercial detergents and organic solvents. The results suggest that the r-LipA protein has some new characteristics potentially promising for industrial applications and S. cellulosum is an intriguing resource for lipase screening.

Partially purified rubber seed lipase for efficient removal of fatty soil

Lipase was extracted from rubber seeds and partially purified 7.59 fold with a yield of 62.14% recovery using (NH4)2SO4 fractionation followed by batch adsorption on diethylaminoethyl (DEAE) cellulose. The extracted enzyme exhibited optimum activity as well as high stability at a temperature of 40 °C and pH 8. The kinetics of product formation continued for 30 minutes and was linear for the first 10 minutes. The enzyme exhibited good stability with sodium dodecyl sulphate (SDS), CaCl2 and Triton X-100 whereas poor stability was observed with sodium perborate and hydrogen peroxide. The enzyme was found to be less stable in the presence of commercial detergents. Hence, rather than supplementing the enzyme with detergents, pre-incubation of the enzyme with fatty soil and subsequent washing with detergents was shown to be more successful in removing fatty soil. Further studies showed that fatty stain caused by coconut oil (1mL) can be completely removed by stirring the fabric with 2% SDS 5.00 mL for 15 minutes, followed by incubation with lipase (4.00 mL, 1 mg/mL) for 30 minutes at 40 oC and subsequent washing with detergent. These findings indicated that rubber seed lipase, with its ability to function in alkaline pH (~ 8.0) and temperature ~ 40 °C and its capability to remove fatty soil efficiently, is suitable for use as a potential bio-detergent. Keywords: Bio-detergent, lipase, removal of fatty soil, rubber seed. Doi: 10.4038/jnsfsr.v39i1.2928 J.Natn.Sci.Foundation Sri Lanka 2011 39 (1):69-76

A novel cold-adapted lipase from Acinetobacter sp. XMZ-26: gene cloning and characterisation

Acinetobacter sp. XMZ-26 (ACCC 05422) was isolated from soil samples obtained from glaciers in Xinjiang Province, China. The partial nucleotide sequence of a lipase gene was obtained by touchdown PCR using degenerate primers designed based on the conserved domains of cold-adapted lipases. Subsequently, a complete gene sequence encoding a 317 amino acid polypeptide was identified. Our novel lipase gene, lipA, was overexpressed in Escherichia coli. The recombinant protein (LipA) was purified by Ni-affinity chromatography, and then deeply characterised. The LipA resulted to hydrolyse pNP esters of fatty acids with acyl chain length from C2 to C16, and the preferred substrate was pNP octanoate showing a k(cat) = 560.52 ± 28.32 s(-1), K(m) = 0.075 ± 0.008 mM, and a k(cat)/K(m) = 7,377.29 ± 118.88 s(-1) mM(-1). Maximal LipA activity was observed at a temperature of 15°C and pH 10.0 using pNP decanoate as substrate. That LipA peaked at such a low temperature and remained most activity between 5°C and 35°C indicated that it was a cold-adapted enzyme. Remarkably, this lipase retained much of its activity in the presence of commercial detergents and organic solvents, including Ninol, Triton X-100, methanol, PEG-600, and DMSO. This cold-adapted lipase may find applications in the detergent industry and organic synthesis.

Production, purification, and characterization of thermostable alkaline protease under solid state fermentation conditions for application in bio-detergent technology

Screening studies were carried out for one hundred, and fifty-three bacterial isolates with respect to their ability to produce protease(s), after growing on some industrial wastes at 55ºC, and pH 9.Two most potent thermophilic bacterial isolates concerning of alkaline thermostable protease(s) production were identified as Bacillus licheniformis B42 and Geobacillus stearothermophilus B78. Alkaline thermostable proteases productivity by the two most potent bacterial isolates was affected by substrate concentrations (solid substrate), carbon source, nitrogen source, mineral ions, vitamins, amino acid supplements, incubation temperature, incubation period, and inoculum size. Maximum both enzymes production by B. licheniformis B42 and G. stearothermophilus B78 were obtained on slaughter house wastes (SHW) concentrations,1.5,2.5 %;carbon sources; galactose, no tested sugar; nitrogen sources; diammonium hydrogen phosphate, ammonium molybdate; chelating agents; ethylene diamine tetra acetic acid (EDTA) (500 ppm), no tested ions; vitamins; thiamine pyridoxine; amino acids; arginine, DL-tyrosine at 55°C for 72 h. when inoculated by 0.5, and 2.5 ml respectively. The protease yield under all optimal conditions was increased many folds from 563.68 to 17825 U/ml (31 fold) by B. licheniformis and from 23.7 to 7096 U/ml (299 fold) by G. stearothermophilus. The purification fold of B. licheniformis B42 alkaline thermostable protease increased to 394.7 after applying Sephadex G200 and 411.9 times after Sephadex G100 column chromatography techniques. Fifteen amino acids were detected in the partially purified protease. Optimum conditions of the partially purified alkaline thermostable protease on Sephadex G200 followed by Sephadex G100 produced by B. licheniformis B42 were: incubation temperature, 50°C; thermostable between 50-70°C; pH,10; and incubation time,36 h exhibited maximal activity. The purified enzymes exhibited good stability towards chlorine. Compatibility of the purified enzyme with various commercial detergents reported that purified protease was unstable in presence of commercial detergents. Calcium chloride was able to restore and enhance the activity of the partially purified enzyme in the presence of commercial detergents. The alkaline serine proteases secreted by both strains are industrially important in respect of their abilities to act in alkaline pH and to show stability in broad pH ranges in addition to their stabilities toward sodium dodecyl sulphate(SDS), and hydrogen peroxide (H2O2), suggesting that it is a potentially candidate as an additive in the detergents formulations. Egyptian Journal of Biotechnology Vol. 25 (1) 2007: pp. 111-129

A novel thermostable lipase from Basidiomycete Bjerkandera adusta R59: characterisation and esterification studies

Microbial lipases are widely diversified in their enzymatic properties and substrate specificities, which make them very attractive for industrial application. Partially purified lipase from Bjerkandera adusta R59 was immobilized on controlled porous glass (CPG) and its properties were compared with those of the free enzyme. The free and immobilized lipases showed optimal activities at 45 and 50 degrees C, respectively. Both enzyme forms were highly thermostable up to 60 degrees C. The enzymes were stable at pH from 6.0 to 9.0 and their optimal pH for activity was 7.0. The free lipase was more thermostable in n-hexane than in aqueous environment. Both lipase preparations had good stabilities in non-polar solvents and were capable of hydrolysing a variety of synthetic and natural fats. Non-immobilized lipase activity was inhibited by disulphide bond reagents, serine and thiol inhibitors, while EDTA and eserine had no effect on enzyme activity. All anionic detergents tested in experiments inhibited lipase activity. The free lipase showed good stability in the presence of commercial detergents at laundry pH and temperatures. Applications of free and immobilized lipases for esterification were also presented.

Production of an oxidant and SDS-stable alkaline protease from an alkaophilic Bacillus clausii I-52 by submerged fermentation: Feasibility as a laundry detergent additive

An investigation was carried out on enzyme production of an oxidant and SDS-stable alkaline protease secreted by Bacillus clausii I-52 using the submerged fermentation and its application as a detergent additive. Maximum enzyme activity was produced when cells were grown under the submerged fermentation conditions at 37 °C for 48 h with an aeration rate of 1.5 vvm and agitation rate of 700 rpm in a medium (pH 10.65) containing (w/v): soybean meal, 20; wheat flour, 10; liquid maltose, 25; K 2HPO 4, 4; Na 2HPO 4, 1; MgSO 4·7H 2O, 0.1; NaCl, 4; FeSO 4·7H 2O, 0.5; Na 2CO 3, 6. The alkaline protease produced was found to be highly compatible and stable against not only the commercial detergent components such as α-orephin sulfonate and zeolite but also the commercial detergent preparations. Wash performance analysis using EMPA test fabrics revealed that BCAP exhibited high efficiency for the removal of protein stains in the presence of commercial detergents as well as surfactants. These results suggest that the alkaline protease produced from B. clausii I-52 which showed high stability against detergents has significance for an industrial perspective, especially, detergent additive.

Production of a novel alkaline lipase by Fusarium globulosum using neem oil, and its applications

Abstract A low-temperature, alkaline, and detergent-compatible lipase from Fusarium globulosum (FGL) has been produced using an inexpensive source, viz. neem oil. Maximum lipase production of 12 300 U/L was achieved in 96 h on optimizing various physicochemical parameters. The lipase exhibited remarkable stability in the presence of commercial detergents, bleaching agents, and proteases. The lipase showed a novel property of marked activation on prolonged incubation at alkaline pH. Wash performance analysis of the commercial detergent for removal of fatty stains improved upon addition of this lipase.