Application In Detergent Formulations Research Articles

Purification and characterization of lipase enzyme from endophytic Bacillus pumilus WSS5 for application in detergent industry

Lipolytic enzymes from endophytic microbes have been the focus of intense and growing research in view of the applicability of such enzymes in various industrial applications and endophytic microorganisms may emerge as a potential source of lipases with distinct characteristics. The current work involved purification and characterization of the lipase from an endophytic-bacteria isolated from the stem of Withania somnifera L. Dunal. Based on the analysis of morphology and 16S rDNA sequence, the endophytic bacteria was identified as Bacillus pumilus and designated as B. pumilus WSS5. Purified lipase from the B. pumilus WSS5 was found to be of 27KDa as revealed by SDS-PAGE with optimum activity at 37 °C and pH 8. The stability of the enzyme in presence of various metal ions, surfactants, inhibitors, and organic solvents suggested that this enzyme could be exploited in leather and detergent industries. In addition, the stain removal potential of the crude and purified lipase was determined on cotton fabric pieces stained with vegetable oil. Lipase added to water along with detergent significantly enhanced the stain removal efficiency of a commercially available detergent. The current findings suggest the potential of B. pumilusWSS5 lipase owing to promising properties such as the alkali-thermostability, organic solvent-tolerance, and broad substrate specificity that makes it a strong candidate for application in detergent formulations, biotransformation, industries, and medicine. To our knowledge, this is the first report on the purification and characterization of lipase from bacterial endophyte isolated from the stem of Withania somnifera L. Dunal.

Production of a halotolerant lipase from Halomonas sp. strain C2SS100: Optimization by response‐surface methodology and application in detergent formulations

AbstractThe aim of this work was to optimize the production of a new lipase by a halotolerant bacterial strain Halomonas sp. C2SS100, by means of the response‐surface methodology (RSM). The process parameters having the most significant effect on lipase production were identified using the Plackett–Burman screening design‐of‐experiments. Then, Box–Behnken design was applied to optimize lipase activity and the quadratic regression model of the lipase production was built. Indeed, the lipase yield was increased, and the value obtained experimentally (39 ± 2 U/ml) was very close to the rate predicted by the model (40.3 U/ml). Likewise, optimization of parameters by RSM resulted in 2.78‐fold increase in lipase activity. These findings provide the first report on lipase production and optimization by a halotolerant bacterial strain belonging to Halomonas genus. Afterward, the biochemical properties of the produced lipase were studied for apply in oil stains removal. The crude lipase showed a maximum activity at 60°C and at pH ranging from 7 to 10. It displayed an important stability at high temperature, pH, and NaCl. Interestingly, this bacterial lipase exhibited a prominent stability toward some commercial solid and liquid detergents after 30 min of incubation at 50°C. The capability of the crude lipase to eliminate stain was ascertained on polycotton fabric pieces stained with lubricating oil. Whether with the addition of hot water alone or of a commercially available detergent, lipase is able to considerably boost the elimination of oil stains. The actual findings highlight the capacity of Halomonas sp. lipase for energy‐efficient biocatalytic application.

Effective bioconversion of feather-waste Keratin by Thermo-Surfactant Stable Alkaline Keratinase produced from Aspergillus sp. DHE7 with promising biotechnological application in detergent formulations

Keratin-rich wastes are troublesome pollutants that their accumulation could lead to environmental problems. Microbial degradation of keratin wastes has emerged as an alternative bio-catalyst to steam-pressure cooking and alkali hydrolysis for the recycling of such residues to value-added products. The current work investigates the purification and biochemical characterisation of an extracellular keratinase from new Aspergillus sp. DHE7 using turkey feathers as substrate. The enzyme was purified 31-fold with a final yield of 37.5%. Purified keratinase is monomeric and its molecular mass was estimated to be 33 kDa as demonstrated on SDS-PAGE. The enzyme was active in wide range of pH (7.0–11) and temperature (37–70 °C) profiles with maximum activity at pH 8.5 and 60 °C. The activity was strongly suppressed by phenylmethylsulfonyl fluoride (93.4% inhibition) and moderately inhibited by EDTA (41.2% inhibition), suggesting that the current keratinase belongs to serine-metalloprotease. Bivalent cations, such as Ca2+, Zn2+, and Mn2+, enhanced enzyme activity by 165.7%, 176.3%, and 194.8%, respectively. The purified keratinase exhibited a wide proteolytic activity towards soluble and insoluble protein substrates displaying its greater activity toward casein, keratin, bovine serum albumin, and gelatin, followed by feathers, goat hair, and wool, and was substantially stable and compliant with surfactants and commercial laundry detergents. The Km, Vmax, Kcat and Kcat/Km values on keratin were 2.2 mg/mL, 2702.7 U/mL, 136.5 s−1 and 62.04 (s−1/mg mL−1), respectively. According to these characteristics, Aspergillus sp. DHE7 keratinase is suggested as a potential candidate for use in detergent formulations (as an additive) and in various biotechnological applications.

Purification of Bacillus licheniformis Lipase and its Application as an Additive in Detergent for Destaining

AbstractIn this study, we aimed to optimize the nutritional and environmental conditions for the production of a novel lipase (LBL) from Bacillus licheniformis (GenBank accession no. MT118724). This strain was characterized by morphological and biochemical assays and Sanger sequencing of 16S rDNA. The crude lipolytic activity reached a maximum level 7.5 U mL−1 at 40 °C and pH 8.0 using olive oil as substrate. Additionally, the crude enzyme maintained 100% of its initial activity after incubation for 1 h at 50 °C and pH 9.0. It is mandatory to note that LBL lipase displayed appreciable stability over a wide pH range and extreme temperatures. After purification, the optimal lipolytic activity was observed at pH 8.0 and 40 °C. LBL was shown to be a monomeric protein with an estimated molecular weight of 40 kDa. This novel lipase exhibited high stability and excellent compatibility compared to lipase extracted from Thermomyces lanuginosa (Lipolase® from Novozymes, Denmark) toward various detergents. Washing performance analysis revealed that it efficiently removes tomato sauce stain from cotton cloth. All these interesting enzymatic properties favor this new lipase as a potent candidate for applications in detergent formulations.

Enhancement of Aeribacillus pallidus strain VP3 lipase catalytic activity through optimization of medium composition using Box-Behnken design and its application in detergent formulations

Lipases are hydrolytic enzymes owing much importance in industrial applications. These enzyme-based detergents are ecofriendly and produce a wastewater with low level of COD (chemical oxygen demand). In the present work, a novel halophilous, thermoalkaline, and detergent-tolerant lipase produced by a newly isolated Aeribacillus pallidus strain VP3 was studied. Considerable interest has been given to this lipase by the improvement of its catalytic activity through the optimization of the pH, the (C/N) ratio, and the inoculum size, using the response surface methodology based on the Box-Behnken design of experiments. A total of 16 experiments were conducted, and the optimized pH, (C/N) ratio, and inoculum size were 10, 1, and 0.3, respectively. The results of the analysis of variance (ANOVA) test indicated that the established model was significant (p value < 0.05). The optimization of the production conditions leads to 2.83-fold of increase in the catalytic activity calculated as the ratio of the activity obtained after optimization (68U) and the initial activity before optimization (24U). All in all, the lipase of Aeribacillus pallidus could be considered as a potential candidate to be incorporated in detergent formulations since it shows a good stability towards detergents and wash performance.

Albacore tuna spleen trypsin: Potential application as laundry detergent additive and in carotenoprotein extraction from Pacific white shrimp shells

Abstract Partitioned trypsin from spleen of albacore tuna (Thunnus alalunga) by ATPS was evaluated for its potential applications in laundry detergents and in the recovery of carotenoprotein from Pacific white shrimp (Litopenaeus vannamei) shells. The partitioned trypsin was extremely stable toward various surfactants and bleach agents and showed excellent stability and compatibility with commercial liquid and solid detergents. Additionally, partitioned trypsin showed an efficient hydrolysis and recovery of carotenoprotein from Pacific white shrimp shells. The carotenoprotein recovery was maximized by the hydrolysis of shrimp shells using 0.8 trypsin units/g shrimp shells at 25 °C for 45 min and shrimp shells/buffer ratio of 1:2 (w/v). Carotenoprotein consisted of 72.4% protein, 18.8% lipid, 7.1% ash, 1.6% chitin, and 73.3 µg total astaxanthin/g sample. It was rich in essential amino acids. When the hydrolytic activities of albacore tuna and bovine trypsins used in the extraction of carotenoprotein in Pacific white shrimp shells were compared, the recovery efficacy of protein and pigment by albacore tuna trypsin was similar to that achieved by bovine trypsin. These results suggest that albacore tuna trypsin could be used as an ideal choice for application in detergent formulations and for extraction of carotenoproteins.

Gene cloning, expression, molecular modeling and docking study of the protease SAPRH from Bacillus safensis strain RH12

The sapRH gene, which encodes the serine alkaline protease SAPRH, from Bacillus safensis RH12, was isolated and its DNA sequence was determined. The deduced amino-acid sequence showed strong homology with other Bacillus proteases. The highest sequence identity value (97%) was obtained with SAPB from B. pumilus CBS, with only 9 amino-acids of difference. The region, encoding SAPRH was heterologously expressed in E. coli BL21-AI™ cells using GATEWAY™ pDEST™17 expression-vector. The recombinant (His)6-tag enzyme (His6-rSAPRH) was purified in a single affinity chromatography step and its biochemical properties were determined and compared to those of SAPRH and rSAPB. Interestingly, His6-rSAPRH showed improved thermostability compared to SAPRH and rSAPB. The molecular dynamics of SAPRH compared to SAPB revealed a more thermostable structure, thus confirming the in vitro results showing that His6-rSAPRH has a t1/2 of 120 min against 90 and 30 min for SAPRH and rSAPB, respectively, at 70 °C and different kinetic parameters to synthetic peptides. The docking simulations data allow in getting an insight into the involvement of some key amino-acids in substrate binding and account for the selectivity. Overall, this is the first report of a sapRH gene cloned from B. safensis which can be a promising potential candidate for future applications in detergent formulations.

Thermodynamics of a Ca2+ dependent, highly thermostable and detergent compatible purified alkaline serine protease from Nocardiopsis xinjiangensis strain OM-6

Extracellular alkaline protease producing salt tolerant alkaliphilic actinobacteria, Nocardiopsis xinjiangensis strain OM-6 was isolated from Okha Madi (OM) site of coastal Gujarat, India. The purified protease was stable even at 70°C in 100mM Ca2+ with Kd=20×10−3 and t1/2=34min. The activation energies (E), enthalpy (∆H*) and entropy (∆S*) for protease deactivation were 29.35kJ/mol, 26.68kJ/mol and −186.22J/mol, respectively in 200mM Ca2+. The ∆G* for protease deactivation was 97.63kJ/mol at 50°C in 100mM Ca2+. OM-6 protease exhibited enhanced residual activities up to 103%, 70%, 144% and 119% with SDS, CTAB, Tween 80 and Triton X-100, respectively after 2h of incubation at 40°C. Interestingly, residual activity of OM-6 protease increased by 450% and 559% in 50mM H2O2 and 10mM β-mercaptoethanol respectively even after 2h of incubation. Moreover, protease retained 100% of its original activity with H2O2 and β-mercaptoethanol at highest concentration after 24h. The protease retained more than 60% of original activity with 1% w/v of each commercial detergent even after 2h at 40°C. These unique properties of protease make it an ideal choice for application in detergent formulations and enzymatic peptide synthesis.

Purification and Characterization of a Halotolerant and Thermotolerant Lipase Produced from a Novel Bacteria "Brevibacterium Halotolerans PS4 |KX671556|" and its Application in Detergent Formulations

An extracellular lipase was isolated and purified from the culture broth of Brevibacterium halotolerans PS4 to provide homogeneity using ammonium sulfate precipitation followed by chromatographic techniques on Sephadex G-75 colummn, resulting in a purification factor of 2.98 fold with specific activity of 1016.10 IU/mg. The molecular weight of the purified lipase was estimated by SDS-PAGE to be 80 kDa. The purified lipase had the maximal activity within the pH range of 6 to 7, with an optimum pH of 7, and within the temperature range of 35 to 55°C. The purified lipase exhibited not only stable but enhanced maximal activity by Triton X100. The enzyme activity of Brevibacterium halotolerans PS4 lipase was enhanced by Ca 2+ and Mg 2+ . SDS and metal ions such as Hg 2+ , Zn 2+ , Cu 2+ , Ag 2+ and Fe 2+ decreased the lipase activity remarkedly. The extracellular lipase from orchard soil isolate was further applied for its application as laundary additives.

Alkaline proteases from a newly isolated Micromonospora chaiyaphumensis S103: Characterization and application as a detergent additive and for chitin extraction from shrimp shell waste

The present study was undertaken to characterize the extracellular thermostable serine alkaline proteases from newly actinomycete strain Micromonospora chaiyaphumensis S103 and to describe their evaluation in commercial detergents and shrimp waste deproteinization. This proteolytic crude extract was active and stable in alkaline solution. It was extremely stable in the pH range of 5.0–12.0. The optimum pH and temperature were 8.0 and 70°C, respectively, using casein as a substrate. The thermoactivity and thermostability of proteases were enhanced by the addition of 5mM Ca2+. Proteases from S103 were also used for shrimp wastes deproteinization in the process of chitin preparation. The percent of protein removal after 3h hydrolysis at 45°C with an enzyme/substrate ratio of 20U/mg had reached 93%. Furthermore, S103 crude enzyme was stable towards several organic solvents and retained 100% of its original activity after 90days of incubation in the presence of methanol, hexane, acetone, and DMSO. These properties make S103 proteases an ideal choice for application in detergent formulations, chitin production, and enzymatic peptide synthesis.

Evaluation of a novel thermo-alkaline Staphylococcus aureus lipase for application in detergent formulations.

An extracellular lipase of a newly isolated S. aureus strain ALA1 (SAL4) was purified from the optimized culture medium. The SAL4 specific activity determined at 60 °C and pH 12 by using olive oil emulsion or TC4, reached 7215 U/mg and 2484 U/mg, respectively. The 38 NH2-terminal amino acid sequence of the purified enzyme starting with two extra amino acid residues (LK) was similar to known staphylococcal lipase sequences. This novel lipase maintained almost 100% and 75% of its full activity in a pH range of 4.0–12 after a 24 h incubation or after 0.5 h treatment at 70 °C, respectively. Interestingly, SAL4 displayed appreciable stability toward oxidizing agents, anionic and non-ionic surfactants in addition to its compatibility with several commercial detergents. Overall, these interesting characteristics make this new lipase promising for its application in detergent industry.

Characterization of a novel protease from Aeribacillus pallidus strain VP3 with potential biotechnological interest

The present study investigates the purification and physico-chemical characterization of an extracellular protease from the Aeribacillus pallidus strain VP3 previously isolated from a geothermal oil-field (Sfax, Tunisia). The maximum protease activity recorded after 22h of incubation at 45°C was 3000U/ml. Pure enzyme, designated as SPVP, was obtained after ammonium sulfate fractionation (40–60%)-dialysis followed by heat-treatment (70°C for 30min) and UNO Q-6 FPLC anion-exchange chromatography. The purified enzyme is a monomer of molecular mass about 29kDa. The sequence of the 25 NH2-terminal residues of SPVP showed a high homology with those of Bacillus proteases. The almost complete inhibition by PMSF and DIFP confirmed that SPVP is a member of serine protease family. Its optima of pH and temperature were pH 10 and 60°C, respectively. Its half-life times at 70 and 80°C were 8 and 4h, respectively. Its catalytic efficiency was higher than those of SAPCG, Alcalase Ultra 2.5L, and Thermolysin type X. SPVP exhibited excellent stability to detergents and wash performance analysis revealed that it could remove blood-stains effectively and high resistance against organic solvents. These properties make SPVP a potential candidate for applications in detergent formulations and non-aqueous peptide biocatalysis.

An organic solvent-stable lipase from a newly isolated Staphylococcus aureus ALA1 strain with potential for use as an industrial biocatalyst.

In this study, a new strain, ALA1, was identified as Staphylococcus aureus by biochemical tests, and its 16S ribosomal DNA sequence was isolated from dromedary milk. ALA1 lipase production was optimized in shake flask experiments and measured with varying pH (3-11), temperature (20-55°C) and substrate concentrations. The maximum lipase production was recorded at pH 8 and 30°C for up to 30H of culture period for the S. aureus ALA1 strain. Among the substrates tested, selected carbon sources, xylose, nitrogen source, yeast extract, and olive oil (1%) were suitable for maximizing lipase production. The effects of surfactants were investigated and showed that Tween 20, Tween 80, and Triton X-100 prevented lipase production. Interestingly, isolate ALA1 was able to grow in high concentrations of benzene or toluene (up to 50% (v/v)). Moreover, the lipolytic activity of the S. aureus ALA1 lipase was stimulated by diethyl ether, whereas almost 100% of S. aureus ALA1 lipase activity was retained in 25% acetone, acetonitrile, benzene, 2-propanol, ethanol, methanol, or toluene. Because of its stability in organic solvent, the S. aureus ALA1 lipase was used as a biocatalyst to synthesize high levels of added value molecules. S. aureus ALA1 lipase could be considered as an ideal choice for applications in detergent formulations because of its high stability and compatibility with various surfactants, oxidizing agents, and commercial detergents.

A novel detergent-stable solvent-tolerant serine thiol alkaline protease from Streptomyces koyangensis TN650

An alkaline proteinase (STAP) was produced from strain TN650 isolated from a Tunisian off-shore oil field and assigned as Streptomyces koyangensis strain TN650 based on physiological and biochemical properties and 16S rRNA gene sequencing. Matrix assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF/MS) analysis revealed that the purified enzyme was a monomer with a molecular mass of 45125.17-Da. The enzyme had an NH2-terminal sequence of TQSNPPSWGLDRIDQTTAFTKACSIKY, thus sharing high homology with those of Streptomyces proteases. The results showed that this protease was completely inhibited by phenylmethanesulfonyl fluoride (PMSF), diiodopropyl fluorophosphates (DFP), and partially inhibited by 5,5-dithio-bis-(2-nitro benzoic acid) (DTNB), which strongly suggested its belonging to the serine thiol protease family. Using casein as a substrate, the optimum pH and temperature values for protease activity were pH 10 and 70°C, respectively. The protease was stable at pH 7–10 and 30–60°C for 24h. STAP exhibited high catalytic efficiency, significant detergent stability, and elevated organic solvent resistance compared to the SG-XIV proteases from S. griseus and KERAB from Streptomyces sp. AB1. The stap gene encoding STAP was isolated, and its DNA sequence was determined. These properties make STAP a potential candidate for future application in detergent formulations and non-aqueous peptide biocatalysis.

&amp;lt;i&amp;gt;Arthrobacter arilaitensis&amp;lt;/i&amp;gt; Re117 as a Source of Solvent-Stable Proteases: Production, Characteristics, Potential Application in the Deproteinization of Shrimp Wastes and Evaluation in Liquid Laundry Commercial Detergents

The present study describes the characterization of crude protease extract from Arthrobacter arilaitensis Re117 and its evaluation in solid and liquid detergent. One caseinolytic protease clear band was observed in zymogram. The crude alkaline protease showed optimum activity at pH 9.0 and 50&degC, and it was highly stable over a wide range of pH from 8.0 to 9.0. Proteolytic enzymes showed extreme stability towards non-ionic surfactants (Tween 80, Tween 20 and Triton X-100) and stimulate activity towards oxidizing agents such as sodium perborate. They also showed high stability and compatibility with various laundry solid detergents from Tunisian market. The protease of A. arilaitensis Re117, was also tested for shrimp waste deproteinization to produce chitin. The protein removal with a ratio E/S of 20 was about 83%. The novelties of the Re117 protease include its high stability to organic solvents and surfactants. These unique properties make it an ideal choice for application in detergent formulations and enzymatic peptide synthesis. In addition, the enzyme may find potential applications in the deproteinization of shrimp wastes to produce chitin.

Biochemical and molecular characterization of a thermo- and detergent-stable alkaline serine keratinolytic protease from Bacillus circulans strain DZ100 for detergent formulations and feather-biodegradation process

An extracellular keratinolytic protease (SAPDZ) was produced and purified from a newly isolated Bacillus circulans strain DZ100. Matrix assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF/MS) analysis revealed that the purified enzyme is a monomer with a molecular mass of 32019.10 Da. The sequence of the 25 N-terminal residues of SAPDZ showed high homology with those of Bacillus proteases. Optimal activity was achieved at pH 12.5 and 85 °C. This enzyme was completely inhibited by phenylmethanesulfonyl fluoride (PMSF) and diiodopropyl fluorophosphates (DFP), which suggests that it belongs to the serine protease family. Compared to the other tested proteases, SAPDZ exhibited broader substrate specificity, higher levels of catalytic efficiency, and greater keratinolytic activity, which made it able to accomplish the entire feather-biodegradation process on its own. The sapDZ gene encoding SAPDZ was cloned, sequenced, and expressed in Escherichia coli. The biochemical properties exhibited by the extracellular purified recombinant enzyme (rSAPDZ) were similar to those of the native one. Above all, SAPDZ exhibited marked stability to detergents, making it a potential candidate for future applications in detergent formulations and an efficient eco-friendly enzyme for the biodegradation of feather keratin.

A newly high alkaline lipase: an ideal choice for application in detergent formulations.

BackgroundBacterial lipases received much attention for their substrate specificity and their ability to function in extreme environments (pH, temperature...). Many staphylococci produced lipases which were released into the culture medium. Reports of thermostable lipases from Staphylococcus sp. and active in alkaline conditions are not previously described.ResultsA newly soil-isolated Staphylococcus sp. strain ESW secretes an induced lipase in the culture medium. The effects of temperature, pH and various components in a detergent on the activity and stability of Staphylococcus sp. lipase (SL1) were studied in a preliminary evaluation for use in detergent formulation solutions. The enzyme was highly active over a wide range of pH from 9.0 to 13.0, with an optimum at pH 12.0. The relative activity at pH 13.0 was about 60% of that obtained at pH 12.0. It exhibited maximal activity at 60°C. This novel lipase, showed extreme stability towards non-ionic and anionic surfactants after pre-incubation for 1 h at 40°C, and relative stability towards oxidizing agents. Additionally, the crude enzyme showed excellent stability and compatibility with various commercial solid and liquid detergents.ConclusionsThese properties added to the high activity in high alkaline pH make this novel lipase an ideal choice for application in detergent formulations.

Purification and characterization of a thermostable keratinolytic serine alkaline proteinase from Streptomyces sp. strain AB1 with high stability in organic solvents

A keratinolytic alkaline proteinase (KERAB) was isolated from Streptomyces sp. strain AB1. Based on MALDI-TOF mass spectrometry analysis, the purified enzyme is a monomer with a molecular mass of 29850.17 Da. The NH 2-terminal sequence of the enzyme was determined to be TQANPPSWGLDDIDQTAL. This keratinase was completely inhibited by phenylmethanesulfonyl fluoride (PMSF) and diiodopropyl fluorophosphates (DIFP), which suggests that it belongs to the serine protease family. Using keratin azure as a substrate, the optimum pH and temperature values for keratinase activity were pH 11.5 and 75 °C, respectively. This keratinase was stable between 30 and 60 °C and pH 4 and 11 for 4 and 96 h, respectively, and thermoactivity and thermostability were enhanced in the presence of 5 mM Mg 2+. Its catalytic efficiency was higher than those of SAPB-L31I/T33S/N99Y, nattokinase and subtilisin Carlsberg. KERAB exhibited stability to detergents and high resistance against organic solvents and was able to degrade feathers completely. These properties make KERAB a potential candidate for future applications in detergent formulations, dehairing during leather processing, and non-aqueous peptide biocatalysis.

A Novel Serine Metallokeratinase from a Newly Isolated Bacillus pumilus A1 Grown on Chicken Feather Meal: Biochemical and Molecular Characterization

A keratinolytic enzyme (KerA1) secreted by a newly isolated Bacillus pumilus strain A1 cultivated in medium containing chicken feather meal was purified and characterized, and the gene was isolated and sequenced. The molecular mass of the purified enzyme was estimated to be 34,000 Da by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis and gel filtration. The optimum pH and temperature for the purified keratinase were 9.0 and 60 degrees C, respectively, using keratin as a substrate. KerA1 showed a high stability towards nonionic surfactants. It was found to be relatively stable toward the strong anionic surfactant (SDS). The deduced amino acid sequence of the keratinase KerA1 differs from both the organic solvent tolerant protease of B. pumilus 115b and the dehairing protease of B. pumilus UN-31-C-42 by one and nine amino acids, respectively. These results suggest that this keratinase may be a useful alternative and ecofriendly route for handling the abundant amount of waste feathers and for applications in detergent formulations.

Optimization of process parameters for the production of alkaline protease from Penicillium godlewskii SBSS 25 and its application in detergent industry

An investigation was carried out on alkaline protease production using solid state fermentation from Penicillium godlewskii SBSS 25 isolated from soil samples collected from Southern Kerala, India and its application as a detergent additive. The maximum protease yield (235 U/gds) were achieved with optimized process parameters like pH (9.0), temperature (35°C), moisture content (60%), nitrogen source (0.5% NH4NO3), carbon source (4% glucose) and incubation time (96 h). The enzyme showed stability with a wide range of commercial detergents. These properties make this protease an ideal choice for application in detergent formulations. Key words: Extracellular, alkaline protease, Penicillium godlewskii, optimization, soil, fermentation.