Identification of a novel protease from the thermophilic Anoxybacillus kamchatkensis M1V and its application as laundry detergent additive

Mechri, Sondes; Bouacem, Khelifa; Jaouadi, Nadia Zaraî; Rekik, Hatem; Elhoul, Mouna Ben; Benmrad, Maroua Omrane; Hacène, Hocine; Béjar, Samír; Bouanane‐Darenfed, Amel; Jaouadi, Bassem

doi:10.1007/s00792-019-01123-6

Cited by 40 publications

(22 citation statements)

References 61 publications

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“…All strains have been previously reported as extracellular proteases producers. However, they did not show any chitinase activity [19][20][21].…”

Section: Microorganismsmentioning

confidence: 86%

“…Aeribacillus pallidus VP3 and Lysinibacillus fusiformis C250R were isolated from the production water of the oilfields yna Petroleum Services (TPS), Sfax, Tunisia [17,18]. Anoxybacillus kamchatkensis M1V was isolated from the Hammam Righa geothermal waters in Algeria [19]. All strains have been previously reported as extracellular proteases producers.…”

Section: Microorganismsmentioning

confidence: 99%

“…A maximum protease activity of 2,000 U/mL was obtained with 25 g/L shrimp waste. e VP3 and C250R strains also produce large amounts of proteases activity in the order of 600 and 200 U/mL (Mechri et al [13,19], submitted for publication), respectively. Bacillus licheniformis RP1 was shown to produce proteases (1,400 U/ mL) when grown in media containing shrimp wastes powder as carbon and nitrogen source, indicating that this bacteria could obtain its needs directly from shrimp by-product [28].…”

Section: Production Of Proteases In Economical Mediummentioning

confidence: 99%

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Statistical Experimental Design Optimization of Microbial Proteases Production under Co-Culture Conditions for Chitin Recovery from Speckled ShrimpMetapenaeus monocerosBy-Product

Jabeur

Mechri

Kriaa

et al. 2020

BioMed Research International

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This study was designed with the aim to produce microbial proteases in presence of speckled shrimp by-product. For this reason, three strains belonging to Bacillus genus, namely, Aeribacillus pallidus VP3, Lysinibacillus fusiformis C250R, and Anoxybacillus kamchatkensis M1V were studied under co-culture procedure. A Taguchi L27 experimental design was applied to optimize the co-culture parameters. The experimental design was built with 9 factors (by-product powder concentration, the pH of the medium, the temperature, the sucrose concentration, the agitation speed, the inoculum sizes of VP3, M1V, and C250R strains, and the culture volume) at three different levels. The obtained results showed that a total protease activity of 8,182 U/mL could be achieved after 24 h of incubation in presence of 20 g/L shrimp by-product and 10 g/L sucrose, at an initial pH of 7, a 40°C temperature and absorbance, at 600 nm, of inoculum sizes of 0.1, 0.3, and 0.1 for VP3, M1V, and C250R strains, respectively. The agitation was set at 200 rpm, and the final volume was 25 mL. Taguchi’s design allowed the identification of temperature, the inoculum size for strain VP3, the inoculum size for strain M1V, and the final culture volume as the most influencing variables. A Box–Behnken design with 27 experiments was carried out for the optimization of these four selected factors. Following such design, the highest protease production reached was 11,300 U/mL. This yield was obtained in a final culture volume of 15 mL containing 20 g/L shrimp by-product powder and 10 g/L sucrose and inoculated with VP3, C250R, and M1V strains at 0.05, 0.1, and 0.2, respectively. The flasks were incubated at 45°C for 24 h with shaking at 200 rpm. The efficiency of chitin extraction by co-cultivation was investigated under the latter conditions. The chitin yield from shells by-product was 16.7%. Fourier-Transform Infrared (FTIR) analysis of the obtained chitin displayed characteristic profiles similar to that of the commercial α-chitin.

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“…All strains have been previously reported as extracellular proteases producers. However, they did not show any chitinase activity [19][20][21].…”

Section: Microorganismsmentioning

confidence: 86%

Section: Microorganismsmentioning

confidence: 99%

Section: Production Of Proteases In Economical Mediummentioning

confidence: 99%

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Statistical Experimental Design Optimization of Microbial Proteases Production under Co-Culture Conditions for Chitin Recovery from Speckled ShrimpMetapenaeus monocerosBy-Product

Jabeur

Mechri

Kriaa

et al. 2020

BioMed Research International

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“…The enzyme (5 µg/ml) was pre-incubated at 40 • C for 1 h or at 30 • C for 24 h in buffer B containing 1.0% of the detergent. Thereafter, the residual activity of the enzyme against N,N-dimethylated casein (Sigma) was determined according to the method of Mechri et al (2019), except that the reaction was carried out at 60 • C for 30 min in buffer B.…”

Section: Effects Of Surfactants Oxidizing Agent Organic Solvents Anmentioning

confidence: 99%

Extracellular Production, Characterization, and Engineering of a Polyextremotolerant Subtilisin-Like Protease From Feather-Degrading Thermoactinomyces vulgaris Strain CDF

et al. 2020

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Here, the gene encoding a subtilisin-like protease (protease Als) was cloned from Thermoactinomyces vulgaris strain CDF and expressed in Escherichia coli. The recombinant enzyme was released into the culture medium of E. coli as a mature form (mAls). Purified mAls displayed optimal activity at 60–70°C and pH 10.0 using azo-casein as the substrate, and showed a half-life of 13.8 h at 70°C. Moreover, the activity of thermostable mAls was comparable to or higher than those of mesophilic subtilisin Carlsberg and proteinase K at low temperatures (10–30°C). Protease Als was also stable in several organic solvents and showed high compatibility with commercial laundry detergents. Notably, mAls exhibited approximately 100% of its activity at 3 M NaCl, and showed enhanced thermostability with the increase of NaCl concentration up to 3 M. Protease Als possesses an excess of solvent-accessible acidic amino acid residues, which may account for the high halotolerance of the enzyme. Compared with homologous protease C2 from the same strain, protease Als exhibits substantially lower activity toward insoluble keratin substrates but efficiently hydrolyzes soluble keratin released from chicken feathers. Additionally, direct substitution of the substrate-binding site of protease Als with that of protease C2 improves its activity against insoluble keratin substrates. By virtue of its polyextremotolerant attribute and kerationolytic capacity, protease Als may find broad applications in various industries such as laundry detergents, food processing, non-aqueous biocatalysis, and feather processing.

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“…In common with all enzymes, external factors such as type of media, pH, and temperature are important for the catalytic efficiency, activity, stability, and proper functioning of proteases [14]. Therefore, the search for novel alkaline-stable and thermostable peptidases from extremophilic microorganisms and the engineering of the already available enzymes have been the major areas of research in this field over the years [15, 16]. Valuable characteristics of peptidases from polyextremophiles and their applications are gathered from a wide literature survey [17–19].…”

Section: Introductionmentioning

confidence: 99%

Identification of a New Serine Alkaline Peptidase from the Moderately Halophilic Virgibacillus natechei sp. nov., Strain FarD^T and its Application as Bioadditive for Peptide Synthesis and Laundry Detergent Formulations

Mechri

Bouacem

Amziane

et al. 2019

BioMed Research International

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A new peptidase designated as SAPV produced from a moderately halophilic Virgibacillus natechei sp. nov., strain FarDT was investigated by purification to homogeneity followed by biochemical and molecular characterization purposes. Through optimization, it was determined that the optimum peptidase activity was 16,000 U/mL. It was achieved after 36 h incubation at 35°C in the optimized enzyme liquid medium (ELM) at pH 7.4 that contains only white shrimp shell by-product (60 g/L) as sole energy and carbon sources. The SAPV enzyme is a monomer protein with a molecular mass of 31 kDa as estimated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and high-performance liquid chromatography (HPLC) gel filtration chromatography. The sequence of its NH2-terminal amino-acid residues showed homology with those of Bacillus peptidases S8/S53 superfamily. The SAPV showed optimal activity at pH 9 and 60°C. Irreversible inhibition of enzyme activity by diiodopropyl fluorophosphates (DFP) and phenylmethanesulfonyl fluoride (PMSF) confirmed its belonging to the serine peptidases. Considering its interesting biochemical characterization, the sapV gene was cloned, sequenced, and heterologously overexpressed in the extracellular fraction of E. coli BL21(DE3)pLysS. The biochemical properties of the recombinant peptidase (rSAPV) were similar to those of the native one. The highest sequence identity value (97.66%) of SAPV was obtained with peptidase S8 from Virgibacillus massiliensis DSM 28587, with 9 amino-acid residues of difference. Interestingly, rSAPV showed an outstanding and high resistance to several organic solvents than SPVP from Aeribacillus pallidus VP3 and Thermolysin type X. Furthermore, rSAPV exhibited an excellent detergent stability and compatibility than Alcalase 2.4 L FG and Bioprotease N100L. Considering all these remarkable properties, rSAPV has attracted the interest of industrialists.

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Identification of a novel protease from the thermophilic Anoxybacillus kamchatkensis M1V and its application as laundry detergent additive

Cited by 40 publications

References 61 publications

Statistical Experimental Design Optimization of Microbial Proteases Production under Co-Culture Conditions for Chitin Recovery from Speckled ShrimpMetapenaeus monocerosBy-Product

Statistical Experimental Design Optimization of Microbial Proteases Production under Co-Culture Conditions for Chitin Recovery from Speckled ShrimpMetapenaeus monocerosBy-Product

Extracellular Production, Characterization, and Engineering of a Polyextremotolerant Subtilisin-Like Protease From Feather-Degrading Thermoactinomyces vulgaris Strain CDF

Identification of a New Serine Alkaline Peptidase from the Moderately Halophilic Virgibacillus natechei sp. nov., Strain FarD^T and its Application as Bioadditive for Peptide Synthesis and Laundry Detergent Formulations

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Identification of a novel protease from the thermophilic Anoxybacillus kamchatkensis M1V and its application as laundry detergent additive

Cited by 40 publications

References 61 publications

Statistical Experimental Design Optimization of Microbial Proteases Production under Co-Culture Conditions for Chitin Recovery from Speckled ShrimpMetapenaeus monocerosBy-Product

Statistical Experimental Design Optimization of Microbial Proteases Production under Co-Culture Conditions for Chitin Recovery from Speckled ShrimpMetapenaeus monocerosBy-Product

Extracellular Production, Characterization, and Engineering of a Polyextremotolerant Subtilisin-Like Protease From Feather-Degrading Thermoactinomyces vulgaris Strain CDF

Identification of a New Serine Alkaline Peptidase from the Moderately Halophilic Virgibacillus natechei sp. nov., Strain FarDT and its Application as Bioadditive for Peptide Synthesis and Laundry Detergent Formulations

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Identification of a New Serine Alkaline Peptidase from the Moderately Halophilic Virgibacillus natechei sp. nov., Strain FarD^T and its Application as Bioadditive for Peptide Synthesis and Laundry Detergent Formulations