Exoproduction and Biochemical Characterization of a Novel Serine Protease from Ornithinibacillus caprae L9T with Hide-Dehairing Activity
0
조회
0
다운로드
0
인용
0
참고문헌
키워드
초록
This study is the first report on production and characterization of the enzyme from an Ornithinibacillus species. A 4.2-fold increase in the extracellular protease (called L9T) production from Ornithinibacillus caprae L9T was achieved through the one-factor-at-a-time approach and response surface methodological optimization. L9T protease exhibited a unique protein band with a mass of 25.9 kDa upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis. This novel protease was active over a range of pH (4–13), temperatures (30–80oC) and salt concentrations (0– 220 g/l), with the maximal activity observed at pH 7, 70oC and 20 g/l NaCl. Proteolytic activity was upgraded in the presence of Ag+, Ca2+ and Sr2+, but was totally suppressed by 5 mM phenylmethylsulfonyl fluoride, which suggests that this enzyme belongs to the serine protease family. L9T protease was resistant to certain common organic solvents and surfactants; particularly, 5 mM Tween 20 and Tween 80 improved the activity by 63 and 15%, respectively. More importantly, L9T protease was found to be effective in dehairing of goatskins, cowhides and rabbit-skins without damaging the collagen fibers. These properties confirm the feasibility of L9T protease in industrial applications, especially in leather processing.
Abstract
This study is the first report on production and characterization of the enzyme from an Ornithinibacillus species. A 4.2-fold increase in the extracellular protease (called L9T) production from Ornithinibacillus caprae L9T was achieved through the one-factor-at-a-time approach and response surface methodological optimization. L9T protease exhibited a unique protein band with a mass of 25.9 kDa upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis. This novel protease was active over a range of pH (4–13), temperatures (30–80oC) and salt concentrations (0– 220 g/l), with the maximal activity observed at pH 7, 70oC and 20 g/l NaCl. Proteolytic activity was upgraded in the presence of Ag+, Ca2+ and Sr2+, but was totally suppressed by 5 mM phenylmethylsulfonyl fluoride, which suggests that this enzyme belongs to the serine protease family. L9T protease was resistant to certain common organic solvents and surfactants; particularly, 5 mM Tween 20 and Tween 80 improved the activity by 63 and 15%, respectively. More importantly, L9T protease was found to be effective in dehairing of goatskins, cowhides and rabbit-skins without damaging the collagen fibers. These properties confirm the feasibility of L9T protease in industrial applications, especially in leather processing.
참고문헌 (47)
- Kandasamy N, "Eco-benign enzymatic dehairing of goatskins utilizing a protease from a Pseudomonas fluorescens species isolated from fish visceral waste", J. Clean. Prod, 25, pp.27~33 (2012)
- Ockerman HW, "BY-PRODUCTS | Hides and Skins. In Dikeman M, Devine C(eds. )", pp.112~124 (2014), Academic Press
- Kanagaraj J, "Eco-friendly waste management strategies for greener environment towards sustainable development in leather industry : A comprehensive review", J. Clean. Prod, 89, pp.1~17 (2015)
- Thanikaivelan P, "Progress and recent trends in biotechnological methods for leather processing", Trends Biotechnol, 22, pp.181~188 (2004)
- Paul T, "Bacterial keratinolytic protease, imminent starter for nextgen leather and detergent industries", Sustain. Chem. Pharm, 3, pp.8~22 (2016)
- Ghafoori H, "Purification and characterization of an extracellular haloalkaline serine protease from the moderately halophilic bacterium, Bacillus iranensis(X5B)", Extremophiles, 20, pp.115~123 (2016)
- Barzkar N, "Marine microbial alkaline protease : an efficient and essential tool for various industrial applications", Int. J. Biol. Macromol, 161, pp.1216~1229 (2020)
- Gradisar H, "Similarities and specificities of fungal keratinolytic proteases : comparison of keratinases of Paecilomyces marquandii and Doratomyces microsporus to some known proteases", Appl. Environ. Microbiol, 71, pp.3420~3426 (2005)
- Dettmer A, "Environmentally friendly hide unhairing : enzymatic hide processing for the replacement of sodium sulfide and delimig", J. Clean. Prod, 47, pp.11~18 (2013)
- Sun F, "Purification and biochemical characteristics of the microbial extracellular protease from Lactobacillus curvatus isolated from Harbin dry sausages", Int. J. Biol. Macromol, 133, pp.987~997 (2019)
- Sharma AK, "Biochemical, thermodynamic and structural characteristics of a biotechnologically compatible alkaline protease from a haloalkaliphilic, Nocardiopsis dassonvillei OK-18", Int. J. Biol. Macromol, 153, pp.680~696 (2020)
- Ben Elhoul M, "A novel detergent-stable solventtolerant serine thiol alkaline protease from Streptomyces koyangensis TN650", Int. J. Biol. Macromol, 79, pp.871~882 (2015)
- Brandelli A, "Bacterial keratinases : useful enzymes for bioprocessing agroindustrial wastes and beyond", Food Bioprocess Tech, 1, pp.105~116 (2007)
- Zarai Jaouadi N, "Biochemical and molecular characterization of a serine keratinase from Brevibacillus brevis US575 with promising keratin-biodegradation and hide-dehairing activities", PLoS One, 8, pp.e76722~ (2013)
- Kostyleva EV, "A new Bacillus licheniformis mutant strain producing serine protease efficient for hydrolysis of soy meal proteins", Microbiology, 85, pp.462~470 (2016)
- Jagadeesan Y, "Sustainable production, biochemical and molecular characterization of thermo-and-solvent stable alkaline serine keratinase from novel Bacillus pumilus AR57 for promising poultry solid waste management", Int. J. Biol. Macromol, 163, pp.135~146 (2020)
- Haddar A, "Two detergent stable alkaline serine-proteases from Bacillus mojavensis A21 : purification, characterization and potential application as a laundry detergent additive", Bioresour. Technol, 100, pp.3366~3373 (2009)
- Pillai P, "Hide depilation and feather disintegration studies with keratinolytic serine protease from a novel Bacillus subtilis isolate", Appl. Microbiol. Biotechnol, 78, pp.643~650 (2008)
- Zhang RX, "Biochemical characterization of a novel surfactant-stable serine keratinase with no collagenase activity from Brevibacillus parabrevis CGMCC 10798", Int. J. Biol. Macromol, 93, pp.843~851 (2016)
- Parte AC, "List of prokaryotic names with standing in nomenclature(LPSN)moves to the DSMZ", Int. J. Syst. Evol. Microbiol, 70, pp.5607~5612 (2020)
- Xiaoguang Li, "Ornithinibacillus caprae sp. nov., a moderate halophile isolated from the hides of a white goat", Archives of Microbiology, 202(6), pp.1469~1476 (2020), Springer Science and Business Media LLC[DOI]
- Meier-KolthoffJP, "TYGS is an automated high-throughput platform for state-of-the-art genome-based taxonomy", Nat. Commun, 10, pp.2182~ (2019)
- Weizhong Li, "Tolerating some redundancy significantly speeds up clustering of large protein databases", Bioinformatics, 18(1), pp.77~82 (2002), Oxford University Press (OUP)[DOI]
- State dministration for Quality Supervision and Inspection and Quarantine of the People’s Republic of China, "The National Standardization Administration Commission GB", T 23527-2009, 2009
- U. K. LAEMMLI, "Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4", Nature, 227(5259), pp.680~685 (1970), Springer Science and Business Media LLC[DOI]
- Garciacarreno FL, "Substrate gel-electrophoresis for composition and molecular-weight of proteinases of proteinaceous proteinase-inhibitors", Anal. Biochem, 214, pp.65~69 (1993)
- Li Y, "Diversity of cultivable protease-producing bacteria in Laizhou Bay sediments, Bohai Sea, China", Front. Microbiol, 8, pp.405~ (2017)
- Pandey S, "Catalysis and stability of an alkaline protease from a haloalkaliphilic bacterium under non-aqueous conditions as a function of pH, salt and temperature", J. Biosci. Bioeng, 114, pp.251~256 (2012)
- Thanapun T, "Screening and characterization of protease-producing Virgibacillus, Halobacillus and Oceanobacillus strains from Thai fermented fish", J. Appl. Pharm. Sci, 3, pp.025~030 (2013)
- Rohban R, "Screening and isolation of halophilic bacteria producing extracellular hydrolyses from Howz Soltan Lake, Iran", J. Ind. Microbiol. Biotechnol, 36, pp.333~340 (2009)
- Seghal Kiran G, "A halotolerant thermostable lipase from the marine bacterium Oceanobacillus sp", PUMB02 with an ability to disrupt bacterial biofilms. Bioengineered, 5, pp.305-318~ (2014)
- Aihua Deng, "Purification and characterization of a surfactant-stable high-alkaline protease from Bacillus sp. B001", Bioresource Technology, 101(18), pp.7100~7106 (2010), Elsevier BV[DOI]
- Abdelnasser S. S. Ibrahim, "Detergent-, solvent- and salt-compatible thermoactive alkaline serine protease from halotolerant alkaliphilic Bacillus sp. NPST-AK15: purification and characterization", Extremophiles, 19(5), pp.961~971 (2015), Springer Science and Business Media LLC[DOI]
- Darwesh OM, "Enzymes immobilization onto magnetic nanoparticles to improve industrial and environmental applications", Methods Enzymol, 630, pp.481~502 (2020)
- Gong JS, "Biochemical characterization of an extreme alkaline and surfactantstable keratinase derived from a newly isolated actinomycete Streptomyces aureofaciens K13", Rsc. Adv, 5, pp.24691~24699 (2015)
- Tork SE, "Production and characterization of thermostable metallokeratinase from newly isolated Bacillus subtilis NRC 3", Int. J. Biol. Macromol, 55, pp.169~175 (2013)
- El-Khonezya MI, "Detergent stable thiol-dependant alkaline protease produced from the endophytic fungus Aspergillus ochraceus BT21 : purification and kinetics", Biocatal. Agric. Biotechnol, 35, pp.102046~ (2021)
- Patil U, "Purification and characterization of solvent-tolerant, thermostable, alkaline metalloprotease from alkalophilic Pseudomonas aeruginosa MTCC 7926", J. Chem. Technol. Biotechnol, 84, pp.1255~1262 (2009)
- Maruthiah T, "Deproteinization potential and antioxidant property of haloalkalophilic organic solvent tolerant protease from marine Bacillus sp. APCMST-RS3 using marine shell wastes", Biotechnol. Rep, 8, pp.124~132 (2015)
- Suwannaphan S, "A serine protease from newly isolated Bacillus sp. for efficient silk degumming, sericin degrading and colour bleaching activities", Int. Biodeter. Biodegr, 117, pp.141~149 (2017)
- Gegeckas A, "Characterization and application of keratinolytic paptidases from Bacillus spp", Int. J. Biol. Macromol, 113, pp.1206~1213 (2018)
- Ben Elhoul M, "Biochemical and molecular characterization of new keratinoytic protease from Actinomadura viridilutea DZ50", Int. J. Biol. Macromol, 92, pp.299~315 (2016)
- Jaouadi B, "Purification and characterization of a thermostable keratinolytic serine alkaline proteinase from Streptomyces sp. strain AB1 with high stability in organic solvents", Bioresour. Technol, 1, pp.8361-8369~ (2010)
- Jellouli K, "Molecular and biochemical characterization of an extracellular serine-protease from Vibrio metschnikovii J1", J. Ind. Microbiol. Biotechnol, 36, pp.939~948 (2009)
- Sujitha P, "Enzymatic dehairing: a comprehensive review on the mechanistic aspects with emphasis on enzyme specificity", Int. J. Biol. Macromol, 118, pp.168~179 (2018)
- Yates JR, "Studies in depilation", J. Soc. Leather Trades Chem, 56, pp.158~177 (1972)[DOI]
- Bouacem K, "Novel serine keratinase from Caldicoprobacter algeriensis exhibiting outstanding hide dehairing abilities", Int. J. Biol. Macromol, 86, pp.321~328 (2016)
