메뉴 건너뛰기




Volumn 99, Issue 6, 2008, Pages 1939-1944

Production of alkaline protease by Pseudomonas aeruginosa using proteinaceous solid waste generated from leather manufacturing industries

Author keywords

Alkaline protease; Amino acids; Animal fleshing (ANFL); Enzyme repression; P. aeruginosa

Indexed keywords

AMINO ACIDS; LEATHER; SOLID WASTES; SUBSTRATES;

EID: 37549038998     PISSN: 09608524     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biortech.2007.03.025     Document Type: Article
Times cited : (65)

References (41)
  • 2
    • 0025133027 scopus 로고
    • Regulation of protease production in Clostridium sporogenes
    • Allison C., and Macfarlane G.T. Regulation of protease production in Clostridium sporogenes. Appl. Environ. Microbiol. 56 (1990) 3485-3490
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 3485-3490
    • Allison, C.1    Macfarlane, G.T.2
  • 3
    • 37549008102 scopus 로고    scopus 로고
    • Analysis for Water and Waste Water and AWWA, 1985. American Water Works Association, Washington, DC.
  • 4
    • 0042632697 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of tannery fleshings using chicken intestine proteases
    • Annapurna Raju A., Rose C., and Muralidhara Rao N. Enzymatic hydrolysis of tannery fleshings using chicken intestine proteases. Animal Feed Sci. Tech. 66 (1997) 139-147
    • (1997) Animal Feed Sci. Tech. , vol.66 , pp. 139-147
    • Annapurna Raju, A.1    Rose, C.2    Muralidhara Rao, N.3
  • 5
    • 37549020882 scopus 로고    scopus 로고
    • APHA, 1995. Standard Methods for the Examination of Water and Wastewater, 19 edition, New York.
  • 6
    • 0032100397 scopus 로고    scopus 로고
    • Processing of leather waste: pilot scale studies on chrome shavings. Isolation of potentially valuable protein products and chromium
    • Cabeza L.F., Taylor M.M., DiMaio G.L., Brown E.M., Marmer W.N., Carrio R., Celma P.J., and Cot J. Processing of leather waste: pilot scale studies on chrome shavings. Isolation of potentially valuable protein products and chromium. Waste Manag. 18 (1998) 211-218
    • (1998) Waste Manag. , vol.18 , pp. 211-218
    • Cabeza, L.F.1    Taylor, M.M.2    DiMaio, G.L.3    Brown, E.M.4    Marmer, W.N.5    Carrio, R.6    Celma, P.J.7    Cot, J.8
  • 7
    • 0002477183 scopus 로고
    • Production of a thermostable alkaline protease by a new Pseudomonas sp. by solid state fermentation
    • Chakraborthy R., and Srinivasan M. Production of a thermostable alkaline protease by a new Pseudomonas sp. by solid state fermentation. J. Microbiol. Biotechnol. 8 (1993) 7-16
    • (1993) J. Microbiol. Biotechnol. , vol.8 , pp. 7-16
    • Chakraborthy, R.1    Srinivasan, M.2
  • 8
    • 0023406986 scopus 로고
    • Effect of hydrophobicity of utilization of peptides by ruminal bacteria invitro
    • Chen G., Strobel H.J., Russell J.B., and Sniffen C.J. Effect of hydrophobicity of utilization of peptides by ruminal bacteria invitro. Appl. Environ. Microbiol. 53 (1987) 2021-2025
    • (1987) Appl. Environ. Microbiol. , vol.53 , pp. 2021-2025
    • Chen, G.1    Strobel, H.J.2    Russell, J.B.3    Sniffen, C.J.4
  • 9
    • 13844317084 scopus 로고    scopus 로고
    • A novel surfactant and oxidation stable alkaline protease Vibrio metschnikovii DL 33-51
    • Chengfang M., and Xiaolu J. A novel surfactant and oxidation stable alkaline protease Vibrio metschnikovii DL 33-51. Proc. Biochem. 40 (2005) 2167-2172
    • (2005) Proc. Biochem. , vol.40 , pp. 2167-2172
    • Chengfang, M.1    Xiaolu, J.2
  • 10
    • 0026928538 scopus 로고
    • Production and degradation of alkaline protease in batch cultures of Bacillus subtilis ATCC 14416
    • Chu I.M., Lee C., and Li T.S. Production and degradation of alkaline protease in batch cultures of Bacillus subtilis ATCC 14416. Enz. Microb. Technol. 14 (1992) 755-761
    • (1992) Enz. Microb. Technol. , vol.14 , pp. 755-761
    • Chu, I.M.1    Lee, C.2    Li, T.S.3
  • 12
    • 0041385610 scopus 로고    scopus 로고
    • Gelatin degradation at elevated temperature
    • Edith V.B., and Constant G. Gelatin degradation at elevated temperature. Int. J. Biol. Macromol. 32 (2003) 129-138
    • (2003) Int. J. Biol. Macromol. , vol.32 , pp. 129-138
    • Edith, V.B.1    Constant, G.2
  • 13
    • 0029948243 scopus 로고    scopus 로고
    • Thermostable alkaline proteases of Bacillus licheniformis MIR 29: isolation production and characterization
    • Ferrero M.A., Castro G.R., Abate C.M., Baigori M.D., and Sineriz F. Thermostable alkaline proteases of Bacillus licheniformis MIR 29: isolation production and characterization. Appl. Microbiol. Biotechnol. 45 (1996) 327-332
    • (1996) Appl. Microbiol. Biotechnol. , vol.45 , pp. 327-332
    • Ferrero, M.A.1    Castro, G.R.2    Abate, C.M.3    Baigori, M.D.4    Sineriz, F.5
  • 14
    • 0031253486 scopus 로고    scopus 로고
    • The use of nug meal as low cost substrates for the production of alkaline protease by the alkalophilic Bacillus sp. AR009 and some properties of the enzyme
    • Gessesse A. The use of nug meal as low cost substrates for the production of alkaline protease by the alkalophilic Bacillus sp. AR009 and some properties of the enzyme. Biores. Technol. 62 (1997) 59-61
    • (1997) Biores. Technol. , vol.62 , pp. 59-61
    • Gessesse, A.1
  • 16
    • 0036323668 scopus 로고    scopus 로고
    • Bacterial alkaline proteases: molecular approaches and industrial applications
    • Gupta R., Beg Q.K., and Lorenz P. Bacterial alkaline proteases: molecular approaches and industrial applications. Appl. Microbiol. Biotechnol. 59 (2002) 15-32
    • (2002) Appl. Microbiol. Biotechnol. , vol.59 , pp. 15-32
    • Gupta, R.1    Beg, Q.K.2    Lorenz, P.3
  • 17
    • 0021311770 scopus 로고
    • Effects of particle size on anaerobic digestion of tomato solid wastes
    • Hills D.J., and Nakamo K. Effects of particle size on anaerobic digestion of tomato solid wastes. Agric. Wastes 10 (1984) 285-295
    • (1984) Agric. Wastes , vol.10 , pp. 285-295
    • Hills, D.J.1    Nakamo, K.2
  • 18
    • 0034769629 scopus 로고    scopus 로고
    • Enhanced thermal stability of an alkaline protease AprP, isolated from a Pseudomonas sp. by mutation at an autoproteolysis site, Ser-331
    • Jang J.W., Jun H.K., Kim E.K., Jang W.H., Kang J.H., and Yoo O.J. Enhanced thermal stability of an alkaline protease AprP, isolated from a Pseudomonas sp. by mutation at an autoproteolysis site, Ser-331. Biotechnol Appl. Biochem. 34 (2001) 81-84
    • (2001) Biotechnol Appl. Biochem. , vol.34 , pp. 81-84
    • Jang, J.W.1    Jun, H.K.2    Kim, E.K.3    Jang, W.H.4    Kang, J.H.5    Yoo, O.J.6
  • 19
    • 0036137697 scopus 로고    scopus 로고
    • Pigeon pea waste as a novel, inexpensive, substrate for production of a thermostable alkaline protease from thermoalkalophilic Bacillus sp. JB-99
    • Johnvesly B., Manjunath B.R., and Naik G.R. Pigeon pea waste as a novel, inexpensive, substrate for production of a thermostable alkaline protease from thermoalkalophilic Bacillus sp. JB-99. Biores. Technol. 82 (2002) 61-64
    • (2002) Biores. Technol. , vol.82 , pp. 61-64
    • Johnvesly, B.1    Manjunath, B.R.2    Naik, G.R.3
  • 20
    • 9644265523 scopus 로고    scopus 로고
    • Production of protease from a new alkalophilic Bacillus sp. I-312 grown on soybean meal: optimization and some properties
    • Joo H.S., and Chang C.S. Production of protease from a new alkalophilic Bacillus sp. I-312 grown on soybean meal: optimization and some properties. Proc. Biochem. 40 (2005) 1263-1270
    • (2005) Proc. Biochem. , vol.40 , pp. 1263-1270
    • Joo, H.S.1    Chang, C.S.2
  • 21
    • 0032893415 scopus 로고    scopus 로고
    • An extracellular protease of Streptococcus gordonii hydrolyzes type IV collagen and collagen analogues
    • Juarez Z.E., and Stinson M.W. An extracellular protease of Streptococcus gordonii hydrolyzes type IV collagen and collagen analogues. Infect. Immun. 67 (1999) 271-278
    • (1999) Infect. Immun. , vol.67 , pp. 271-278
    • Juarez, Z.E.1    Stinson, M.W.2
  • 22
    • 0003659735 scopus 로고
    • Krieg N.R., and Holt J.G. (Eds), Williams and Wilkins, Baltimore, MD
    • In: Krieg N.R., and Holt J.G. (Eds). Bergey's Manual of Systematic Bacteriology (1984), Williams and Wilkins, Baltimore, MD
    • (1984) Bergey's Manual of Systematic Bacteriology
  • 23
    • 0037208123 scopus 로고    scopus 로고
    • The influence of post-mortem ageing and roasting on the microstructure, texture and collagen solubility of bovine semitendinosus muscle
    • Krystyna P. The influence of post-mortem ageing and roasting on the microstructure, texture and collagen solubility of bovine semitendinosus muscle. Meat Sci. 64 (2003) 191-198
    • (2003) Meat Sci. , vol.64 , pp. 191-198
    • Krystyna, P.1
  • 24
    • 0033572187 scopus 로고    scopus 로고
    • Microbial alkaline proteases: from a bioindustrial viewpoint
    • Kumar C.G., and Takagi H. Microbial alkaline proteases: from a bioindustrial viewpoint. Biotechnol. Adv. 17 (1999) 561-594
    • (1999) Biotechnol. Adv. , vol.17 , pp. 561-594
    • Kumar, C.G.1    Takagi, H.2
  • 25
    • 0031998258 scopus 로고    scopus 로고
    • Hydrolysis of tannery fleshings using pancreatic enzymes: a biotechnological tool for solid waste management
    • Kumaraguru S., Sastry T.P., and Rose C. Hydrolysis of tannery fleshings using pancreatic enzymes: a biotechnological tool for solid waste management. Am. Leather Chem. Assoc. 93 (1998) 32-39
    • (1998) Am. Leather Chem. Assoc. , vol.93 , pp. 32-39
    • Kumaraguru, S.1    Sastry, T.P.2    Rose, C.3
  • 26
    • 0028181795 scopus 로고
    • Extracellular alkaline protease from alkalophilic Vibrio metschnikovii strain RH 530
    • Kwon Y.T., Kim J.O., Moon S.Y., Lee H.H., and Rho H.M. Extracellular alkaline protease from alkalophilic Vibrio metschnikovii strain RH 530. Biotechnol. Lett. 16 (1994) 413-418
    • (1994) Biotechnol. Lett. , vol.16 , pp. 413-418
    • Kwon, Y.T.1    Kim, J.O.2    Moon, S.Y.3    Lee, H.H.4    Rho, H.M.5
  • 30
    • 0142216556 scopus 로고    scopus 로고
    • Towards zero discharge of chromium-containing leather waste through improved alkali hydrolysis
    • Mu C., Lin W., Zhang M., and Zhu Q. Towards zero discharge of chromium-containing leather waste through improved alkali hydrolysis. Waste Manag. 23 (2003) 835-843
    • (2003) Waste Manag. , vol.23 , pp. 835-843
    • Mu, C.1    Lin, W.2    Zhang, M.3    Zhu, Q.4
  • 31
    • 0034769033 scopus 로고    scopus 로고
    • Characterization and wash performance analysis of an SDS-stable alkaline protease from Bacillus sp.
    • Oberoi R., Beg Q.K., Puri S., Saxena R.K., and Gupta R. Characterization and wash performance analysis of an SDS-stable alkaline protease from Bacillus sp. World J. Microbiol. Biotechnol. 17 (2001) 493-497
    • (2001) World J. Microbiol. Biotechnol. , vol.17 , pp. 493-497
    • Oberoi, R.1    Beg, Q.K.2    Puri, S.3    Saxena, R.K.4    Gupta, R.5
  • 32
    • 33646822133 scopus 로고    scopus 로고
    • Green gram husk an inexpensive substrate for alkaline protease production by Bacillus sp. in solid-state fermentation
    • Prakasham R.S., Subba Rao Ch., and Sarma P.N. Green gram husk an inexpensive substrate for alkaline protease production by Bacillus sp. in solid-state fermentation. Biores. Technol. 97 (2006) 449-454
    • (2006) Biores. Technol. , vol.97 , pp. 449-454
    • Prakasham, R.S.1    Subba Rao, Ch.2    Sarma, P.N.3
  • 33
    • 0036545890 scopus 로고    scopus 로고
    • Optimization of alkaline protease production from Bacillus sp. using response surface methodology
    • Puri S., Beg Q.K., and Gupta R.G. Optimization of alkaline protease production from Bacillus sp. using response surface methodology. Curr. Microbiol. 44 (2002) 286-290
    • (2002) Curr. Microbiol. , vol.44 , pp. 286-290
    • Puri, S.1    Beg, Q.K.2    Gupta, R.G.3
  • 34
    • 0029770704 scopus 로고    scopus 로고
    • Free alanine, aspartic acid, or glutamic acid reduce the glycation of human lens proteins
    • Ramakrishnan S., Sulochana K.N., Punitham R., and Arunagiri K. Free alanine, aspartic acid, or glutamic acid reduce the glycation of human lens proteins. Glycoconjugate J. 13 (1996) 519-523
    • (1996) Glycoconjugate J. , vol.13 , pp. 519-523
    • Ramakrishnan, S.1    Sulochana, K.N.2    Punitham, R.3    Arunagiri, K.4
  • 36
    • 49749221698 scopus 로고
    • A modified ninhydrin colorimetric analysis for amino acids
    • Rosen H. A modified ninhydrin colorimetric analysis for amino acids. Arch. Biochem. Biophys. 67 (1957) 10-15
    • (1957) Arch. Biochem. Biophys. , vol.67 , pp. 10-15
    • Rosen, H.1
  • 37
    • 33746233270 scopus 로고    scopus 로고
    • Using a medium free of amino acids to produce penicillin g acylase in fed -batch cultivations of Bacillus megaterium ATCC 14945
    • Silva R.G., Souza V.R., Nucci E.R., Pinotti L.M., Cruz A.J.G., Giordano R.C., and Giordanao R.L.C. Using a medium free of amino acids to produce penicillin g acylase in fed -batch cultivations of Bacillus megaterium ATCC 14945. Braz. J. Chem. Eng. 23 (2006) 37-43
    • (2006) Braz. J. Chem. Eng. , vol.23 , pp. 37-43
    • Silva, R.G.1    Souza, V.R.2    Nucci, E.R.3    Pinotti, L.M.4    Cruz, A.J.G.5    Giordano, R.C.6    Giordanao, R.L.C.7
  • 39
    • 14544270524 scopus 로고    scopus 로고
    • Purification and characterization of a serine protease extracellularly produced by Aspergillus fumigatus in a shrimp and crab shell powder medium
    • Wang S., Chen Y., Wang C., Yen Y., and Chern M. Purification and characterization of a serine protease extracellularly produced by Aspergillus fumigatus in a shrimp and crab shell powder medium. Enz. Microb. Technol. 36 (2005) 660-665
    • (2005) Enz. Microb. Technol. , vol.36 , pp. 660-665
    • Wang, S.1    Chen, Y.2    Wang, C.3    Yen, Y.4    Chern, M.5
  • 40
    • 0027481151 scopus 로고
    • Designer enzyme and cell applications in industry and environmental monitoring
    • Wiseman A. Designer enzyme and cell applications in industry and environmental monitoring. J. Chem. Tech. Biotechnol. 56 (1993) 3-13
    • (1993) J. Chem. Tech. Biotechnol. , vol.56 , pp. 3-13
    • Wiseman, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.