메뉴 건너뛰기




Volumn 99, Issue 7, 2008, Pages 2364-2372

Purification of extracellular acid protease and analysis of fermentation metabolites by Synergistes sp. utilizing proteinaceous solid waste from tanneries

Author keywords

Acid protease; Animal fleshing (ANFL); Surfactant resistant enzyme; Synergistes sp.; Tannery solid waste

Indexed keywords

FERMENTATION; METABOLITES; PURIFICATION; SOLID WASTES;

EID: 38849160976     PISSN: 09608524     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biortech.2007.05.001     Document Type: Article
Times cited : (54)

References (41)
  • 1
    • 14544267136 scopus 로고    scopus 로고
    • Purification and characterisation of extracellular protease produced by Clostridium sp. from Schirmacher oasis, Antarctica
    • Alam S.I., Dube S., Reddy G.S.N., Bhattacharya B.K., Shivaji S., and Singh L. Purification and characterisation of extracellular protease produced by Clostridium sp. from Schirmacher oasis, Antarctica. Enz. Microb. Technol. 36 (2005) 824-831
    • (2005) Enz. Microb. Technol. , vol.36 , pp. 824-831
    • Alam, S.I.1    Dube, S.2    Reddy, G.S.N.3    Bhattacharya, B.K.4    Shivaji, S.5    Singh, L.6
  • 2
    • 0022797706 scopus 로고
    • Amino acid sequence information in proteins and complex proteinaceous material revealed by pyrolysis-capillary gas chromatography-low and high-resolution mass spectrometry
    • Boon J.J., and de Leeuw J.W. Amino acid sequence information in proteins and complex proteinaceous material revealed by pyrolysis-capillary gas chromatography-low and high-resolution mass spectrometry. J. Anal. Appl. Pyrolysis 11 (1987) 313-327
    • (1987) J. Anal. Appl. Pyrolysis , vol.11 , pp. 313-327
    • Boon, J.J.1    de Leeuw, J.W.2
  • 3
    • 0029874404 scopus 로고    scopus 로고
    • An investigation into the use of SDS-PAGE of cell surface extracts and proteolytic activity to differentiate Prevotella nigrescens and Prevotella intermedia
    • Cookson A.L., Wray A., Handley P.S., and Jacob A.E. An investigation into the use of SDS-PAGE of cell surface extracts and proteolytic activity to differentiate Prevotella nigrescens and Prevotella intermedia. FEMS Microbiol. Lett. 136 (1996) 109-115
    • (1996) FEMS Microbiol. Lett. , vol.136 , pp. 109-115
    • Cookson, A.L.1    Wray, A.2    Handley, P.S.3    Jacob, A.E.4
  • 4
    • 38849110902 scopus 로고
    • (Phylogenetic Inference Package) version 3.51c
    • Felsenstein J., and Phylip. (Phylogenetic Inference Package) version 3.51c. Bacteriol. 98 (1993) 756-766
    • (1993) Bacteriol. , vol.98 , pp. 756-766
    • Felsenstein, J.1    Phylip2
  • 5
    • 0030872620 scopus 로고    scopus 로고
    • Molecular microbial diversity of an anaerobic digestor as determined by small-subunit rDNA sequence analysis
    • Godon J.J., Zumstein E., Dabert P., Habouzit F., and Moletta R. Molecular microbial diversity of an anaerobic digestor as determined by small-subunit rDNA sequence analysis. Appl. Environ. Microbiol. 63 (1997) 2802-2813
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 2802-2813
    • Godon, J.J.1    Zumstein, E.2    Dabert, P.3    Habouzit, F.4    Moletta, R.5
  • 6
    • 12744279470 scopus 로고    scopus 로고
    • Rarity associated with specific ecological niches in the bacterial world: the 'Synergistes' example
    • Godon J.J., Morinière J., Moletta M., Gaillac M., Bru V., and Delgènes J.P. Rarity associated with specific ecological niches in the bacterial world: the 'Synergistes' example. Environ. Microbiol. 7 (2005) 213-224
    • (2005) Environ. Microbiol. , vol.7 , pp. 213-224
    • Godon, J.J.1    Morinière, J.2    Moletta, M.3    Gaillac, M.4    Bru, V.5    Delgènes, J.P.6
  • 7
    • 0031587431 scopus 로고    scopus 로고
    • Stability of protease Q against autolysis and in sodium dodecyl sulfate and urea solutions
    • Han X.Q., and Damodaran S. Stability of protease Q against autolysis and in sodium dodecyl sulfate and urea solutions. Biochem. Biophy. Res. Commun. 240 (1997) 839-843
    • (1997) Biochem. Biophy. Res. Commun. , vol.240 , pp. 839-843
    • Han, X.Q.1    Damodaran, S.2
  • 8
    • 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. Was. 10 (1984) 285-295
    • (1984) Agric. Was. , vol.10 , pp. 285-295
    • Hills, D.J.1    Nakamo, K.2
  • 9
    • 0002578411 scopus 로고
    • Characterisation of sinking particles in the ocean by pyrolysis gas chromatography mass spectrometry
    • Ishiwatary R., Yamamoto S., and Handa N. Characterisation of sinking particles in the ocean by pyrolysis gas chromatography mass spectrometry. J. Anal. Appl. Pyrolysis 32 (1995) 75-89
    • (1995) J. Anal. Appl. Pyrolysis , vol.32 , pp. 75-89
    • Ishiwatary, R.1    Yamamoto, S.2    Handa, N.3
  • 10
    • 27844533545 scopus 로고    scopus 로고
    • Production of an oxidant and SDS-stable alkaline protease from an alkalophilic Bacillus clausii I-52 by submerged fermentation: Feasibility as a laundry detergent additive
    • Joo H.S., and Chang C.S. Production of an oxidant and SDS-stable alkaline protease from an alkalophilic Bacillus clausii I-52 by submerged fermentation: Feasibility as a laundry detergent additive. Enz. Microb. Technol. 38 (2006) 176-183
    • (2006) Enz. Microb. Technol. , vol.38 , pp. 176-183
    • Joo, H.S.1    Chang, C.S.2
  • 11
    • 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
  • 14
    • 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
  • 15
    • 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. J. Am. Leather Chem. Assoc. 93 (1998) 32-39
    • (1998) J. Am. Leather Chem. Assoc. , vol.93 , pp. 32-39
    • Kumaraguru, S.1    Sastry, T.P.2    Rose, C.3
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0033831538 scopus 로고    scopus 로고
    • Phylogenetic analysis of bacterial communities in mesophilic and thermophilic bioreactors treating pharmaceutical wastewater
    • LaPara T.M., Nakatsu C.H., Pantea L., and Alleman J.E. Phylogenetic analysis of bacterial communities in mesophilic and thermophilic bioreactors treating pharmaceutical wastewater. Appl. Environ. Microbiol. 66 (2000) 3951-3959
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 3951-3959
    • LaPara, T.M.1    Nakatsu, C.H.2    Pantea, L.3    Alleman, J.E.4
  • 18
    • 0032755142 scopus 로고    scopus 로고
    • Electrophoretic characterization of a novel cysteine protease produced by Vibro harveyi
    • Lee K.K., Liu P.C., and Chen Y.L. Electrophoretic characterization of a novel cysteine protease produced by Vibro harveyi. Electrophor 20 (1999) 3343-3346
    • (1999) Electrophor , vol.20 , pp. 3343-3346
    • Lee, K.K.1    Liu, P.C.2    Chen, Y.L.3
  • 19
    • 38849096636 scopus 로고    scopus 로고
    • Lenore, S.C., Arnold, E.G., Rhodes, R.T., 1989. Standard methods for the examination of water and wastewater-17th edition, APHA publication, Washington DC. ISBN 0-87553-161-X.
    • Lenore, S.C., Arnold, E.G., Rhodes, R.T., 1989. Standard methods for the examination of water and wastewater-17th edition, APHA publication, Washington DC. ISBN 0-87553-161-X.
  • 20
    • 0031884187 scopus 로고    scopus 로고
    • Biochemical and genetic characterization of an extracellular protease from Pseudomonas fluorescens CY091
    • Liao C.H., and McCallus D.E. Biochemical and genetic characterization of an extracellular protease from Pseudomonas fluorescens CY091. Appl. Environ. Microbiol. 64 (1998) 914-921
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 914-921
    • Liao, C.H.1    McCallus, D.E.2
  • 21
    • 0000916969 scopus 로고
    • Calcium-dependent pectate lyase production in the soft-rotting bacterium Pseudomonas fluorescens
    • Liao C.H., McCallus D.E., and Wells J.M. Calcium-dependent pectate lyase production in the soft-rotting bacterium Pseudomonas fluorescens. Phytopathology 83 (1993) 813-818
    • (1993) Phytopathology , vol.83 , pp. 813-818
    • Liao, C.H.1    McCallus, D.E.2    Wells, J.M.3
  • 22
    • 0026554417 scopus 로고
    • Physiological and nutritional factors affecting synthesis of extracellular metalloproteases by Clostridium bifermentans NCTC 2914
    • Macfarlane G.T., and Macfarlane S. Physiological and nutritional factors affecting synthesis of extracellular metalloproteases by Clostridium bifermentans NCTC 2914. Appl. Environ. Microbiol. 58 (1992) 1195-1200
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 1195-1200
    • Macfarlane, G.T.1    Macfarlane, S.2
  • 24
    • 85010439719 scopus 로고
    • Procedure for the isolation of deoxyribonucleic acid from microorganisms
    • Marmur J. Procedure for the isolation of deoxyribonucleic acid from microorganisms. J. Mol. Biol. 3 (1961) 208-218
    • (1961) J. Mol. Biol. , vol.3 , pp. 208-218
    • Marmur, J.1
  • 25
    • 85010093042 scopus 로고
    • Purification and properties of an S-PI (Pepstatin Ac)-insensitive carboxyl proteinase from a Xanthomonas sp. bacterium
    • Oda K., Nakazima T., Terashita T., Suziki K.I., and Murao S. Purification and properties of an S-PI (Pepstatin Ac)-insensitive carboxyl proteinase from a Xanthomonas sp. bacterium. Agric. Biol. Chem. 51 (1987) 3073-3080
    • (1987) Agric. Biol. Chem. , vol.51 , pp. 3073-3080
    • Oda, K.1    Nakazima, T.2    Terashita, T.3    Suziki, K.I.4    Murao, S.5
  • 26
    • 0023154620 scopus 로고
    • Purification and properties of a pepstatin-insensitive carboxylproteinase from a gram negative bacterium
    • Oda K., Sugitani M., Fukuhara K., and Murao S. Purification and properties of a pepstatin-insensitive carboxylproteinase from a gram negative bacterium. Biochim. Biophys. Acta. 923 (1987) 463-469
    • (1987) Biochim. Biophys. Acta. , vol.923 , pp. 463-469
    • Oda, K.1    Sugitani, M.2    Fukuhara, K.3    Murao, S.4
  • 27
    • 0036114373 scopus 로고    scopus 로고
    • Combination of zymography and immunodetection to analyze proteins in complex culture supernatants
    • Poppelmann M., Becker W.M., and Petersen A. Combination of zymography and immunodetection to analyze proteins in complex culture supernatants. Electrophor. 23 (2002) 993-997
    • (2002) Electrophor. , vol.23 , pp. 993-997
    • Poppelmann, M.1    Becker, W.M.2    Petersen, A.3
  • 28
    • 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
  • 29
    • 0029146134 scopus 로고
    • Characterization of a thermostable pepstatin-insensitive acid proteinase from a Bacillus sp.
    • Prescott M., Peek K., and Daniel R.M. Characterization of a thermostable pepstatin-insensitive acid proteinase from a Bacillus sp. Int. J. Biochem. 27 (1995) 729-739
    • (1995) Int. J. Biochem. , vol.27 , pp. 729-739
    • Prescott, M.1    Peek, K.2    Daniel, R.M.3
  • 30
    • 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
  • 32
    • 0033858506 scopus 로고    scopus 로고
    • Arthrobacter flavus sp. nov., a psychrophilic bacterium isolated from a pond in McMurdo Dry Valley, Antarctica
    • Reddy G.S.N., Aggarwal R.K., Matsumoto G.I., and Shivaji S. Arthrobacter flavus sp. nov., a psychrophilic bacterium isolated from a pond in McMurdo Dry Valley, Antarctica. Int. J. Syst. Evol. Microbiol. 50 (2000) 1553-1561
    • (2000) Int. J. Syst. Evol. Microbiol. , vol.50 , pp. 1553-1561
    • Reddy, G.S.N.1    Aggarwal, R.K.2    Matsumoto, G.I.3    Shivaji, S.4
  • 33
    • 0344838589 scopus 로고    scopus 로고
    • Kinetic and phylogenetic characterization of an anaerobic dechlorinating microbial community
    • Rossetti S., Blackall L.L., Majone M., Hugenholtz P., Plumb J.J., and Tandoi V. Kinetic and phylogenetic characterization of an anaerobic dechlorinating microbial community. Microbiol. 149 (2003) 459-469
    • (2003) Microbiol. , vol.149 , pp. 459-469
    • Rossetti, S.1    Blackall, L.L.2    Majone, M.3    Hugenholtz, P.4    Plumb, J.J.5    Tandoi, V.6
  • 34
    • 0031719182 scopus 로고    scopus 로고
    • Phylogenetic diversity of mesophilic and thermophilic granular sludges determined by 16 S rRNA gene analysis
    • Sekiguchi Y., Kamagata Y., Syutsubo K., Ohashi A., Harada H., and Nakamura K. Phylogenetic diversity of mesophilic and thermophilic granular sludges determined by 16 S rRNA gene analysis. Microbiol. 144 (1998) 2655-2665
    • (1998) Microbiol. , vol.144 , pp. 2655-2665
    • Sekiguchi, Y.1    Kamagata, Y.2    Syutsubo, K.3    Ohashi, A.4    Harada, H.5    Nakamura, K.6
  • 35
    • 33748049437 scopus 로고    scopus 로고
    • An extracellular-Pepstatin insensitive acid protease produced by Thermoplasma volcanium
    • Semra K., and Hatice O. An extracellular-Pepstatin insensitive acid protease produced by Thermoplasma volcanium. Biores. Technol. 98 (2007) 112-117
    • (2007) Biores. Technol. , vol.98 , pp. 112-117
    • Semra, K.1    Hatice, O.2
  • 36
    • 0031593689 scopus 로고    scopus 로고
    • 2+/calmodulin dependent protein kinase from Mycobacterium smegmatis ATCC 607
    • 2+/calmodulin dependent protein kinase from Mycobacterium smegmatis ATCC 607. Mol. Cell. Biol. 183 (1998) 183-191
    • (1998) Mol. Cell. Biol. , vol.183 , pp. 183-191
    • Sharma, S.1    Giri, S.2    Khuller, G.K.3
  • 37
    • 0026212764 scopus 로고
    • Purification and properties of a novel surface-active agent and alkaline-resistant protease from Bacillus sp.
    • Shimogaki H., Takeuchi K., Nishino, Ohdera M., Kudo T., Ohba K., Iwama M., and Irie M. Purification and properties of a novel surface-active agent and alkaline-resistant protease from Bacillus sp. J. Agric. Biol. Chem. 55 (1991) 2251-2258
    • (1991) J. Agric. Biol. Chem. , vol.55 , pp. 2251-2258
    • Shimogaki, H.1    Takeuchi, K.2    Nishino3    Ohdera, M.4    Kudo, T.5    Ohba, K.6    Iwama, M.7    Irie, M.8
  • 38
    • 20344378937 scopus 로고    scopus 로고
    • Features of the acid protease partition in aqueous two phase systems of polyethylene glycol-phosphate: chymosin and pepsin
    • Spelzini D., Farruggia B., and Pico G. Features of the acid protease partition in aqueous two phase systems of polyethylene glycol-phosphate: chymosin and pepsin. J. Chromatogr. B. 821 (2005) 60-66
    • (2005) J. Chromatogr. B. , vol.821 , pp. 60-66
    • Spelzini, D.1    Farruggia, B.2    Pico, G.3
  • 39
    • 33646089909 scopus 로고    scopus 로고
    • Characterization of alkaline protease from Vibrio fluvialis strain VM10 isolated from a mangrove sediment sample and its application as a laundry detergent additive
    • Venugopal M., and Saramma A.V. Characterization of alkaline protease from Vibrio fluvialis strain VM10 isolated from a mangrove sediment sample and its application as a laundry detergent additive. Proc. Biochem. 41 (2006) 1239-1243
    • (2006) Proc. Biochem. , vol.41 , pp. 1239-1243
    • Venugopal, M.1    Saramma, A.V.2
  • 40
    • 0022174928 scopus 로고    scopus 로고
    • Ward, O.P., 1985. Proteolytic enzymes. In: Moo-Young M, editor. Oxford: Pergamon, Comprehensive Biotechnol., vol. 3. pp. 789-818.
    • Ward, O.P., 1985. Proteolytic enzymes. In: Moo-Young M, editor. Oxford: Pergamon, Comprehensive Biotechnol., vol. 3. pp. 789-818.
  • 41
    • 0025159447 scopus 로고
    • Purification, characterization, and gene cloning of thermopsin, a thermostable acid protease from Sulfolobus acidocaldarius
    • Xin-li L., and Jordan T. Purification, characterization, and gene cloning of thermopsin, a thermostable acid protease from Sulfolobus acidocaldarius. J. Biol. Chem. 265 (1990) 1490-1495
    • (1990) J. Biol. Chem. , vol.265 , pp. 1490-1495
    • Xin-li, L.1    Jordan, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.