메뉴 건너뛰기




Volumn 6, Issue 1, 2012, Pages 55-65

Proteolytic enzyme production by isolated serratia sp RSPB11: Role of environmental parameters

Author keywords

Enzyme; Fermentation; Isolation; Protease; Serratia sp

Indexed keywords

BENZYLSULFONYL FLUORIDE; CASEIN; CHITIN; EDETIC ACID; GELATIN; METALLOPROTEINASE; PROTEINASE;

EID: 84856184994     PISSN: 09738916     EISSN: 22307303     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (7)

References (37)
  • 1
    • 0027941838 scopus 로고
    • Families of zinc metalloproteases
    • Hooper, N.M. (1994). Families of zinc metalloproteases, FEBS Letters, 354 (1):1-6.
    • (1994) FEBS Letters , vol.354 , Issue.1 , pp. 1-6
    • Hooper, N.M.1
  • 2
  • 3
    • 84954960336 scopus 로고
    • Serratia protease. Part III. Characteristics of the enzyme as a metalloenzyme
    • Miyata, K., Tomoda, K., Isono, M. (1971). Serratia protease. Part III. Characteristics of the enzyme as a metalloenzyme. Agricultural and Biological Chemistry, 35: 460-467.
    • (1971) Agricultural and Biological Chemistry , vol.35 , pp. 460-467
    • Miyata, K.1    Tomoda, K.2    Isono, M.3
  • 4
    • 0029907110 scopus 로고    scopus 로고
    • Role of microbial proteases in pathogenesis
    • Maeda, H. (1996). Role of microbial proteases in pathogenesis. Microbiology and Immunology,40:685-699
    • (1996) Microbiology and Immunology , vol.40 , pp. 685-699
    • Maeda, H.1
  • 5
    • 0032729823 scopus 로고    scopus 로고
    • Use of a 49-peptide library for a qualitative and quantitative determination of pseudomonal serralysin specificity
    • Louis, D., Bernillon, J. and Wallach J.M. (1999). Use of a 49-peptide library for a qualitative and quantitative determination of pseudomonal serralysin specificity. International Journal of Biochemistry and Cell Biology, 12:1435-41.
    • (1999) International Journal of Biochemistry and Cell Biology , vol.12 , pp. 1435-1441
    • Louis, D.1    Bernillon, J.2    Wallach, J.M.3
  • 7
    • 0021335808 scopus 로고
    • Purification and characterization of four proteases from a clinical isolate of Serratia marcescens kums 3958
    • Matsumoto, K., Maeda, H., Takata, K., Kamata, R. and Okamura, R. (1984). Purification and characterization of four proteases from a clinical isolate of Serratia marcescens kums 3958. Journal of Bacteriology, 157:225-232.
    • (1984) Journal of Bacteriology , vol.157 , pp. 225-232
    • Matsumoto, K.1    Maeda, H.2    Takata, K.3    Kamata, R.4    Okamura, R.5
  • 8
    • 77955923960 scopus 로고    scopus 로고
    • Cloning, Expression, and Identification of a Novel Extracellular Cold-Adapted Alkaline Protease Gene of the Marine Bacterium Strain YS-80-122
    • Fang. W., Jianhua, H., Chengye, Y. and Mi, S. (2010). Cloning, Expression, and Identification of a Novel Extracellular Cold-Adapted Alkaline Protease Gene of the Marine Bacterium Strain YS-80-122, Applied Biochemistry and Biotechnology, 162:1497-1505.
    • (2010) Applied Biochemistry and Biotechnology , vol.162 , pp. 1497-1505
    • Fang, W.1    Jianhua, H.2    Chengye, Y.3    Mi, S.4
  • 9
    • 0034660603 scopus 로고    scopus 로고
    • Purification, physico-chemical characterization and sequence of a heat labile alkaline metalloprotease isolated from a psychrophilic Pseudomonas species
    • Jean-Pierre, C., Ioan, P., Mostafa, B., Jozef, V.B. and Charles, G., (2000). Purification, physico-chemical characterization and sequence of a heat labile alkaline metalloprotease isolated from a psychrophilic Pseudomonas species, Biochimica Biophysica Acta 1479: 265-274.
    • (2000) Biochimica Biophysica Acta , vol.1479 , pp. 265-274
    • Jean-Pierre, C.1    Ioan, P.2    Mostafa, B.3    Jozef, V.B.4    Charles, G.5
  • 10
    • 0035144817 scopus 로고    scopus 로고
    • Production, purification and partial characterization of two extracellular proteases from Serratia marcescens grown in whey
    • Romero, F., Garcia, L.A., Salas, J., Diaz, M. and Quiros, L. (2001). Production, purification and partial characterization of two extracellular proteases from Serratia marcescens grown in whey. Process Biochemistry, 36: 501-515.
    • (2001) Process Biochemistry , vol.36 , pp. 501-515
    • Romero, F.1    Garcia, L.A.2    Salas, J.3    Diaz, M.4    Quiros, L.5
  • 11
    • 0018347406 scopus 로고
    • Regulation of extracellular protease formation by Serratia marcescens
    • Bromke, B. J. and Hammel, J. M. (1978). Regulation of extracellular protease formation by Serratia marcescens. Canadian Journal of Microbiology, 25:47-52.
    • (1978) Canadian Journal of Microbiology , vol.25 , pp. 47-52
    • Bromke, B.J.1    Hammel, J.M.2
  • 12
    • 0018932609 scopus 로고
    • Excretion of a protease by Serratia marcescens
    • Braun, V. and Schmitz, G. (1980). Excretion of a protease by Serratia marcescens. Archieves of Microbiology, 124: 55-61.
    • (1980) Archieves of Microbiology , vol.124 , pp. 55-61
    • Braun, V.1    Schmitz, G.2
  • 13
    • 70349504352 scopus 로고    scopus 로고
    • Purification and characterization of solvent-tolerant, thermostable, alkaline metalloprotease from alkalophilic Pseudomonas aeruginosa MTCC 7926
    • Ulhas, P. and Ambalal, C. (2009). Purification and characterization of solvent-tolerant, thermostable, alkaline metalloprotease from alkalophilic Pseudomonas aeruginosa MTCC 7926, Journal of Chemical Technology and Biotechnology, 84: 1255-1262.
    • (2009) Journal of Chemical Technology and Biotechnology , vol.84 , pp. 1255-1262
    • Ulhas, P.1    Ambalal, C.2
  • 14
    • 0035132024 scopus 로고    scopus 로고
    • The aprX-lipA operon of Pseudomonas fluorescens B52: A molecular analysis of metalloprotease and lipase production
    • Rick, G. W., Michelle, B., Carie, A. B. and Ifor, R. B. (2001). The aprX-lipA operon of Pseudomonas fluorescens B52: a molecular analysis of metalloprotease and lipase production, Microbiology 147: 345-354.
    • (2001) Microbiology , vol.147 , pp. 345-354
    • Rick, G.W.1    Michelle, B.2    Carie, A.B.3    Ifor, R.B.4
  • 15
    • 0036181917 scopus 로고    scopus 로고
    • Characterization of a Cytotoxic Factor in Culture Filtrates of Serratia marcescens
    • Kent, B., Marty, Christopher L. W. and Linda J. G. (2002). Characterization of a Cytotoxic Factor in Culture Filtrates of Serratia marcescens, Infection and Immunity, 70:1121-1128.
    • (2002) Infection and Immunity , vol.70 , pp. 1121-1128
    • Kent, B.1    Marty Christopher, L.W.2    Linda, J.G.3
  • 16
    • 0032470995 scopus 로고    scopus 로고
    • Protease production from whey at high concentrations by Serratia marcescens
    • Romero, F., García, L.A. and Díaz, M. (1998). Protease production from whey at high concentrations by Serratia marcescens. Resource and Environmental Biotechnology, 2: 93-115.
    • (1998) Resource and Environmental Biotechnology , vol.2 , pp. 93-115
    • Romero, F.1    García, L.A.2    Díaz, M.3
  • 18
    • 63449128513 scopus 로고    scopus 로고
    • Purification and Characterization of Protease and Chitinase from Bacillus cereus TKU006 and Conversion of Marine Wastes by These Enzymes
    • Wang, S.L., Chao, C.H., Liang, T.Z. and Chen, C.C. (2009). Purification and Characterization of Protease and Chitinase from Bacillus cereus TKU006 and Conversion of Marine Wastes by These Enzymes, Marine Biotechnology, 11:334-344.
    • (2009) Marine Biotechnology , vol.11 , pp. 334-344
    • Wang, S.L.1    Chao, C.H.2    Liang, T.Z.3    Chen, C.C.4
  • 19
    • 0029028241 scopus 로고
    • Over production of Serratia marcescens metalloprotease (SMP) from the recombinant Serratia marcescens strains
    • Kim, K.S., Park, K.S., Byun, S.M., Pan, J.G. and Shin, Y.C. (1995). Over production of Serratia marcescens metalloprotease (SMP) from the recombinant Serratia marcescens strains, Biotechnology Letters, 17:497-502.
    • (1995) Biotechnology Letters , vol.17 , pp. 497-502
    • Kim, K.S.1    Park, K.S.2    Byun, S.M.3    Pan, J.G.4    Shin, Y.C.5
  • 20
    • 0037213311 scopus 로고    scopus 로고
    • An Overview on Fermentation, downstream processing and properties of microbial alkaline proteases
    • Gupta, R., Beg, Q.K., Khan, S. and Chauhan, B. (2002). An Overview on Fermentation, downstream processing and properties of microbial alkaline proteases, Applied Microbiology and Biotechnology, 60: 381-395.
    • (2002) Applied Microbiology and Biotechnology , vol.60 , pp. 381-395
    • Gupta, R.1    Beg, Q.K.2    Khan, S.3    Chauhan, B.4
  • 21
    • 34247503754 scopus 로고    scopus 로고
    • L-Asparaginase production by isolated Staphylococcus sp.-6A: Design of experiment considering interaction effect for process parameter optimization
    • Prakasham, R.S., Subba Rao, Ch., Rao, R.S., Lakshmi, G.S. and Sarma, P.N. (2007). L-Asparaginase production by isolated Staphylococcus sp.-6A: design of experiment considering interaction effect for process parameter optimization. Journal of Applied Microbiology, 102:1382-1391.
    • (2007) Journal of Applied Microbiology , vol.102 , pp. 1382-1391
    • Prakasham, R.S.1    Subba Rao, C.2    Rao, R.S.3    Lakshmi, G.S.4    Sarma, P.N.5
  • 22
    • 70449678570 scopus 로고    scopus 로고
    • Corn husk as a novel substrate for the production of rifamycin B by isolated Amycolatopsis sp. RSP 3 under SSF
    • Mahalaxmi, Y., Sathish, T., Subba Rao, Ch. and Prakasham, R.S. (2010). Corn husk as a novel substrate for the production of rifamycin B by isolated Amycolatopsis sp. RSP 3 under SSF. Process Biochemistry, 45: 47-53.
    • (2010) Process Biochemistry , vol.45 , pp. 47-53
    • Mahalaxmi, Y.1    Sathish, T.2    Subba Rao, C.3    Prakasham, R.S.4
  • 23
    • 0000468087 scopus 로고
    • Genus VIII. Serratia
    • In: Krieg NR, Holt JG (eds), Baltimore, Williams and Wilkins
    • Grimont, P.A.D. and Grimont, F. (1984). Genus VIII. Serratia. In: Krieg NR, Holt JG (eds) Bergey's Manual of systematic bacteriology, vol 1. Baltimore, Williams and Wilkins. 477-484.
    • (1984) Bergey's Manual of systematic bacteriology , vol.1 , pp. 477-484
    • Grimont, P.A.D.1    Grimont, F.2
  • 24
    • 85012738381 scopus 로고
    • Estimation of Pepsin, Papain and Cathepsin with haemogloblin
    • Anson, M.L. (1938). Estimation of Pepsin, Papain and Cathepsin with haemogloblin. Journal of General Physiology, 22: 79-89.
    • (1938) Journal of General Physiology , vol.22 , pp. 79-89
    • Anson, M.L.1
  • 25
    • 0035806167 scopus 로고    scopus 로고
    • Concurrent production of chitin from shrimp shells and fungi
    • Teng, W.L., Khor, E., Tan, T.K., Lim, L.Y. and Tana, S.C. (2001). Concurrent production of chitin from shrimp shells and fungi, Carbohydrate Research 332 305-316.
    • (2001) Carbohydrate Research , vol.332 , pp. 305-316
    • Teng, W.L.1    Khor, E.2    Tan, T.K.3    Lim, L.Y.4    Tana, S.C.5
  • 26
    • 0018130363 scopus 로고
    • Inactivation of the protease inhibitor phenylmethyldulfonyl fluoride in buffers
    • James, G.T. (1978). Inactivation of the protease inhibitor phenylmethyldulfonyl fluoride in buffers, Analytical Biochemistry 86: 574.
    • (1978) Analytical Biochemistry , vol.86 , pp. 574
    • James, G.T.1
  • 27
    • 84856152549 scopus 로고    scopus 로고
    • Issue date: 28.09.10 Issued by: Standards Unit, Department for Evaluations, Standards and Training. BSOP ID 16i3
    • Identification of Enterobacteriaceae, Issue no: 3 Issue date: 28.09.10 Issued by: Standards Unit, Department for Evaluations, Standards and Training. BSOP ID 16i3.
    • Identification of Enterobacteriaceae , Issue.3
  • 29
    • 84856159798 scopus 로고    scopus 로고
    • Over production of an extracellular protease from Serratia sp. DT3 just using soybean powder
    • Nguyen, T.T. and Quyen, D.T. (2011). Over production of an extracellular protease from Serratia sp. DT3 just using soybean powder, World journal of agricultural sciences 7(1):29-36.
    • (2011) World journal of agricultural sciences , vol.7 , Issue.1 , pp. 29-36
    • Nguyen, T.T.1    Quyen, D.T.2
  • 30
    • 79953287445 scopus 로고    scopus 로고
    • Determination of Alkaline Protease Production In Serratia Marcescens Sp7 Using Agro Wastes As Substrate Medium
    • World Academy of Science, Engineering and Technology
    • Joseph, B. and Palaniyandi, S. (2011). Determination of Alkaline Protease Production In Serratia Marcescens Sp7 Using Agro Wastes As Substrate Medium, Optimization Of Production Parameters And Purification Of The Enzyme, World Academy of Science, Engineering and Technology, 74: 252-256.
    • (2011) Optimization Of Production Parameters And Purification Of The Enzyme , vol.74 , pp. 252-256
    • Joseph, B.1    Palaniyandi, S.2
  • 31
    • 69549098243 scopus 로고    scopus 로고
    • Application of response surface methodology in medium optimization for protease production by the new strain of Serratia marcescens sb08
    • Venil, C.K. and Lakshmanperumalsamy, P. (2009). Application of response surface methodology in medium optimization for protease production by the new strain of Serratia marcescens sb08, Polish journal of microbiology 58:117-124.
    • (2009) Polish journal of microbiology , vol.58 , pp. 117-124
    • Venil, C.K.1    Lakshmanperumalsamy, P.2
  • 32
    • 77954983933 scopus 로고    scopus 로고
    • Evolutionary Operation (EVOP) to Optimize Whey-Independent Serratiopeptidase Production from Serratia marcescens NRRL B-23112
    • Pansuriya, R.C. and Rekha, S. S. (2010). Evolutionary Operation (EVOP) to Optimize Whey-Independent Serratiopeptidase Production from Serratia marcescens NRRL B-23112, Journal of Microbiology and Biotechnology, 20: 950-957.
    • (2010) Journal of Microbiology and Biotechnology , vol.20 , pp. 950-957
    • Pansuriya, R.C.1    Rekha, S.S.2
  • 33
    • 7444225196 scopus 로고    scopus 로고
    • Physical factors affecting the production of organic solventtolerant protease by 30 Pseudomonas aeruginosa strain K
    • Rahman, R.N.Z.R., Geok, L.P., Basri M. and Salleh, A.B. (2005). Physical factors affecting the production of organic solventtolerant protease by 30 Pseudomonas aeruginosa strain K. Resource Technology, 96: 429-436.
    • (2005) Resource Technology , vol.96 , pp. 429-436
    • Rahman, R.N.Z.R.1    Geok, L.P.2    Basri, M.3    Salleh, A.B.4
  • 34
    • 14544307871 scopus 로고    scopus 로고
    • An organic solvent-tolerant protease from Pseudomonas aeruginosa strain K Nutritional factors affecting protease production
    • Rahman, R.N.Z.R., Geok, L.P., Basri M. and Salleh, A.B. (2005). An organic solvent-tolerant protease from Pseudomonas aeruginosa strain K Nutritional factors affecting protease production. Enzyme and Microbial Technology 36: 749-757
    • (2005) Enzyme and Microbial Technology , vol.36 , pp. 749-757
    • Rahman, R.N.Z.R.1    Geok, L.P.2    Basri, M.3    Salleh, A.B.4
  • 35
    • 19944397523 scopus 로고    scopus 로고
    • Production and properties of an extracellular from thermophilic Bacillus sp
    • Nascimento, W.C.A. and Martins, M.L.L. (2004). Production and properties of an extracellular from thermophilic Bacillus sp. Brazilian journal of microbiology, 35: 91-95.
    • (2004) Brazilian journal of microbiology , vol.35 , pp. 91-95
    • Nascimento, W.C.A.1    Martins, M.L.L.2
  • 36
    • 0030885049 scopus 로고    scopus 로고
    • Production, purification and characterization of a 50-kDa extracellular metalloprotease from Serratia marcescens
    • Salamone, P.R. and Wodzinski, R.J. (1997). Production, purification and characterization of a 50-kDa extracellular metalloprotease from Serratia marcescens, Applied microbiology and biotechnology, 48: 317-324.
    • (1997) Applied microbiology and biotechnology , vol.48 , pp. 317-324
    • Salamone, P.R.1    Wodzinski, R.J.2
  • 37
    • 58249140685 scopus 로고    scopus 로고
    • Characterization of thermo-and detergent stable serine protease from isolated Bacillus circulans and evaluation of ecofriendly applications
    • Subba Rao, Ch., Sathish, T., Ravichandra, P. and Prakasham, R.S. (2009). Characterization of thermo-and detergent stable serine protease from isolated Bacillus circulans and evaluation of ecofriendly applications, Process Biochemistry, 44:262-268
    • (2009) Process Biochemistry , vol.44 , pp. 262-268
    • Subba Rao, C.1    Sathish, T.2    Ravichandra, P.3    Prakasham, R.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.