메뉴 건너뛰기




Volumn 43, Issue 1, 2009, Pages 64-71

Statistical optimization of l-leucine amino peptidase production from Streptomyces gedanensis IFO 13427 under submerged fermentation using response surface methodology

Author keywords

Central composite design; Leucine amino peptidase; Response surface methodology; Soyabean; Streptomyces gedanensis; Submerged fermentation

Indexed keywords

AMINATION; AMINES; AMINO ACIDS; BIOCHEMICAL ENGINEERING; CHARGE COUPLED DEVICES; DESIGN; EXPERIMENTS; FERMENTATION; REGRESSION ANALYSIS; SODIUM CHLORIDE; SURFACE PROPERTIES;

EID: 56949102505     PISSN: 1369703X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bej.2008.08.011     Document Type: Article
Times cited : (30)

References (35)
  • 1
    • 0027208935 scopus 로고
    • Aminopeptidase: towards a mechanism of action
    • Taylor A. Aminopeptidase: towards a mechanism of action. Trends Biochem. Sci. 18 (1993) 167-172
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 167-172
    • Taylor, A.1
  • 2
    • 84944039718 scopus 로고    scopus 로고
    • Introduction: metallopeptidases and their clans
    • Barrett A.J., Rawlings N.D., and Woesner J.F. (Eds), Elsevier/Academic Press, San Diego, USA
    • Rawlings N.D., and Barrett A.J. Introduction: metallopeptidases and their clans. In: Barrett A.J., Rawlings N.D., and Woesner J.F. (Eds). Handbook of Proteolytic Enzymes. 2nd ed. (2004), Elsevier/Academic Press, San Diego, USA 231-263
    • (2004) Handbook of Proteolytic Enzymes. 2nd ed. , pp. 231-263
    • Rawlings, N.D.1    Barrett, A.J.2
  • 3
    • 0033821610 scopus 로고    scopus 로고
    • Nociceptin/orphanin FQ metabolism and bioactive metabolites
    • Terenius L., Sandin J., and Sakurada T. Nociceptin/orphanin FQ metabolism and bioactive metabolites. Peptides 21 (2000) 919-922
    • (2000) Peptides , vol.21 , pp. 919-922
    • Terenius, L.1    Sandin, J.2    Sakurada, T.3
  • 4
    • 0036777957 scopus 로고    scopus 로고
    • The importance of the proteasome and subsequent proteolytic steps in the generation of antigenic peptides
    • Goldberg A.L., Cascio P., Saric T., and Rock K.L. The importance of the proteasome and subsequent proteolytic steps in the generation of antigenic peptides. Mol. Immunol. 39 (2002) 147-164
    • (2002) Mol. Immunol. , vol.39 , pp. 147-164
    • Goldberg, A.L.1    Cascio, P.2    Saric, T.3    Rock, K.L.4
  • 7
    • 0009163148 scopus 로고
    • A computer program predicting the bitterness of peptides, esp. in protein hydrolysates, based on amino acid composition and chain length (computer Q)
    • Charalambous G. (Ed). Elsevier, Amsterdam
    • Ney K.H., and Retzlaff G. A computer program predicting the bitterness of peptides, esp. in protein hydrolysates, based on amino acid composition and chain length (computer Q). In: Charalambous G. (Ed). The Shelf Life of Foods and Beverage, Proceedings of the 4th International Flavor Conference. Elsevier, Amsterdam (1985) 543-550
    • (1985) The Shelf Life of Foods and Beverage, Proceedings of the 4th International Flavor Conference , pp. 543-550
    • Ney, K.H.1    Retzlaff, G.2
  • 8
    • 0035096518 scopus 로고    scopus 로고
    • Enzymatic protein hydrolysates in human nutrition
    • Clemente A. Enzymatic protein hydrolysates in human nutrition. Trends Food Sci. Technol. 11 (2000) 254-262
    • (2000) Trends Food Sci. Technol. , vol.11 , pp. 254-262
    • Clemente, A.1
  • 9
    • 0034120834 scopus 로고    scopus 로고
    • Contribution of muscle aminopeptidase to flavor development in dry cured ham
    • Toldra F., Aristoy A.C., and Flores M. Contribution of muscle aminopeptidase to flavor development in dry cured ham. Food Res. Int. 33 (2000) 181-185
    • (2000) Food Res. Int. , vol.33 , pp. 181-185
    • Toldra, F.1    Aristoy, A.C.2    Flores, M.3
  • 10
    • 33745163242 scopus 로고    scopus 로고
    • Dipeptide synthesis by an amino peptidase from Streptomyces septatus TH-2 and its application to synthesis of biologically active peptides
    • Arima J., Uesugi Y., Uraji M., Iwabuchi M., and Hatanaka T. Dipeptide synthesis by an amino peptidase from Streptomyces septatus TH-2 and its application to synthesis of biologically active peptides. Appl. Environ. Microbiol. 72 (2006) 4225-4231
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 4225-4231
    • Arima, J.1    Uesugi, Y.2    Uraji, M.3    Iwabuchi, M.4    Hatanaka, T.5
  • 12
    • 33645700889 scopus 로고    scopus 로고
    • Study on peptide hydrolysis by amino peptidases from Streptomyces griseus, Streptomyces septatus and Aeromonas proteolytica
    • Arima J., Uesugi Y., Iwabuchi M., and Hatanaka T. Study on peptide hydrolysis by amino peptidases from Streptomyces griseus, Streptomyces septatus and Aeromonas proteolytica. Appl. Microb. Biotechnol. 70 (2006) 541-547
    • (2006) Appl. Microb. Biotechnol. , vol.70 , pp. 541-547
    • Arima, J.1    Uesugi, Y.2    Iwabuchi, M.3    Hatanaka, T.4
  • 13
    • 1842531108 scopus 로고    scopus 로고
    • Gene cloning and overproduction of an amino peptidase from Streptomyces septatus TH-2, and comparison with a calcium-activated enzyme from Streptomyces griseus
    • Arima J., Iwabuchi M., and Hatanaka T. Gene cloning and overproduction of an amino peptidase from Streptomyces septatus TH-2, and comparison with a calcium-activated enzyme from Streptomyces griseus. Biochem. Biophys. Res. Commun. 317 (2004) 531-538
    • (2004) Biochem. Biophys. Res. Commun. , vol.317 , pp. 531-538
    • Arima, J.1    Iwabuchi, M.2    Hatanaka, T.3
  • 14
    • 0030200482 scopus 로고    scopus 로고
    • Bacterial amino peptidases: properties and functions
    • Gonzalez T., and Baudouy J.R. Bacterial amino peptidases: properties and functions. FEMS Microbiol. Rev. 18 (1996) 319-344
    • (1996) FEMS Microbiol. Rev. , vol.18 , pp. 319-344
    • Gonzalez, T.1    Baudouy, J.R.2
  • 15
    • 0014200109 scopus 로고
    • Multiple proteolytic enzymes of Streptomyces fradiae. Production, isolation, and preliminary characterization
    • Morihara K., Tatsushi O., and Tsuzuki H. Multiple proteolytic enzymes of Streptomyces fradiae. Production, isolation, and preliminary characterization. Biochim. Biophys. Acta 139 (1967) 382-397
    • (1967) Biochim. Biophys. Acta , vol.139 , pp. 382-397
    • Morihara, K.1    Tatsushi, O.2    Tsuzuki, H.3
  • 16
    • 0022620569 scopus 로고
    • Streptomyces rimosus extracellular proteases. 3. Isolation and characterization of leucine aminopeptidase
    • Vitale L., Renko M., Lenarcic B., Turk V., and Pokorny M. Streptomyces rimosus extracellular proteases. 3. Isolation and characterization of leucine aminopeptidase. Appl. Microbiol. Biotechnol. (1986) 449-455
    • (1986) Appl. Microbiol. Biotechnol. , pp. 449-455
    • Vitale, L.1    Renko, M.2    Lenarcic, B.3    Turk, V.4    Pokorny, M.5
  • 17
    • 0015803160 scopus 로고
    • The proteolytic enzymes of the K-1 strain of Streptomyces griseus obtained from a commercial preparation (Pronase). Purification and characterization of the amino peptidases
    • Vosbeck K.D., Chow K.F., and Awad Jr. W.M. The proteolytic enzymes of the K-1 strain of Streptomyces griseus obtained from a commercial preparation (Pronase). Purification and characterization of the amino peptidases. J. Biol. Chem. 248 (1973) 6029-6034
    • (1973) J. Biol. Chem. , vol.248 , pp. 6029-6034
    • Vosbeck, K.D.1    Chow, K.F.2    Awad Jr., W.M.3
  • 18
    • 0027473733 scopus 로고
    • Specificity of Streptomyces griseus amino peptidase and modulation of activity by divalent metal ion binding and substitution
    • Ben-Meir D., Spungin A., Ashkenazi R., and Blumberg S. Specificity of Streptomyces griseus amino peptidase and modulation of activity by divalent metal ion binding and substitution. Eur. J. Biochem. 212 (1993) 107-112
    • (1993) Eur. J. Biochem. , vol.212 , pp. 107-112
    • Ben-Meir, D.1    Spungin, A.2    Ashkenazi, R.3    Blumberg, S.4
  • 19
    • 0027419919 scopus 로고
    • Purification and properties of an extra cellular amino peptidase from Streptomyces lividans 1326
    • Aphale J.S., and Strohl W.R. Purification and properties of an extra cellular amino peptidase from Streptomyces lividans 1326. J. Gen. Microbiol. 139 (1993) 417-424
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 417-424
    • Aphale, J.S.1    Strohl, W.R.2
  • 20
    • 0029564363 scopus 로고
    • Production dynamics of extracellular proteases accompanying morphological differentiation of Streptomyces albidoflavus SMF301
    • Kang S.G., Kim I.S., Rho Y.T., and Lee K.J. Production dynamics of extracellular proteases accompanying morphological differentiation of Streptomyces albidoflavus SMF301. Microbiology 141 (1995) 3095-3103
    • (1995) Microbiology , vol.141 , pp. 3095-3103
    • Kang, S.G.1    Kim, I.S.2    Rho, Y.T.3    Lee, K.J.4
  • 22
    • 23544438306 scopus 로고
    • Bioprocessing
    • Rehm H.J., Read G., Puhler A., and Stagler P. (Eds), VCH Publishers Inc., New York
    • Greasham R.L. Bioprocessing. In: Rehm H.J., Read G., Puhler A., and Stagler P. (Eds). Biotechnology vol. 3 (1983), VCH Publishers Inc., New York 128-139
    • (1983) Biotechnology , vol.3 , pp. 128-139
    • Greasham, R.L.1
  • 24
    • 33645966799 scopus 로고    scopus 로고
    • Optimization of the medium composition for production of mycelial biomass and exo-polymer by Grifola frondosa GF9801 using response surface methodology
    • Cui F.J., Li Y., Xu Z.H., Xu H.Y., Sun K., and Tao W.Y. Optimization of the medium composition for production of mycelial biomass and exo-polymer by Grifola frondosa GF9801 using response surface methodology. Bioresour. Technol. 97 (2006) 1209-1216
    • (2006) Bioresour. Technol. , vol.97 , pp. 1209-1216
    • Cui, F.J.1    Li, Y.2    Xu, Z.H.3    Xu, H.Y.4    Sun, K.5    Tao, W.Y.6
  • 25
    • 0001175580 scopus 로고
    • Production of lipase by Candida rugosa in solid-state fermentation. 2. Medium optimization and effect of aeration
    • Rao P.V., Jayaraman K., and Lakshmanan C.M. Production of lipase by Candida rugosa in solid-state fermentation. 2. Medium optimization and effect of aeration. Process Biochem. 28 (1993) 391-395
    • (1993) Process Biochem. , vol.28 , pp. 391-395
    • Rao, P.V.1    Jayaraman, K.2    Lakshmanan, C.M.3
  • 26
    • 26444555646 scopus 로고    scopus 로고
    • Optimizing the concentrations of carbon, nitrogen and phosphorus in citric acid fermentation with response surface method
    • Chen H.C. Optimizing the concentrations of carbon, nitrogen and phosphorus in citric acid fermentation with response surface method. Food Biotechnol. 10 (1996) 13-27
    • (1996) Food Biotechnol. , vol.10 , pp. 13-27
    • Chen, H.C.1
  • 27
    • 0025164840 scopus 로고    scopus 로고
    • Purification and characterization of an aminopeptidase from Lactococcus lactis subsp. cremoris Wg2
    • Tan P.S.T., and Konings W.N. Purification and characterization of an aminopeptidase from Lactococcus lactis subsp. cremoris Wg2. Appl. Environ. Microbiol. 56 (1996) 526-532
    • (1996) Appl. Environ. Microbiol. , vol.56 , pp. 526-532
    • Tan, P.S.T.1    Konings, W.N.2
  • 30
    • 0142075822 scopus 로고    scopus 로고
    • Optimization of medium and cultivation conditions for pullulan production by a new pullulan-producing yeast
    • Chi Z., and Zhao S. Optimization of medium and cultivation conditions for pullulan production by a new pullulan-producing yeast. Enzyme Microb. Technol. 33 (2003) 206-221
    • (2003) Enzyme Microb. Technol. , vol.33 , pp. 206-221
    • Chi, Z.1    Zhao, S.2
  • 31
    • 0000816944 scopus 로고
    • Surface active agents
    • Furia T.E. (Ed), CRC Press, New York, NY
    • Griffin W.C., and Lynch M.J. Surface active agents. In: Furia T.E. (Ed). Handbook of Food Additives. 2nd ed. (1972), CRC Press, New York, NY 397-429
    • (1972) Handbook of Food Additives. 2nd ed. , pp. 397-429
    • Griffin, W.C.1    Lynch, M.J.2
  • 32
    • 0033572187 scopus 로고    scopus 로고
    • Microbial alkaline protease: from bioindustrial viewpoint
    • Kurmar C.G., and Tagaki H. Microbial alkaline protease: from bioindustrial viewpoint. Biotechnol. Adv. 17 (1999) 561-594
    • (1999) Biotechnol. Adv. , vol.17 , pp. 561-594
    • Kurmar, C.G.1    Tagaki, H.2
  • 33
    • 0002448654 scopus 로고
    • Statistical problem solving
    • Haaland P.D. (Ed), Marcel Dekker Incorporation, New York
    • Haaland P.D. Statistical problem solving. In: Haaland P.D. (Ed). Experimental Design in Biotechnology (1989), Marcel Dekker Incorporation, New York 1-18
    • (1989) Experimental Design in Biotechnology , pp. 1-18
    • Haaland, P.D.1
  • 34
    • 0034752195 scopus 로고    scopus 로고
    • A response surface approach for the comparison of lipase production by Candida cylindracea using two different carbon sources
    • Muralidhar R.V., Chirumamila R.R., Marchant R., and Nigam P. A response surface approach for the comparison of lipase production by Candida cylindracea using two different carbon sources. Biochem. Eng. J. 9 (2001) 17-23
    • (2001) Biochem. Eng. J. , vol.9 , pp. 17-23
    • Muralidhar, R.V.1    Chirumamila, R.R.2    Marchant, R.3    Nigam, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.