메뉴 건너뛰기




Volumn 29, Issue 1, 2013, Pages 11-16

Shrimp (Litopenaeus vannamei) trypsinogen production in Pichia pastoris bioreactor cultures

Author keywords

Litopenaeus vannamei; Pichia pastoris; Trypsinogen production

Indexed keywords

BIOREACTOR CULTURES; CULTURE MEDIUM; EFFECT OF PH; HIGH DENSITY; HOST CELLS; INDUCTION TEMPERATURES; LITOPENAEUS; METABOLIC ACTIVITY; METHANOL CONCENTRATION; METHANOL UTILIZATION; P. PASTORIS; PICHIA PASTORIS; PRODUCT YIELDS; SHAKE FLASKS;

EID: 84873280945     PISSN: 87567938     EISSN: 15206033     Source Type: Journal    
DOI: 10.1002/btpr.1646     Document Type: Article
Times cited : (13)

References (18)
  • 1
    • 0029888861 scopus 로고    scopus 로고
    • Molecular cloning and sequencing of trypsin cDNAs from Penaeus vannamei (Crustacea, Decapoda): use in assessing gene expression during the moult cycle
    • Klein B, Le Moullac G, Sellos D, Van Wormhoudt A. Molecular cloning and sequencing of trypsin cDNAs from Penaeus vannamei (Crustacea, Decapoda): use in assessing gene expression during the moult cycle. Int J Biochem Cell Biol. 1996; 28: 551-563.
    • (1996) Int J Biochem Cell Biol. , vol.28 , pp. 551-563
    • Klein, B.1    Le Moullac, G.2    Sellos, D.3    Van Wormhoudt, A.4
  • 2
    • 0027909211 scopus 로고
    • Recombinant trypsin production in high cell density fed-batch cultures in E. coli
    • Yee L, Blanch HW. Recombinant trypsin production in high cell density fed-batch cultures in E. coli. Biotechnol Bioeng. 1993; 41: 781-790.
    • (1993) Biotechnol Bioeng. , vol.41 , pp. 781-790
    • Yee, L.1    Blanch, H.W.2
  • 3
    • 0014603717 scopus 로고
    • Isolation and comparative properties of shrimp trypsin
    • Gates BJ, Travis J. Isolation and comparative properties of shrimp trypsin. Biochemistry. 1969; 8: 4483-4489.
    • (1969) Biochemistry. , vol.8 , pp. 4483-4489
    • Gates, B.J.1    Travis, J.2
  • 7
    • 0031608474 scopus 로고    scopus 로고
    • High cell-density fermentation
    • Higgins DR, Cregg JM, editors. Pichia Protocols. Methods in Molecular Biology. Totowa: Humana Press Inc.
    • Stratton J, Chiruvolu V, Meagher M. High cell-density fermentation. In: Higgins DR, Cregg JM, editors. Pichia Protocols. Methods in Molecular Biology. Totowa: Humana Press Inc.; 1998, Vol. 103: 107-120.
    • (1998) , vol.103 , pp. 107-120
    • Stratton, J.1    Chiruvolu, V.2    Meagher, M.3
  • 8
    • 84873301377 scopus 로고    scopus 로고
    • Anonymous. Pichia fermentation process guidelines. Invitrogen. Available at: URL: Last accessed date September, 2012.
    • Anonymous. Pichia fermentation process guidelines. Invitrogen. 2002. Available at: URL: http://tools.invitrogen.com/content/sfs/manuals/pichiaferm_prot.pdf. Last accessed date September, 2012.
    • (2002)
  • 9
    • 0032416188 scopus 로고    scopus 로고
    • Effect of methanol concentration on the production of human b2-glycoprotein I domain V by a recombinant Pichia pastoris: a simple system for the control of methanol concentration using a semiconductor gas sensor
    • Katakura Y, Zhang W, Zhuang G, Omasa T, Kishimoto M, Goto Y, Suga K-I. Effect of methanol concentration on the production of human b2-glycoprotein I domain V by a recombinant Pichia pastoris: a simple system for the control of methanol concentration using a semiconductor gas sensor. J Ferment Bioeng. 1998; 86: 482-487.
    • (1998) J Ferment Bioeng. , vol.86 , pp. 482-487
    • Katakura, Y.1    Zhang, W.2    Zhuang, G.3    Omasa, T.4    Kishimoto, M.5    Goto, Y.6    Suga, K.-I.7
  • 10
    • 0000189612 scopus 로고
    • A salicylate-hypochlorite method for determining ammonia in seawater
    • Bower CE, Holm-Hansen T. A salicylate-hypochlorite method for determining ammonia in seawater. Can J Fish Aquat Sci. 1980; 37: 794-798.
    • (1980) Can J Fish Aquat Sci. , vol.37 , pp. 794-798
    • Bower, C.E.1    Holm-Hansen, T.2
  • 11
    • 50549163362 scopus 로고
    • The preparation and properties of two new chromogenic substrates of trypsin
    • Erlanger BF, Kokowsky N, Cohen W. The preparation and properties of two new chromogenic substrates of trypsin. Arch Biochem Biophys. 1961; 95: 271-278.
    • (1961) Arch Biochem Biophys. , vol.95 , pp. 271-278
    • Erlanger, B.F.1    Kokowsky, N.2    Cohen, W.3
  • 12
    • 0037430841 scopus 로고    scopus 로고
    • Analysis and control of proteolysis of a fusion protein in Pichia pastoris fed-batch processes
    • Jahic M, Gustavsson M, Jansen AK, Martinelle M, Enfors S-O. Analysis and control of proteolysis of a fusion protein in Pichia pastoris fed-batch processes. J Biotechnol. 2003; 102: 45-53.
    • (2003) J Biotechnol. , vol.102 , pp. 45-53
    • Jahic, M.1    Gustavsson, M.2    Jansen, A.K.3    Martinelle, M.4    Enfors, S.-O.5
  • 15
    • 43549095966 scopus 로고    scopus 로고
    • Anionic trypsin from North Pacific Krill (Euphausia pacifica): purification and characterization
    • Wu Z, Jiang G, Xiang P, Xu H. Anionic trypsin from North Pacific Krill (Euphausia pacifica): purification and characterization. Int J Pept Res Ther. 2008; 14: 113-120.
    • (2008) Int J Pept Res Ther. , vol.14 , pp. 113-120
    • Wu, Z.1    Jiang, G.2    Xiang, P.3    Xu, H.4
  • 16
    • 2942627936 scopus 로고    scopus 로고
    • Temperature limited fed-batch technique for control of proteolysis in Pichia pastoris bioreactor cultures
    • Jahic M, Walberg F, Bollok M, Garcia P, Enfors S-O. Temperature limited fed-batch technique for control of proteolysis in Pichia pastoris bioreactor cultures. Microb Cell Fact. 2003; 2: 6-11.
    • (2003) Microb Cell Fact. , vol.2 , pp. 6-11
    • Jahic, M.1    Walberg, F.2    Bollok, M.3    Garcia, P.4    Enfors, S.-O.5
  • 17
    • 0035715001 scopus 로고    scopus 로고
    • Low temperature increases the yield of biologically active herring antifreeze protein in Pichia pastoris
    • Li Z, Xiong F, Lin Q, d'Anjou M, Daugulis AJ, Yang DSC, Hew CL. Low temperature increases the yield of biologically active herring antifreeze protein in Pichia pastoris. Protein Expr Purif. 2001; 21: 438-445.
    • (2001) Protein Expr Purif. , vol.21 , pp. 438-445
    • Li, Z.1    Xiong, F.2    Lin, Q.3    d'Anjou, M.4    Daugulis, A.J.5    Yang, D.S.C.6    Hew, C.L.7
  • 18
    • 0036734202 scopus 로고    scopus 로고
    • Decrease of proteolytic degradation of recombinant hirudin produced by Pichia pastoris by controlling the specific growth rate
    • Zhou XS, Zhang YX. Decrease of proteolytic degradation of recombinant hirudin produced by Pichia pastoris by controlling the specific growth rate. Biotechnol Lett. 2002; 24: 1449-1453.
    • (2002) Biotechnol Lett. , vol.24 , pp. 1449-1453
    • Zhou, X.S.1    Zhang, Y.X.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.