메뉴 건너뛰기




Volumn 16, Issue 4, 2009, Pages 453-456

Cloning and expression in Saccharomyces cerevisiae of chit2 gene from Beauveria bassiana

Author keywords

Beauveria bassiana; Chitinase; Expression; Saccharomyces cerevisiae

Indexed keywords

BEAUVERIA BASSIANA; CHITINASE; CHITINASE GENES; CHITINASES; CLONING AND EXPRESSION; CULTURE TIME; EXPRESSION; EXPRESSION VECTORS; POLYMERASE CHAIN REACTION; SACCHAROMYCES CEREVISIAE; YEAST EXPRESSION;

EID: 70350589176     PISSN: 10059113     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (1)

References (15)
  • 1
    • 0000971679 scopus 로고
    • Chitinous structure
    • New York: Elsevier
    • Jeuniaux C. Chitinous structure. Comprehensive Biochemistry. New York: Elsevier, 1971. 595-632.
    • (1971) Comprehensive Biochemistry , pp. 595-632
    • Jeuniaux, C.1
  • 3
    • 0030748702 scopus 로고    scopus 로고
    • Human enzymatic activities related to the therapeutic administration of chitin derivatives
    • Muzzarelli R A. Human enzymatic activities related to the therapeutic administration of chitin derivatives. Cellular and Molecular Life Sciences, 1997, (53): 131-140.
    • (1997) Cellular and Molecular Life Sciences , Issue.53 , pp. 131-140
    • Muzzarelli, R.A.1
  • 6
    • 0032485890 scopus 로고    scopus 로고
    • The strongly conserved lysine 256 of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase is essential for phosphoryl transfer
    • Krautwurst H, Bazaes S, Gonzalez F D, et al. The strongly conserved lysine 256 of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase is essential for phosphoryl transfer. Biochemistry, 1998, 37: 6295-6302.
    • (1998) Biochemistry , vol.37 , pp. 6295-6302
    • Krautwurst, H.1    Bazaes, S.2    Gonzalez, F.D.3
  • 8
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid for estimation of reducing sugar
    • Miller G L. Use of dinitrosalicylic acid for estimation of reducing sugar. Analytical Chemistry, 1959, 31: 426-434.
    • (1959) Analytical Chemistry , vol.31 , pp. 426-434
    • Miller, G.L.1
  • 9
    • 0026778048 scopus 로고
    • Foreign gene expression in yeast: A review
    • Romanos M A, Scorer C A, Clare I I. Foreign gene expression in yeast: a review. Yeast, 1992, 8: 423-488.
    • (1992) Yeast , vol.8 , pp. 423-488
    • Romanos, M.A.1    Scorer, C.A.2    Clare, I.I.3
  • 10
    • 0023050642 scopus 로고
    • The purification of eukariotic polypeptides synthesized in Escherichia coli
    • Marston F A O. The purification of eukariotic polypeptides synthesized in Escherichia coli. Biochemical Journal, 1986, 240: 1-12.
    • (1986) Biochemical Journal , vol.240 , pp. 1-12
    • Marston, F.A.O.1
  • 11
    • 0030934889 scopus 로고    scopus 로고
    • Methodology for the preparation of pure recombinant S. cerevisiae lanosterol synthase using a baculuvirus expression system. Evidence that oxirane cleavage and A-ring formation are concerted in the biosynthesis of lanosterol from 2, 3-oxidosqualene
    • Corey E J, Chen H, Baker C H, et al. Methodology for the preparation of pure recombinant S. cerevisiae lanosterol synthase using a baculuvirus expression system. Evidence that oxirane cleavage and A-ring formation are concerted in the biosynthesis of lanosterol from 2, 3-oxidosqualene. Journal of the American Chemical Society, 1997, 116: 1277-1288.
    • (1997) Journal of the American Chemical Society , vol.116 , pp. 1277-1288
    • Corey, E.J.1    Chen, H.2    Baker, C.H.3
  • 12
    • 0031435426 scopus 로고    scopus 로고
    • Construction of a gene encoding the insect bactericidal protein attacin. Studies on its expression in Escherichia coli
    • Santibáñez E, Gómez I, Martínez M T, et al. Construction of a gene encoding the insect bactericidal protein attacin. Studies on its expression in Escherichia coli. Biological Research, 1997, 30: 149-160.
    • (1997) Biological Research , vol.30 , pp. 149-160
    • Santibáñez, E.1    Gómez, I.2    Martínez, M.T.3
  • 13
    • 0034003717 scopus 로고    scopus 로고
    • Production and purification of protease from a Bacillus subtilis that can deproteinize crustacean wastes
    • Yang J K, Shih I L, Tzeng Y M, et al. Production and purification of protease from a Bacillus subtilis that can deproteinize crustacean wastes. Enzyme and Microbial Technology, 2000, 26: 406-419.
    • (2000) Enzyme and Microbial Technology , vol.26 , pp. 406-419
    • Yang, J.K.1    Shih, I.L.2    Tzeng, Y.M.3
  • 14
    • 0033991016 scopus 로고    scopus 로고
    • Submerged culture oroduction of chitinase by Trichoderma harzianum in stirred tank bioreactors - The influence of agitator speed
    • Arthur F P, Panda T. Submerged culture oroduction of chitinase by Trichoderma harzianum in stirred tank bioreactors-the influence of agitator speed. Biochemical Engineering Journal, 2000, 4: 112-120.
    • (2000) Biochemical Engineering Journal , vol.4 , pp. 112-120
    • Arthur, F.P.1    Panda, T.2
  • 15
    • 0030900026 scopus 로고    scopus 로고
    • Purification and characterization of two bifunctional chitinase/lysozymes extracellularly produced by Pseudomonas aeruginosa K-187 in a shrimp and crab shell powder medium
    • Wang S L, Chang W T. Purification and characterization of two bifunctional chitinase/lysozymes extracellularly produced by Pseudomonas aeruginosa K-187 in a shrimp and crab shell powder medium. Applied and Environmental Microbiology, 1997, 63: 380-386.
    • (1997) Applied and Environmental Microbiology , vol.63 , pp. 380-386
    • Wang, S.L.1    Chang, W.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.