메뉴 건너뛰기




Volumn 27, Issue 12, 2011, Pages 2813-2819

An acidic β-mannanase from Penicillium sp. C6: Gene cloning and over-expression in Pichia pastoris

Author keywords

Mannanase; Over expression; Penicillium sp. C6; Pichia pastoris

Indexed keywords

AMINO ACID SEQUENCE; ELECTROPHORETIC HOMOGENEITY; GENE CLONING; GLYCOSIDE HYDROLASES; HIGH-LEVEL PRODUCTION; LOCUST BEAN GUM; LOW COSTS; MANNANASE; OPEN READING FRAME; OPTIMAL ACTIVITY; OVER-EXPRESSION; PCR TECHNIQUES; PENICILLIUM SP; PICHIA PASTORIS; PROCESSING TECHNOLOGIES; RECOMBINANT ENZYMES; REVERSE TRANSCRIPTION; SIGNAL PEPTIDE; SPECIFIC ACTIVITY;

EID: 82355164368     PISSN: 09593993     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11274-011-0759-6     Document Type: Article
Times cited : (10)

References (18)
  • 1
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 2
    • 33846392320 scopus 로고    scopus 로고
    • Cloning, functional expression and characterization of Aspergillus sulphureus β-mannanase in Pichia pastoris
    • Chen X, Cao Y, Ding Y, Lu W, Li D (2007) Cloning, functional expression and characterization of Aspergillus sulphureus β-mannanase in Pichia pastoris. J Biotechnol 128: 452-461.
    • (2007) J Biotechnol , vol.128 , pp. 452-461
    • Chen, X.1    Cao, Y.2    Ding, Y.3    Lu, W.4    Li, D.5
  • 3
    • 38949182004 scopus 로고    scopus 로고
    • Microbial mannanases: an overview of production and applications
    • Dhawan S, Kaur J (2007) Microbial mannanases: an overview of production and applications. Crit Rev Biotechnol 27: 197-216.
    • (2007) Crit Rev Biotechnol , vol.27 , pp. 197-216
    • Dhawan, S.1    Kaur, J.2
  • 4
    • 71049124032 scopus 로고    scopus 로고
    • Cloning, expression in Pichia pastoris, and characterization of a thermostable GH5 mannan endo-1, 4-β-mannosidase from Aspergillus niger BK01
    • Do BC, Dang TT, Berrin JG, Haltrich D, To KA, Sigoillot JC, Yamabhai M (2009) Cloning, expression in Pichia pastoris, and characterization of a thermostable GH5 mannan endo-1, 4-β-mannosidase from Aspergillus niger BK01. Microb Cell Fact 8: 59.
    • (2009) Microb Cell Fact , vol.8 , pp. 59
    • Do, B.C.1    Dang, T.T.2    Berrin, J.G.3    Haltrich, D.4    To, K.A.5    Sigoillot, J.C.6    Yamabhai, M.7
  • 5
    • 0346669801 scopus 로고    scopus 로고
    • Localisation and characterization of cell wall mannan polysaccharides in Arabidopsis thaliana
    • Handford MG, Baldwin TC, Gobet F, Prime TA, Miles J, Yu X, Dupree P (2003) Localisation and characterization of cell wall mannan polysaccharides in Arabidopsis thaliana. Planta 218: 27-36.
    • (2003) Planta , vol.218 , pp. 27-36
    • Handford, M.G.1    Baldwin, T.C.2    Gobet, F.3    Prime, T.A.4    Miles, J.5    Yu, X.6    Dupree, P.7
  • 6
    • 43949113609 scopus 로고    scopus 로고
    • Inducible and constitutive expression of a novel thermostable alkaline β-mannanase from alkaliphilic Bacillus sp. N16-5 in Pichia pastoris and characterization of the recombinant enzyme
    • He X, Liu N, Li W, Zhang Z, Zhang B, Ma Y (2008) Inducible and constitutive expression of a novel thermostable alkaline β-mannanase from alkaliphilic Bacillus sp. N16-5 in Pichia pastoris and characterization of the recombinant enzyme. Enzyme Microb Tech 43: 13-18.
    • (2008) Enzyme Microb Tech , vol.43 , pp. 13-18
    • He, X.1    Liu, N.2    Li, W.3    Zhang, Z.4    Zhang, B.5    Ma, Y.6
  • 7
    • 0026055308 scopus 로고
    • Classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat BA (1991) Classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J 280: 309-316.
    • (1991) Biochem J , vol.280 , pp. 309-316
    • Henrissat, B.A.1
  • 8
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 9
    • 0028949381 scopus 로고
    • Thermal asymmetric interlaced PCR: automatable amplification and sequencing of insert end fragments from P1 and YAC clones for chromosome walking
    • Liu YG, Whittier RF (1995) Thermal asymmetric interlaced PCR: automatable amplification and sequencing of insert end fragments from P1 and YAC clones for chromosome walking. Genomics 25: 674-681.
    • (1995) Genomics , vol.25 , pp. 674-681
    • Liu, Y.G.1    Whittier, R.F.2
  • 10
    • 60549106842 scopus 로고    scopus 로고
    • A novel highly acidic β-mannanase from the acidophilic fungus Bispora sp. MEY-1: gene cloning and overexpression in Pichia pastoris
    • Luo H, Wang Y, Wang H, Yang J, Yang Y, Huang H, Yang P, Bai Y, Shi P, Fan Y, Yao B (2009) A novel highly acidic β-mannanase from the acidophilic fungus Bispora sp. MEY-1: gene cloning and overexpression in Pichia pastoris. Appl Microbiol Biotechnol 82: 453-461.
    • (2009) Appl Microbiol Biotechnol , vol.82 , pp. 453-461
    • Luo, H.1    Wang, Y.2    Wang, H.3    Yang, J.4    Yang, Y.5    Huang, H.6    Yang, P.7    Bai, Y.8    Shi, P.9    Fan, Y.10    Yao, B.11
  • 11
    • 0001174333 scopus 로고
    • β-d-Mannanase
    • McCleary BV (1988) β-d-Mannanase. Methods Enzymol 160: 596-610.
    • (1988) Methods Enzymol , vol.160 , pp. 596-610
    • McCleary, B.V.1
  • 12
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller GL (1959) Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal Chem 31: 426-428.
    • (1959) Anal Chem , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 13
    • 42649129680 scopus 로고    scopus 로고
    • An overview of mannan structure and mannan-degrading enzyme systems
    • Moreira LR, Filho EX (2008) An overview of mannan structure and mannan-degrading enzyme systems. Appl Microbiol Biotechnol 79: 165-178.
    • (2008) Appl Microbiol Biotechnol , vol.79 , pp. 165-178
    • Moreira, L.R.1    Filho, E.X.2
  • 15
    • 0031535476 scopus 로고    scopus 로고
    • Chemistry and biochemistry of hemicelluloses: relationship between hemicellulose structure and enzymes required for hydrolysis
    • Puls J (1997) Chemistry and biochemistry of hemicelluloses: relationship between hemicellulose structure and enzymes required for hydrolysis. Macromol Symp 120: 183-196.
    • (1997) Macromol Symp , vol.120 , pp. 183-196
    • Puls, J.1
  • 16
    • 0028932041 scopus 로고
    • Cloning and expression in Saccharomyces cerevisiae of a Trichoderma reesei β-mannanase gene containing a cellulose binding domain
    • Stålbrand H, Saloheimo A, Vehmaanperä J, Henrissat B, Penttilä M (1995) Cloning and expression in Saccharomyces cerevisiae of a Trichoderma reesei β-mannanase gene containing a cellulose binding domain. Appl Environ Microbiol 61: 1090-1097.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 1090-1097
    • Stålbrand, H.1    Saloheimo, A.2    Vehmaanperä, J.3    Henrissat, B.4    Penttilä, M.5
  • 17
    • 0036223868 scopus 로고    scopus 로고
    • Cloning and expression in Pichia pastoris of a blue mussel (Mytilus edulis) β-mannanase gene
    • Xu B, Sellos D, Janson JC (2002) Cloning and expression in Pichia pastoris of a blue mussel (Mytilus edulis) β-mannanase gene. Eur J Biochem 269: 1753-1760.
    • (2002) Eur J Biochem , vol.269 , pp. 1753-1760
    • Xu, B.1    Sellos, D.2    Janson, J.C.3
  • 18
    • 77949350981 scopus 로고    scopus 로고
    • An acidophilic and acid-stable β-mannanase from Phialophora sp. P13 with high mannan hydrolysis activity under simulated gastric conditions
    • Zhao J, Shi P, Luo H, Yang P, Zhao H, Bai Y, Huang H, Wang H, Yao B (2010) An acidophilic and acid-stable β-mannanase from Phialophora sp. P13 with high mannan hydrolysis activity under simulated gastric conditions. J Agric Food Chem 58: 3184-3190.
    • (2010) J Agric Food Chem , vol.58 , pp. 3184-3190
    • Zhao, J.1    Shi, P.2    Luo, H.3    Yang, P.4    Zhao, H.5    Bai, Y.6    Huang, H.7    Wang, H.8    Yao, B.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.