메뉴 건너뛰기




Volumn 46, Issue 1, 1998, Pages 354-360

Heterologous Expression of a Candida molischiana Anthocyanin-β-glucosidase in a Wine Yeast Strain

Author keywords

Anthocyanin glucosidase; Candida molischiana; Gene expression; Wine aroma

Indexed keywords

CANDIDA; PICHIA CAPSULATA; SACCHAROMYCES CEREVISIAE;

EID: 0542417490     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf970570r     Document Type: Article
Times cited : (54)

References (29)
  • 1
    • 0027435429 scopus 로고
    • Cloning, sequence and expression of the gene encoding the malolactic enzyme from Lactococcus lactis
    • Ansanay, V.; Dequin, B.; Blondin, B.; Barre, P. Cloning, sequence and expression of the gene encoding the malolactic enzyme from Lactococcus lactis. FEBS Lett. 1993, 332, 74-80.
    • (1993) FEBS Lett. , vol.332 , pp. 74-80
    • Ansanay, V.1    Dequin, B.2    Blondin, B.3    Barre, P.4
  • 2
    • 0000507509 scopus 로고
    • Partial characterization of thermostable anthocyanin-β-glycosidase from Aspergillus niger
    • Blom, H. Partial characterization of thermostable anthocyanin-β-glycosidase from Aspergillus niger. Food Chem. 1983,12, 197-204.
    • (1983) Food Chem. , vol.12 , pp. 197-204
    • Blom, H.1
  • 3
    • 0002797920 scopus 로고
    • Integration of the yeast k1 killer toxin gene into the genome of marked wine yeasts and its effect on vinification
    • Boone, C.; Sdicu, A. M.; Wagner, J.; Degré, R.; Sánchez, C.; Bussey, H. Integration of the yeast k1 killer toxin gene into the genome of marked wine yeasts and its effect on vinification. Am. J. Enol. Vitic. 1990, 41, 37-42.
    • (1990) Am. J. Enol. Vitic. , vol.41 , pp. 37-42
    • Boone, C.1    Sdicu, A.M.2    Wagner, J.3    Degré, R.4    Sánchez, C.5    Bussey, H.6
  • 4
    • 25344463456 scopus 로고
    • New developments in industrial enzymes for wine treatment
    • Novo Nordisk Ferment Ltd.: Neumatt, Switzerland
    • Canal-Llaubères, R-M. New developments in industrial enzymes for wine treatment. 3rd International Novo Symposium, Stuttgart-Killesberg; Novo Nordisk Ferment Ltd.: Neumatt, Switzerland, 1992; pp 147-157.
    • (1992) 3rd International Novo Symposium, Stuttgart-Killesberg , pp. 147-157
    • Canal-Llaubères, R.-M.1
  • 6
    • 0028851198 scopus 로고
    • Functional expression in Saccharomyces cerevisiae of the Lactococcus lactis mleS gene encoding the malolactic enzyme
    • Denayrrolles, M.; Aigle, M.; Lonvaud-Funel, A. Functional expression in Saccharomyces cerevisiae of the Lactococcus lactis mleS gene encoding the malolactic enzyme. FEMS Microbiol. Lett. 1995, 125, 37-44.
    • (1995) FEMS Microbiol. Lett. , vol.125 , pp. 37-44
    • Denayrrolles, M.1    Aigle, M.2    Lonvaud-Funel, A.3
  • 7
    • 0028154060 scopus 로고
    • Mixed lactic acid-alcoholic fermentation by Saccharomyces cerevisiae expressing the Lactobacillus casei L(+)-LDH
    • Dequin, S.; Barre, P. Mixed lactic acid-alcoholic fermentation by Saccharomyces cerevisiae expressing the Lactobacillus casei L(+)-LDH. Bio/Technology 1994, 12, 173-177.
    • (1994) Bio/Technology , vol.12 , pp. 173-177
    • Dequin, S.1    Barre, P.2
  • 8
    • 0022402482 scopus 로고
    • Purification and characterization of the extracel-lular β-glucosidase produced by Candida wickerhamii
    • Freer, S. N. Purification and characterization of the extracel-lular β-glucosidase produced by Candida wickerhamii. Arch. Biochem. Biophys. 1985, 243, 515-522.
    • (1985) Arch. Biochem. Biophys. , vol.243 , pp. 515-522
    • Freer, S.N.1
  • 9
    • 0024266139 scopus 로고
    • New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites
    • Gietz, R. D.; Sugino, A. New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene 1988, 74, 527-534.
    • (1988) Gene , vol.74 , pp. 527-534
    • Gietz, R.D.1    Sugino, A.2
  • 10
    • 0022381958 scopus 로고
    • Purification and properties of an exocellular β-glucosidase of Candida molischiana (Zikes) Meyer and Yarrow capable of hydrolyzing soluble cellodextrins
    • Grondé, P.; Ratomahenina, R.; Arnaud, A.; Galzy P. Purification and properties of an exocellular β-glucosidase of Candida molischiana (Zikes) Meyer and Yarrow capable of hydrolyzing soluble cellodextrins. Can. J. Biochem. Cell. Biol. 1985, 63, 1160-1166.
    • (1985) Can. J. Biochem. Cell. Biol. , vol.63 , pp. 1160-1166
    • Grondé, P.1    Ratomahenina, R.2    Arnaud, A.3    Galzy, P.4
  • 11
    • 0029109404 scopus 로고
    • Construction of a recombinant wine yeast strain expressing a fungal pectate lyase gene
    • González-Candelas, L.; Cortell, A.; Ramón, D. Construction of a recombinant wine yeast strain expressing a fungal pectate lyase gene. FEMS Microbiol. Lett. 1995, 126, 263-270.
    • (1995) FEMS Microbiol. Lett. , vol.126 , pp. 263-270
    • González-Candelas, L.1    Cortell, A.2    Ramón, D.3
  • 12
    • 33947449233 scopus 로고
    • Decolorization of anthocyanins by fungal enzymes
    • Huang, H. T. Decolorization of anthocyanins by fungal enzymes. J. Agric. Food Chem. 1955, 3, 141-146.
    • (1955) J. Agric. Food Chem. , vol.3 , pp. 141-146
    • Huang, H.T.1
  • 13
    • 0029337222 scopus 로고
    • A very stable β-glucosidase from a Candida molischiana mutant strain: Enzymatic properties, sequencing, and homology with other yeast β-glucosidases
    • Janbon, G.; Derancourt, J.; Chemardin, P.; Arnaud, A.; Galzy, P. A very stable β-glucosidase from a Candida molischiana mutant strain: enzymatic properties, sequencing, and homology with other yeast β-glucosidases. Biosci., Biotechnol., Biochem. 1995a, 59, 1320-1322.
    • (1995) Biosci., Biotechnol., Biochem. , vol.59 , pp. 1320-1322
    • Janbon, G.1    Derancourt, J.2    Chemardin, P.3    Arnaud, A.4    Galzy, P.5
  • 14
    • 0028973426 scopus 로고
    • Cloning and sequencing of the β-glucosidase-encoding gene from Candida molischiana strain 35M5N
    • Janbon, G.; Magnet, R.; Arnaud, A.; Galzy, P. Cloning and sequencing of the β-glucosidase-encoding gene from Candida molischiana strain 35M5N. Gene 1995b, 165, 109-113.
    • (1995) Gene , vol.165 , pp. 109-113
    • Janbon, G.1    Magnet, R.2    Arnaud, A.3    Galzy, P.4
  • 15
    • 71849104860 scopus 로고
    • Protein measurement with the folin phenol reagent
    • Lowry, O.; Rosebrough, A.; Farr, A.; Randall, R. Protein measurement with the folin phenol reagent. J. Biol. Chem. 1951, 193, 265-275.
    • (1951) J. Biol. Chem. , vol.193 , pp. 265-275
    • Lowry, O.1    Rosebrough, A.2    Farr, A.3    Randall, R.4
  • 16
    • 84987316939 scopus 로고
    • Kar-mediated transformation of brewing yeast
    • Navas, L.; Esteban, M.; Delgado, M. A. Kar-mediated transformation of brewing yeast. J. Inst. Brew. 1991, 97, 115-118.
    • (1991) J. Inst. Brew. , vol.97 , pp. 115-118
    • Navas, L.1    Esteban, M.2    Delgado, M.A.3
  • 17
    • 0027244827 scopus 로고
    • Construction of a recombinant wine yeast strain expressing β-(1-4)- endoglucanase and its use in microvinification processes
    • Pérez-González, J. A.; González, R.; Querol, A.; Sendra, J.; Ramón, D. Construction of a recombinant wine yeast strain expressing β-(1-4)- endoglucanase and its use in microvinification processes. Appl. Environ. Microbiol. 1993, 59, 2801-2806.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 2801-2806
    • Pérez-González, J.A.1    González, R.2    Querol, A.3    Sendra, J.4    Ramón, D.5
  • 18
    • 0030026260 scopus 로고    scopus 로고
    • The application of molecular techniques in wine microbiology
    • Querol, A.; Ramón, D. The application of molecular techniques in wine microbiology. Trends Food Sci. Technol. 1996, 7, 73-78.
    • (1996) Trends Food Sci. Technol. , vol.7 , pp. 73-78
    • Querol, A.1    Ramón, D.2
  • 19
    • 0026714612 scopus 로고
    • Molecular monitoring of wine fermentations conducted by active dry yeast strains
    • Querol, A.; Barrio, E.; Huerta, T.; Ramón, D. Molecular monitoring of wine fermentations conducted by active dry yeast strains. Appl. Environ. Microbiol. 1992a, 58, 2948-2953.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 2948-2953
    • Querol, A.1    Barrio, E.2    Huerta, T.3    Ramón, D.4
  • 20
    • 84987367527 scopus 로고
    • Dry yeast strain for use in fermentation of Alicante wines: Selection and DNA patterns
    • Querol, A.; Huerta, T.; Barrio, E.; Ramón, D. Dry yeast strain for use in fermentation of Alicante wines: selection and DNA patterns. J. Food Sci. 1992b, 57, 183-185.
    • (1992) J. Food Sci. , vol.57 , pp. 183-185
    • Querol, A.1    Huerta, T.2    Barrio, E.3    Ramón, D.4
  • 21
    • 0030562068 scopus 로고    scopus 로고
    • A sequence analysis of β-glucosidase subfamily B
    • Rojas, A.; Romeu, A. A sequence analysis of β-glucosidase subfamily B. FEBS Lett. 1996, 378, 93-97.
    • (1996) FEBS Lett. , vol.378 , pp. 93-97
    • Rojas, A.1    Romeu, A.2
  • 25
    • 0542415739 scopus 로고    scopus 로고
    • Flavor and fragrance enhancing enzymes. Eur. Pat. Appl. 88305760.6, 1988
    • Shoseyov, O.; Chet, L; Bravdo, B.-A.; Ikan, R. Flavor and fragrance enhancing enzymes. Eur. Pat. Appl. 88305760.6, 1988.
    • Shoseyov, O.1    Chet, L.2    Bravdo, B.-A.3    Ikan, R.4
  • 26
    • 0002746977 scopus 로고
    • Genetic improvement of wine yeast
    • Spencer, J. F., Spencer, D. M., Smith, A. R. W., Eds.; Springer-Verlag, New York
    • Snow, R. Genetic improvement of wine yeast. In Yeast Genetics- Fundamental and Applied Aspects; Spencer, J. F., Spencer, D. M., Smith, A. R. W., Eds.; Springer-Verlag, New York, 1983; pp 439-459.
    • (1983) Yeast Genetics- Fundamental and Applied Aspects , pp. 439-459
    • Snow, R.1
  • 28
    • 84985294915 scopus 로고
    • Purification and properties of the β-glucosidase of a new strain of Candida molischiana able to work at low pH values: Possible use in the liberation of bound terpenols
    • Vasserot, Y.; Chemardin, P.; Arnaud, A.; Galzy, P. Purification and properties of the β-glucosidase of a new strain of Candida molischiana able to work at low pH values: Possible use in the liberation of bound terpenols. J. Basic Microbiol. 1991, 31, 301-312.
    • (1991) J. Basic Microbiol. , vol.31 , pp. 301-312
    • Vasserot, Y.1    Chemardin, P.2    Arnaud, A.3    Galzy, P.4
  • 29
    • 0029800393 scopus 로고    scopus 로고
    • β-glucosidase activity in juice-processing enzymes based on anthocyanin analysis
    • Wightman. J. D.; Wrolstad, R. E. β-glucosidase activity in juice-processing enzymes based on anthocyanin analysis. J. Food Sci. 1996, 61, 544-547.
    • (1996) J. Food Sci. , vol.61 , pp. 544-547
    • Wightman, J.D.1    Wrolstad, R.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.