메뉴 건너뛰기




Volumn 118, Issue 5, 2014, Pages 546-553

Differential activities of fungi-derived tannases on biotransformation and substrate inhibition in green tea extract

Author keywords

Antioxidative activity; Biotransformation; Substrate inhibition; Tannase; Tea catechins

Indexed keywords

ANTIOXIDANTS; BIOCONVERSION; CATALYSIS; FLAVONOIDS; PHENOLS;

EID: 84927178280     PISSN: 13891723     EISSN: 13474421     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2014.04.012     Document Type: Article
Times cited : (13)

References (42)
  • 1
    • 84878243371 scopus 로고    scopus 로고
    • Chemical composition, plant secondary metabolites, and minerals of green and black teas and the effect of different tea-to-water ratios during their extraction on the composition of their spent leaves as potential additives for ruminants
    • Ramdani D., Chaudhry A.S., Seal C.J. Chemical composition, plant secondary metabolites, and minerals of green and black teas and the effect of different tea-to-water ratios during their extraction on the composition of their spent leaves as potential additives for ruminants. J.Agric. Food Chem. 2013, 61:4961-4967.
    • (2013) J.Agric. Food Chem. , vol.61 , pp. 4961-4967
    • Ramdani, D.1    Chaudhry, A.S.2    Seal, C.J.3
  • 2
    • 0042423355 scopus 로고    scopus 로고
    • Epigallocatechin-3-gallate-induced stress signals in HT-29 human colon adenocarcinoma cells
    • Chen C., Shen G., Hebbar V., Hu R., Owuor E.D., Kong A.N. Epigallocatechin-3-gallate-induced stress signals in HT-29 human colon adenocarcinoma cells. Carcinogenesis 2003, 24:1369-1378.
    • (2003) Carcinogenesis , vol.24 , pp. 1369-1378
    • Chen, C.1    Shen, G.2    Hebbar, V.3    Hu, R.4    Owuor, E.D.5    Kong, A.N.6
  • 3
    • 0030773429 scopus 로고    scopus 로고
    • Production and application of tannin acyl hydrolase: state of the art
    • Lekha P.K., Lonsane B.K. Production and application of tannin acyl hydrolase: state of the art. Adv. Appl. Microbiol. 1997, 44:215-260.
    • (1997) Adv. Appl. Microbiol. , vol.44 , pp. 215-260
    • Lekha, P.K.1    Lonsane, B.K.2
  • 5
    • 84895072248 scopus 로고    scopus 로고
    • Catechine biotransformation by tannase with sequential addition of substrate
    • Noh D.O., Choi H.-S., Suh H.J. Catechine biotransformation by tannase with sequential addition of substrate. Process Biochem. 2014, 49:271-276.
    • (2014) Process Biochem. , vol.49 , pp. 271-276
    • Noh, D.O.1    Choi, H.-S.2    Suh, H.J.3
  • 6
    • 0035528050 scopus 로고    scopus 로고
    • Review: sources, properties, applications and potential uses of tannin acyl hydrolase
    • Aguilar C.N., Gutiérrez-Sánchez G. Review: sources, properties, applications and potential uses of tannin acyl hydrolase. Food Sci. Technol. Int. 2001, 7:373-382.
    • (2001) Food Sci. Technol. Int. , vol.7 , pp. 373-382
    • Aguilar, C.N.1    Gutiérrez-Sánchez, G.2
  • 8
    • 34547937883 scopus 로고    scopus 로고
    • Enzymatic tannase treatment of green tea increases in vitro inhibitory activity against N-nitrosation of dimethylamine
    • Lu M.-J., Chen C. Enzymatic tannase treatment of green tea increases in vitro inhibitory activity against N-nitrosation of dimethylamine. Process Biochem. 2007, 42:1285-1290.
    • (2007) Process Biochem. , vol.42 , pp. 1285-1290
    • Lu, M.-J.1    Chen, C.2
  • 14
    • 0034902542 scopus 로고    scopus 로고
    • Production of tannase by Aspergillus niger Aa-20 in submerged and solid-state fermentation: influence of glucose and tannic acid
    • Aguilar C.N., Augur C., Favela-Torres E., Viniegra-Gonzalez G. Production of tannase by Aspergillus niger Aa-20 in submerged and solid-state fermentation: influence of glucose and tannic acid. J.Ind. Microbiol. Biotechnol. 2001, 26:296-302.
    • (2001) J.Ind. Microbiol. Biotechnol. , vol.26 , pp. 296-302
    • Aguilar, C.N.1    Augur, C.2    Favela-Torres, E.3    Viniegra-Gonzalez, G.4
  • 15
    • 0035143223 scopus 로고    scopus 로고
    • Induction and repression patterns of fungal tannase in solid-state and submerged cultures
    • Aguilar C.N., Augur C., Favela-Torres E., Viniegra-González G. Induction and repression patterns of fungal tannase in solid-state and submerged cultures. Process Biochem. 2001, 36:565-570.
    • (2001) Process Biochem. , vol.36 , pp. 565-570
    • Aguilar, C.N.1    Augur, C.2    Favela-Torres, E.3    Viniegra-González, G.4
  • 16
    • 39149143996 scopus 로고    scopus 로고
    • Enzymatic modification by tannase increases the antioxidant activity of green tea
    • Lu M.-J., Chen C. Enzymatic modification by tannase increases the antioxidant activity of green tea. Food Res. Int. 2008, 41:130-137.
    • (2008) Food Res. Int. , vol.41 , pp. 130-137
    • Lu, M.-J.1    Chen, C.2
  • 17
    • 0037403151 scopus 로고    scopus 로고
    • Antioxidant activity and total phenolics of edible mushroom extracts
    • Cheung L., Cheung P.C., Ooi V.E. Antioxidant activity and total phenolics of edible mushroom extracts. Food Chem. 2003, 81:249-255.
    • (2003) Food Chem. , vol.81 , pp. 249-255
    • Cheung, L.1    Cheung, P.C.2    Ooi, V.E.3
  • 19
    • 0029152168 scopus 로고
    • Polyphenols as cancer chemopreventive agents
    • Stoner G.D., Mukhtar H. Polyphenols as cancer chemopreventive agents. J.Cell. Biochem. 1995, 59:169-180.
    • (1995) J.Cell. Biochem. , vol.59 , pp. 169-180
    • Stoner, G.D.1    Mukhtar, H.2
  • 20
    • 0030748611 scopus 로고    scopus 로고
    • Parametric optimization and biochemical regulation of extracellular tannase from Aspergillus japonicus
    • Bradoo S., Gupta R., Saxena R. Parametric optimization and biochemical regulation of extracellular tannase from Aspergillus japonicus. Process Biochem. 1997, 32:135-139.
    • (1997) Process Biochem. , vol.32 , pp. 135-139
    • Bradoo, S.1    Gupta, R.2    Saxena, R.3
  • 21
    • 0036239325 scopus 로고    scopus 로고
    • Tea as a functional food for oral health
    • Wu C.D., Wei G.-X. Tea as a functional food for oral health. Nutrition 2002, 18:443-444.
    • (2002) Nutrition , vol.18 , pp. 443-444
    • Wu, C.D.1    Wei, G.-X.2
  • 22
    • 0842287839 scopus 로고    scopus 로고
    • Effects of tea polyphenols on the activities of soybean trypsin inhibitors and trypsin
    • Huang H.H., Kwok K.C., Liang H.H. Effects of tea polyphenols on the activities of soybean trypsin inhibitors and trypsin. J.Sci. Food Agric. 2004, 84:121-126.
    • (2004) J.Sci. Food Agric. , vol.84 , pp. 121-126
    • Huang, H.H.1    Kwok, K.C.2    Liang, H.H.3
  • 23
  • 26
    • 33847099548 scopus 로고    scopus 로고
    • Bioconversion of butyronitrile to butyramide using whole cells of Rhodococcus rhodochrous PA-34
    • Raj J., Seth A., Prasad S., Bhalla T.C. Bioconversion of butyronitrile to butyramide using whole cells of Rhodococcus rhodochrous PA-34. Appl. Microbiol. Biotechnol. 2007, 74:535-539.
    • (2007) Appl. Microbiol. Biotechnol. , vol.74 , pp. 535-539
    • Raj, J.1    Seth, A.2    Prasad, S.3    Bhalla, T.C.4
  • 27
    • 53549108512 scopus 로고    scopus 로고
    • Statistical optimization for tannase production from Aspergillus niger under submerged fermentation
    • Sharma S., Agarwal L., Saxena R.K. Statistical optimization for tannase production from Aspergillus niger under submerged fermentation. Indian J. Microbiol. 2007, 47:132-138.
    • (2007) Indian J. Microbiol. , vol.47 , pp. 132-138
    • Sharma, S.1    Agarwal, L.2    Saxena, R.K.3
  • 28
    • 37249052381 scopus 로고    scopus 로고
    • Characterization of tannase activity in cell-free extracts of Lactobacillus plantarum CECT 748T
    • Rodriguez H., de las Rivas B., Gomez-Cordoves C., Munoz R. Characterization of tannase activity in cell-free extracts of Lactobacillus plantarum CECT 748T. Int. J. Food Microbiol. 2008, 121:92-98.
    • (2008) Int. J. Food Microbiol. , vol.121 , pp. 92-98
    • Rodriguez, H.1    de las Rivas, B.2    Gomez-Cordoves, C.3    Munoz, R.4
  • 30
    • 0031685554 scopus 로고    scopus 로고
    • Purification, characterization, and substrate specificity of a novel highly glucose-tolerant beta-glucosidase from Aspergillus oryzae
    • Riou C., Salmon J.M., Vallier M.J., Gunata Z., Barre P. Purification, characterization, and substrate specificity of a novel highly glucose-tolerant beta-glucosidase from Aspergillus oryzae. Appl. Environ. Microbiol. 1998, 64:3607-3614.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 3607-3614
    • Riou, C.1    Salmon, J.M.2    Vallier, M.J.3    Gunata, Z.4    Barre, P.5
  • 31
    • 0037409519 scopus 로고    scopus 로고
    • Study of carbohydrate influence on protein-tannin aggregation by nephelometry
    • de Freitas V., Carvalho E., Mateus N. Study of carbohydrate influence on protein-tannin aggregation by nephelometry. Food Chem. 2003, 81:503-509.
    • (2003) Food Chem. , vol.81 , pp. 503-509
    • de Freitas, V.1    Carvalho, E.2    Mateus, N.3
  • 35
    • 0002156239 scopus 로고    scopus 로고
    • Immobilized enzymes: methods and applications
    • Springer, Berlin, A. de Meijere, K.N. Houk, H. Kessler, J.-M. Lehn, S.V. Ley, S.L. Schreiber, J. Thiem, B.M. Trost, F. Vogtle, H. Yamamoto (Eds.)
    • Tischer W., Wedekind F. Immobilized enzymes: methods and applications. Biocatalysis-from discovery to application 1999, 95-126. Springer, Berlin. A. de Meijere, K.N. Houk, H. Kessler, J.-M. Lehn, S.V. Ley, S.L. Schreiber, J. Thiem, B.M. Trost, F. Vogtle, H. Yamamoto (Eds.).
    • (1999) Biocatalysis-from discovery to application , pp. 95-126
    • Tischer, W.1    Wedekind, F.2
  • 36
    • 84884866893 scopus 로고    scopus 로고
    • Parameters affecting the performance of immobilized enzyme
    • Zhang D.-H., Yuwen L.-X., Peng L.-J. Parameters affecting the performance of immobilized enzyme. J.Chem. 2013, 2013:1-7.
    • (2013) J.Chem. , vol.2013 , pp. 1-7
    • Zhang, D.-H.1    Yuwen, L.-X.2    Peng, L.-J.3
  • 37
    • 84875631715 scopus 로고    scopus 로고
    • Potential response of soil processes to diterpenes, triterpenes and tannins: nitrification, growth of microorganisms and precipitation of proteins
    • Adamczyk S., Kiikkila O., Kitunen V., Smolander A. Potential response of soil processes to diterpenes, triterpenes and tannins: nitrification, growth of microorganisms and precipitation of proteins. Appl. Soil. Ecol. 2013, 67:47-52.
    • (2013) Appl. Soil. Ecol. , vol.67 , pp. 47-52
    • Adamczyk, S.1    Kiikkila, O.2    Kitunen, V.3    Smolander, A.4
  • 38
    • 0002401732 scopus 로고
    • Purification, characterization, and substrate relationships of the tannase from Cryphonectria parasitica
    • Farias G., Gorbea C., Elkins J., Griffin G. Purification, characterization, and substrate relationships of the tannase from Cryphonectria parasitica. Physiol. Mol. Plant Pathol. 1994, 44:51-63.
    • (1994) Physiol. Mol. Plant Pathol. , vol.44 , pp. 51-63
    • Farias, G.1    Gorbea, C.2    Elkins, J.3    Griffin, G.4
  • 39
    • 37049060576 scopus 로고
    • Gallotannins. Part I. Introduction: and the fractionation of tannase
    • Haslam E., Haworth R., Jones K., Rogers H. Gallotannins. Part I. Introduction: and the fractionation of tannase. J.Chem. Soc. (Resumed) 1961, 1829-1835.
    • (1961) J.Chem. Soc. (Resumed) , pp. 1829-1835
    • Haslam, E.1    Haworth, R.2    Jones, K.3    Rogers, H.4
  • 40
    • 37549025470 scopus 로고    scopus 로고
    • Hydrolysis of epigallocatechin gallate using a tannase from Paecilomyces variotii
    • Battestin V., Macedo G., De Freitas V. Hydrolysis of epigallocatechin gallate using a tannase from Paecilomyces variotii. Food Chem. 2008, 108:228-233.
    • (2008) Food Chem. , vol.108 , pp. 228-233
    • Battestin, V.1    Macedo, G.2    De Freitas, V.3
  • 41
    • 0033050624 scopus 로고    scopus 로고
    • ESR study on the structure-antioxidant activity relationship of tea catechins and their epimers
    • Guo Q., Zhao B.L., Shen S.R., Hou J.W., Hu J.G., Xin W.J. ESR study on the structure-antioxidant activity relationship of tea catechins and their epimers. Biochim. Biophys. Acta 1999, 1427:13-23.
    • (1999) Biochim. Biophys. Acta , vol.1427 , pp. 13-23
    • Guo, Q.1    Zhao, B.L.2    Shen, S.R.3    Hou, J.W.4    Hu, J.G.5    Xin, W.J.6
  • 42
    • 0141957301 scopus 로고    scopus 로고
    • (-)-Epigallocatechin gallate causes oxidative damage to isolated and cellular DNA
    • Furukawa A., Oikawa S., Murata M., Hiraku Y., Kawanishi S. (-)-Epigallocatechin gallate causes oxidative damage to isolated and cellular DNA. Biochem. Pharmacol. 2003, 66:1769-1778.
    • (2003) Biochem. Pharmacol. , vol.66 , pp. 1769-1778
    • Furukawa, A.1    Oikawa, S.2    Murata, M.3    Hiraku, Y.4    Kawanishi, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.