메뉴 건너뛰기




Volumn 41, Issue 8, 2006, Pages 1729-1735

A novel α-glucosidase from Chaetomium thermophilum var. coprophilum that converts maltose into trehalose: Purification and partial characterisation of the enzyme

Author keywords

Glucosidase; Chaetomium thermophilum; Maltase; Maltooligosyl trehalose synthase

Indexed keywords

GELS; GLUCOSE; PH EFFECTS; POLYPEPTIDES; THERMAL EFFECTS;

EID: 33646776730     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2006.03.017     Document Type: Article
Times cited : (23)

References (35)
  • 1
    • 0031972297 scopus 로고    scopus 로고
    • Plant α-glucosides of the glycoside hydrolase family 31. Molecular properties, substrate specifity, reaction mechanism, and comparison with family members of different origin
    • Frandsen T.P., and Svensson B. Plant α-glucosides of the glycoside hydrolase family 31. Molecular properties, substrate specifity, reaction mechanism, and comparison with family members of different origin. Plant Mol Biol 27 (1998) 1-13
    • (1998) Plant Mol Biol , vol.27 , pp. 1-13
    • Frandsen, T.P.1    Svensson, B.2
  • 2
    • 0042075003 scopus 로고    scopus 로고
    • Purification and characterization of a novel fungal α-glucosidase from Mortierella alliacea with high starch-hydrolytic activity
    • Tanaka Y., Aki T., Hidaka Y., Furuya Y., Kawamoto S., Shigeta S., et al. Purification and characterization of a novel fungal α-glucosidase from Mortierella alliacea with high starch-hydrolytic activity. Biosci Biotechnol Biochem 66 (2002) 2415-2423
    • (2002) Biosci Biotechnol Biochem , vol.66 , pp. 2415-2423
    • Tanaka, Y.1    Aki, T.2    Hidaka, Y.3    Furuya, Y.4    Kawamoto, S.5    Shigeta, S.6
  • 3
    • 0346345623 scopus 로고    scopus 로고
    • Enzymatic properties of three α-glucosidases from Aspergillus orizae
    • Kita A., Matsui H., Honma M., and Chiba S. Enzymatic properties of three α-glucosidases from Aspergillus orizae. J Appl Glycosci 43 (1996) 325-330
    • (1996) J Appl Glycosci , vol.43 , pp. 325-330
    • Kita, A.1    Matsui, H.2    Honma, M.3    Chiba, S.4
  • 4
    • 84954871548 scopus 로고
    • Substrate specificity and subsite affinities of crystalline α-glucosidase from Aspergillus niger
    • Kita A., Matsui H., Somoto A., Kimura A., Takata M., and Chiba S. Substrate specificity and subsite affinities of crystalline α-glucosidase from Aspergillus niger. Agric Biol Chem 55 (1991) 2327-2335
    • (1991) Agric Biol Chem , vol.55 , pp. 2327-2335
    • Kita, A.1    Matsui, H.2    Somoto, A.3    Kimura, A.4    Takata, M.5    Chiba, S.6
  • 5
    • 0015802212 scopus 로고
    • Properties of crystalline α-glucosidase from Mucor javanicus
    • Yamasaki Y., Miyake T., and Suzuki Y. Properties of crystalline α-glucosidase from Mucor javanicus. Agric Biol Chem 37 (1973) 251-259
    • (1973) Agric Biol Chem , vol.37 , pp. 251-259
    • Yamasaki, Y.1    Miyake, T.2    Suzuki, Y.3
  • 6
    • 0017659029 scopus 로고
    • Certain properties of α-glucosidase from Mucor racemosus
    • Yamasaki Y., Suzuki Y., and Ozawa J. Certain properties of α-glucosidase from Mucor racemosus. Agric Biol Chem 41 (1977) 1559-1565
    • (1977) Agric Biol Chem , vol.41 , pp. 1559-1565
    • Yamasaki, Y.1    Suzuki, Y.2    Ozawa, J.3
  • 7
    • 4544240287 scopus 로고
    • Purification and substrate specificity of α-glucosidase from Paecilomyces varioti AHU 9471
    • Oguma T., Matsui H., Tanida M., Takao S., Honma M., and Chiba S. Purification and substrate specificity of α-glucosidase from Paecilomyces varioti AHU 9471. Biosci Biotechnol Biochem 56 (1992) 1906-1910
    • (1992) Biosci Biotechnol Biochem , vol.56 , pp. 1906-1910
    • Oguma, T.1    Matsui, H.2    Tanida, M.3    Takao, S.4    Honma, M.5    Chiba, S.6
  • 8
    • 0017173062 scopus 로고
    • Purification and properties of α-glucosidase from Penicillium purpurogenum
    • Yamasaki Y., Susuki Y., and Ozawa J. Purification and properties of α-glucosidase from Penicillium purpurogenum. Agric Biol Chem 40 (1976) 669-676
    • (1976) Agric Biol Chem , vol.40 , pp. 669-676
    • Yamasaki, Y.1    Susuki, Y.2    Ozawa, J.3
  • 9
    • 0017702826 scopus 로고
    • Purification and properties of α-glucosidase from Penicillium oxalicum
    • Yamasaki Y., Susuki Y., and Ozawa J. Purification and properties of α-glucosidase from Penicillium oxalicum. Agric Biol Chem 41 (1977) 1451-1458
    • (1977) Agric Biol Chem , vol.41 , pp. 1451-1458
    • Yamasaki, Y.1    Susuki, Y.2    Ozawa, J.3
  • 10
    • 0000389353 scopus 로고
    • Purification, properties, and industrial significance of transglucosidase from Aspergillus niger
    • Mcleary B.V., and Gibson T.S. Purification, properties, and industrial significance of transglucosidase from Aspergillus niger. Carbohydr Res 185 (1989) 147-162
    • (1989) Carbohydr Res , vol.185 , pp. 147-162
    • Mcleary, B.V.1    Gibson, T.S.2
  • 11
    • 0042352394 scopus 로고    scopus 로고
    • Purification and characterization of a new type of α-glucosidase from Paecilomyces lilacinus that has transglycosylation activity to produce α-1,3 and α-1,2 linked oligosaccharides
    • Kobayash I., Tokuda M., Konda T., Nakano H., and Kitahata S. Purification and characterization of a new type of α-glucosidase from Paecilomyces lilacinus that has transglycosylation activity to produce α-1,3 and α-1,2 linked oligosaccharides. Biosci Biotechnol Biochem 67 (2003) 29-35
    • (2003) Biosci Biotechnol Biochem , vol.67 , pp. 29-35
    • Kobayash, I.1    Tokuda, M.2    Konda, T.3    Nakano, H.4    Kitahata, S.5
  • 12
    • 0016305880 scopus 로고
    • The metabolism of α- α-trehalose
    • Elbein A.D. The metabolism of α- α-trehalose. Adv Carbohydr Chem Biochem 30 (1974) 227-256
    • (1974) Adv Carbohydr Chem Biochem , vol.30 , pp. 227-256
    • Elbein, A.D.1
  • 13
    • 24944461127 scopus 로고    scopus 로고
    • Trehalose metabolism: enzymatic pathways and physiological functions
    • Brambl R., and Marzluf G.A. (Eds), Springer-Verlag, Berlin
    • Bonini B.M., Dijck P.-V., and Thevelein J.M. Trehalose metabolism: enzymatic pathways and physiological functions. In: Brambl R., and Marzluf G.A. (Eds). The Mycota III-biochemistry and molecular biology (2004), Springer-Verlag, Berlin 291-332
    • (2004) The Mycota III-biochemistry and molecular biology , pp. 291-332
    • Bonini, B.M.1    Dijck, P.-V.2    Thevelein, J.M.3
  • 17
    • 0004237567 scopus 로고
    • Cold Springer Harbor Laboratory Press, New York
    • Miller J.H., and Reznikoff W.S. The operon (1978), Cold Springer Harbor Laboratory Press, New York
    • (1978) The operon
    • Miller, J.H.1    Reznikoff, W.S.2
  • 18
    • 0018736190 scopus 로고
    • Induction of cellulolytic enzymes in Trichoderma reesei by sophorose
    • Sternberg D., and Mandels G.R. Induction of cellulolytic enzymes in Trichoderma reesei by sophorose. J Bacteriol 139 (1979) 761-769
    • (1979) J Bacteriol , vol.139 , pp. 761-769
    • Sternberg, D.1    Mandels, G.R.2
  • 19
    • 0029741760 scopus 로고    scopus 로고
    • Reaction mechanism of a new glycosyltrehalose-hydrolyzing enzyme isolated from the hyperthermophilic archae, Sulfolobus solfataricus KM1
    • Kato M., Miura Y., Kettoku M., Komeda T., Iwamatsu A., and Kobayashi K. Reaction mechanism of a new glycosyltrehalose-hydrolyzing enzyme isolated from the hyperthermophilic archae, Sulfolobus solfataricus KM1. Biosci Biotechnol Biochem 60 (1996) 925-928
    • (1996) Biosci Biotechnol Biochem , vol.60 , pp. 925-928
    • Kato, M.1    Miura, Y.2    Kettoku, M.3    Komeda, T.4    Iwamatsu, A.5    Kobayashi, K.6
  • 20
    • 0344096670 scopus 로고    scopus 로고
    • +2-dependent acid trehalase activity from the thermophilic fungus Chaetomium thermophilum var. coprophilum
    • +2-dependent acid trehalase activity from the thermophilic fungus Chaetomium thermophilum var. coprophilum. FEMS Microbiol Lett 171 (1999) 11-15
    • (1999) FEMS Microbiol Lett , vol.171 , pp. 11-15
    • Almeida, E.M.1    Polizeli, M.L.2    Terenzi, H.F.3    Jorge, J.A.4
  • 21
    • 0003443846 scopus 로고
    • Bergmeyer H.U. (Ed), Verlag Chimie/Academic Press, New York
    • Begmeyer H.U., and Bernt E. In: Bergmeyer H.U. (Ed). Methods of enzymatic analysis vol. 3 (1974), Verlag Chimie/Academic Press, New York 1205-1215
    • (1974) Methods of enzymatic analysis , vol.3 , pp. 1205-1215
    • Begmeyer, H.U.1    Bernt, E.2
  • 22
    • 36949089946 scopus 로고
    • Disc electrophoresis of basic protein and peptides on polyacrylamide gels
    • Reisfeld R.A., Lewis U.J., and Williams D.E. Disc electrophoresis of basic protein and peptides on polyacrylamide gels. Nature 195 (1962) 281-283
    • (1962) Nature , vol.195 , pp. 281-283
    • Reisfeld, R.A.1    Lewis, U.J.2    Williams, D.E.3
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0014478917 scopus 로고
    • Determination of enzymatic activities in polyacrylamide gels. I. Enzyme catalyzing the conversion of nonreducing substrates to reducing products
    • Gabriel O., and Wang S.F. Determination of enzymatic activities in polyacrylamide gels. I. Enzyme catalyzing the conversion of nonreducing substrates to reducing products. Anal Biochem 27 (1969) 545-554
    • (1969) Anal Biochem , vol.27 , pp. 545-554
    • Gabriel, O.1    Wang, S.F.2
  • 25
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugars and related substances
    • Dubois M., Gilles K.A., Hamilton J.K., Rebers P.A., and Simth F. Colorimetric method for determination of sugars and related substances. Anal Chem 28 (1956) 250-356
    • (1956) Anal Chem , vol.28 , pp. 250-356
    • Dubois, M.1    Gilles, K.A.2    Hamilton, J.K.3    Rebers, P.A.4    Simth, F.5
  • 27
    • 0003039477 scopus 로고
    • Sigraf-a versatile computer program for fitting enzyme kinetic data
    • Leone F.A., Degreve L., and Baranauskas J.A. Sigraf-a versatile computer program for fitting enzyme kinetic data. Biochem Educ 20 (1992) 94-96
    • (1992) Biochem Educ , vol.20 , pp. 94-96
    • Leone, F.A.1    Degreve, L.2    Baranauskas, J.A.3
  • 28
    • 3242716846 scopus 로고    scopus 로고
    • Purification and purification of Acremonium implicatum α-glucosidase having regioselectivity for α-1,3-glucosidic linkage
    • Yamamoto T., Unno T., Watanabe Y., Yamamoto M., Okuyama M., Mori H., et al. Purification and purification of Acremonium implicatum α-glucosidase having regioselectivity for α-1,3-glucosidic linkage. Biochim Biophys Acta 1700 (2004) 189-198
    • (2004) Biochim Biophys Acta , vol.1700 , pp. 189-198
    • Yamamoto, T.1    Unno, T.2    Watanabe, Y.3    Yamamoto, M.4    Okuyama, M.5    Mori, H.6
  • 29
    • 23744447380 scopus 로고    scopus 로고
    • Purification and characterization of the hyper-glycosylated extracellular α-glucosidase from Schizosaccharomyces pombe
    • Okuyama M., Tanimoto Y., Ito T., Anzai A., Mori H., Kimura A., et al. Purification and characterization of the hyper-glycosylated extracellular α-glucosidase from Schizosaccharomyces pombe. Enzyme Microb Technol 37 (2005) 472-480
    • (2005) Enzyme Microb Technol , vol.37 , pp. 472-480
    • Okuyama, M.1    Tanimoto, Y.2    Ito, T.3    Anzai, A.4    Mori, H.5    Kimura, A.6
  • 31
    • 0030573172 scopus 로고    scopus 로고
    • Characterization of the trehalase system from the thermophilic fungus Scytalidium thermophilum
    • Kadowaki M.K., Polizeli M.L., Terenzi H.F., and Jorge J.A. Characterization of the trehalase system from the thermophilic fungus Scytalidium thermophilum. Biochim Biophys Acta 1291 (1996) 199-205
    • (1996) Biochim Biophys Acta , vol.1291 , pp. 199-205
    • Kadowaki, M.K.1    Polizeli, M.L.2    Terenzi, H.F.3    Jorge, J.A.4
  • 32
    • 0343724851 scopus 로고    scopus 로고
    • Biochemical characterization of glucoamylase from the hyperproducer exo-1 mutant strain of Neurospora crassa
    • Spinelli L.B.B., Polizeli M.L., Terenzi H.F., and Jorge J.A. Biochemical characterization of glucoamylase from the hyperproducer exo-1 mutant strain of Neurospora crassa. FEMS Microbiol Lett 138 (1996) 173-178
    • (1996) FEMS Microbiol Lett , vol.138 , pp. 173-178
    • Spinelli, L.B.B.1    Polizeli, M.L.2    Terenzi, H.F.3    Jorge, J.A.4
  • 33
    • 8644245771 scopus 로고    scopus 로고
    • Trehalose synthase of Mycobacterium smegmatis: purification, cloning, expression, and properties of the enzyme
    • Pan Y.T., Edavana V.K., Jourdian W.J., Edmondson R., Carroll J.D., Pastuszal I., et al. Trehalose synthase of Mycobacterium smegmatis: purification, cloning, expression, and properties of the enzyme. Eur J Biochem 271 (2004) 4259-4269
    • (2004) Eur J Biochem , vol.271 , pp. 4259-4269
    • Pan, Y.T.1    Edavana, V.K.2    Jourdian, W.J.3    Edmondson, R.4    Carroll, J.D.5    Pastuszal, I.6
  • 34
    • 27144498562 scopus 로고    scopus 로고
    • Production of trehalose by intramolecular transglycosylation of maltose catalysed by a new enzyme from Thermus thermophilus HB-8
    • Zdzieblo A., and Synowiecki J. Production of trehalose by intramolecular transglycosylation of maltose catalysed by a new enzyme from Thermus thermophilus HB-8. Food Chem 96 (2006) 8-13
    • (2006) Food Chem , vol.96 , pp. 8-13
    • Zdzieblo, A.1    Synowiecki, J.2
  • 35
    • 0029150144 scopus 로고
    • Transglucosylation of a fungal α-glucosidase. The enzyme properties and correlations of isomaltooligosacharide production
    • Duan K.J., Sheu D.C., and Lin C.T. Transglucosylation of a fungal α-glucosidase. The enzyme properties and correlations of isomaltooligosacharide production. Ann N Y Acad Sci 750 (1995) 325-328
    • (1995) Ann N Y Acad Sci , vol.750 , pp. 325-328
    • Duan, K.J.1    Sheu, D.C.2    Lin, C.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.