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Volumn 25, Issue 1-2, 1999, Pages 3-14

Microbial β-N-acetylhexosaminidases and their biotechnological applications

Author keywords

Applications; Chitobiase; Microbial N acetylhexosaminidase; Sequence

Indexed keywords

AMINO ACIDS; CATALYSIS; FUNGI; POLYSACCHARIDES; SYNTHESIS (CHEMICAL);

EID: 0032998434     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0141-0229(98)00171-9     Document Type: Review
Times cited : (53)

References (129)
  • 1
    • 3342910756 scopus 로고
    • Hexosaminidases
    • E.A. Balazs, & R.W. Jeanloz. New York: Academic Press
    • Walker P.G. Hexosaminidases. Balazs E.A., Jeanloz R.W. The amino sugars, Vol. 2B. 1966;155-169 Academic Press, New York.
    • (1966) The Amino Sugars, Vol. 2B , pp. 155-169
    • Walker, P.G.1
  • 2
    • 0345109845 scopus 로고
    • Chitin: Accomplishments and perspectives
    • J.P. Zikakis. New York: Academic Press
    • Brine C.J. Chitin Accomplishments and perspectives . Zikakis J.P. Chitin, chitosan and related enzymes. 1984;18-24 Academic Press, New York.
    • (1984) Chitin, Chitosan and Related Enzymes , pp. 18-24
    • Brine, C.J.1
  • 3
    • 0002256521 scopus 로고
    • Physiology of microbial degradation of chitin and chitosan
    • C. Ratledge. Dordecht: Kluwer
    • Gooday G.W. Physiology of microbial degradation of chitin and chitosan. Ratledge C. Biochemistry of microbial degradation. 1993;279-312 Kluwer, Dordecht.
    • (1993) Biochemistry of Microbial Degradation , pp. 279-312
    • Gooday, G.W.1
  • 4
    • 0026331471 scopus 로고
    • A complex chitinolytic system in exponentially growing mycelium of Mucor rouxi: Properties and function
    • Rast D.M., Horsch M., Furter R., Gooday G.W. A complex chitinolytic system in exponentially growing mycelium of Mucor rouxi Properties and function . J Gen Microbiol. 137:1991;2792-2810.
    • (1991) J Gen Microbiol , vol.137 , pp. 2792-2810
    • Rast, D.M.1    Horsch, M.2    Furter, R.3    Gooday, G.W.4
  • 5
    • 0345586800 scopus 로고
    • Mise en évidence et propriétés d'une N-acétyl-β-D-glucosaminidase exocellulaire chez Botrytis cinerea, champignon parasite du raisin
    • Grassin C., Dubourdieu D., Koh K.H., Ribéreau-Gayon P. Mise en évidence et propriétés d'une N-acétyl-β-D-glucosaminidase exocellulaire chez Botrytis cinerea, champignon parasite du raisin. C R Acad Sc Paris. 304:1987;381-384.
    • (1987) C R Acad Sc Paris , vol.304 , pp. 381-384
    • Grassin, C.1    Dubourdieu, D.2    Koh, K.H.3    Ribéreau-Gayon, P.4
  • 6
    • 0017228929 scopus 로고
    • Purification and properties of β-N-acetylglucosaminidase from Escherichia coli
    • Yem D.W., Wu H.C. Purification and properties of β-N-acetylglucosaminidase from Escherichia coli. J Bacteriol. 125:1976;324-331.
    • (1976) J Bacteriol , vol.125 , pp. 324-331
    • Yem, D.W.1    Wu, H.C.2
  • 7
    • 0001519173 scopus 로고
    • Plant chitinases are potent inhibitors of fungal growth
    • Schlumbaum A., Manch F., Vögeli V., Boller T. Plant chitinases are potent inhibitors of fungal growth. Nature (London). 324:1986;365-367.
    • (1986) Nature (London) , vol.324 , pp. 365-367
    • Schlumbaum, A.1    Manch, F.2    Vögeli, V.3    Boller, T.4
  • 8
    • 0024850749 scopus 로고
    • Lysosomal degradation of asparagine-linked glycoproteins
    • Aronson N.N., Kuranda M.J. Lysosomal degradation of asparagine-linked glycoproteins. FASEB J. 3:1989;2615-2622.
    • (1989) FASEB J , vol.3 , pp. 2615-2622
    • Aronson, N.N.1    Kuranda, M.J.2
  • 10
    • 0001645848 scopus 로고
    • Mannosyl- And xylosyl-containing glycans promote tomato (Lycopersicon esculetum Mill
    • Priem B., Gross K.C. Mannosyl- and xylosyl-containing glycans promote tomato (Lycopersicon esculetum Mill. ) fruit ripening. Plant Physiol. 98:1992;399-401.
    • (1992) ) Fruit Ripening. Plant Physiol , vol.98 , pp. 399-401
    • Priem, B.1    Gross, K.C.2
  • 12
    • 0025361205 scopus 로고
    • Symbiotic host-specificity of Rhizobium meliloti is determined by a sulphated and acylated glucosamine oligosaccharide signal
    • Lerouge P., Roche P., Faucher C., Maillet F., Truchet G., Promé J.C., Dénarié J. Symbiotic host-specificity of Rhizobium meliloti is determined by a sulphated and acylated glucosamine oligosaccharide signal. Nature (London). 344:1990;781-784.
    • (1990) Nature (London) , vol.344 , pp. 781-784
    • Lerouge, P.1    Roche, P.2    Faucher, C.3    Maillet, F.4    Truchet, G.5    Promé, J.C.6    Dénarié, J.7
  • 13
    • 85008733163 scopus 로고
    • Immunopotentiating function of N-acetylchitooligosaccharides and chitooligosaccharides
    • Suzuki S. Immunopotentiating function of N-acetylchitooligosaccharides and chitooligosaccharides. Nihon Nogeikagu Kaishi. 62:1988;1241-1242.
    • (1988) Nihon Nogeikagu Kaishi , vol.62 , pp. 1241-1242
    • Suzuki, S.1
  • 16
    • 0024709802 scopus 로고
    • Some comments on the type references of the official nomenclature (IUB) for β-N-acetylglucosaminidase, β-N-acetylhexosaminidase and β-N-acetylgalactosaminidase
    • Cabezas J.A. Some comments on the type references of the official nomenclature (IUB) for β-N-acetylglucosaminidase, β-N-acetylhexosaminidase and β-N-acetylgalactosaminidase. Biochem J. 261:1989;1059-1060.
    • (1989) Biochem J , vol.261 , pp. 1059-1060
    • Cabezas, J.A.1
  • 17
    • 0018379543 scopus 로고
    • Purification and characterization of an extracellular β-N-acetylhexosaminidase from Paecilomyces persicinus
    • Eriquez L.A., Pisano M.A. Purification and characterization of an extracellular β-N-acetylhexosaminidase from Paecilomyces persicinus. J Bacteriol. 137:1979;620-626.
    • (1979) J Bacteriol , vol.137 , pp. 620-626
    • Eriquez, L.A.1    Pisano, M.A.2
  • 18
    • 84985200222 scopus 로고
    • The formation of N-acetyl-β-D-hexosaminidase is repressed by glucose in Penicillium chrysogenum
    • Pócsi I., Pusztàhelyi T., Bogáti MSz, Szentirmai A. The formation of N-acetyl-β-D-hexosaminidase is repressed by glucose in Penicillium chrysogenum. J Basic Microbiol. 33:1993;259-267.
    • (1993) J Basic Microbiol , vol.33 , pp. 259-267
    • Pócsi, I.1    Pusztàhelyi, T.2    Bogáti, M.3    Szentirmai, A.4
  • 19
    • 0000819044 scopus 로고
    • Purification and characterization of β-N-acetylhexosaminidase from Penicillium oxalicum
    • Yamamoto K., Lee K.M., Kumagai H., Tochikura T. Purification and characterization of β-N-acetylhexosaminidase from Penicillium oxalicum. Agric Biol Chem. 49:1985;611-619.
    • (1985) Agric Biol Chem , vol.49 , pp. 611-619
    • Yamamoto, K.1    Lee, K.M.2    Kumagai, H.3    Tochikura, T.4
  • 20
    • 0001499738 scopus 로고
    • Purification and characterization of β-N-acetylhexosaminidase from Pycnoporus cinnabarinus
    • Ohtakara A., Yoshida M., Murakami M., Izumi T. Purification and characterization of β-N-acetylhexosaminidase from Pycnoporus cinnabarinus. Agric Biol Chem. 45:1981;239-247.
    • (1981) Agric Biol Chem , vol.45 , pp. 239-247
    • Ohtakara, A.1    Yoshida, M.2    Murakami, M.3    Izumi, T.4
  • 21
    • 0026248355 scopus 로고
    • Purification and characterization of β-N-acetylhexosaminidase from Trichoderma harzianum
    • Koga K., Iwamoto Y., Sakamoto H., Hatano K., Sano M., Kato I. Purification and characterization of β-N-acetylhexosaminidase from Trichoderma harzianum. Agric Biol Chem. 55:1991;2817-2823.
    • (1991) Agric Biol Chem , vol.55 , pp. 2817-2823
    • Koga, K.1    Iwamoto, Y.2    Sakamoto, H.3    Hatano, K.4    Sano, M.5    Kato, I.6
  • 22
    • 0015623796 scopus 로고
    • The purification and properties of extracellular glycosidases of the cellular slime mold Dictyostelium discoideum
    • Every D., Ashworth J.M. The purification and properties of extracellular glycosidases of the cellular slime mold Dictyostelium discoideum. J Biochem. 133:1973;37-47.
    • (1973) J Biochem , vol.133 , pp. 37-47
    • Every, D.1    Ashworth, J.M.2
  • 23
    • 0022494319 scopus 로고
    • Purification and properties of β-N-acetylhexosaminidase from Mucor fragilis grown in bovine blood
    • Yamamoto K., Tsuji Y., Matsushita S., Kumagai H., Tochikura T. Purification and properties of β-N-acetylhexosaminidase from Mucor fragilis grown in bovine blood. Appl Environ Microbiol. 51:1986;1019-1023.
    • (1986) Appl Environ Microbiol , vol.51 , pp. 1019-1023
    • Yamamoto, K.1    Tsuji, Y.2    Matsushita, S.3    Kumagai, H.4    Tochikura, T.5
  • 24
    • 0016315665 scopus 로고
    • Immunological evidence to show that the N-acetylglucosaminidase and N-acetylgalactosaminidase activities of Dictyostelium discoideum reside in the same protein molecule
    • Every D., Ashworth J.M. Immunological evidence to show that the N-acetylglucosaminidase and N-acetylgalactosaminidase activities of Dictyostelium discoideum reside in the same protein molecule. J Biochem. 143:1974;785-787.
    • (1974) J Biochem , vol.143 , pp. 785-787
    • Every, D.1    Ashworth, J.M.2
  • 25
    • 0028015702 scopus 로고
    • Purification and characterization of two forms of N-acetylglucosaminidase from Candida albicans showing outer chain glycosylation
    • Molloy C., Cannon R.D., Sullivan P.A., Shepherd M.G. Purification and characterization of two forms of N-acetylglucosaminidase from Candida albicans showing outer chain glycosylation. Microbiology. 140:1994;1543-1553.
    • (1994) Microbiology , vol.140 , pp. 1543-1553
    • Molloy, C.1    Cannon, R.D.2    Sullivan, P.A.3    Shepherd, M.G.4
  • 26
    • 0030832677 scopus 로고    scopus 로고
    • Purification and characterization of a thermostable and highly specific β-N-acetyl-D-glucosaminidase from Aspergillus niger 419
    • Pera L.M., Infante Majollí M.V., Baigorí M.D. Purification and characterization of a thermostable and highly specific β-N-acetyl-D-glucosaminidase from Aspergillus niger 419. Biotechnol Appl Biochem. 26:1997;183-187.
    • (1997) Biotechnol Appl Biochem , vol.26 , pp. 183-187
    • Pera, L.M.1    Infante Majollí, M.V.2    Baigorí, M.D.3
  • 27
  • 28
    • 0345541257 scopus 로고
    • Phosphatase, esterase, N-acetylglucosaminidase, and adenosine triphosphatase of group A Streptococci (35639)
    • Ginsburg I., Heller M., Gallis H.A. Phosphatase, esterase, N-acetylglucosaminidase, and adenosine triphosphatase of group A Streptococci (35639). Proc Soc Exp Biol Med. 137:1971;645-652.
    • (1971) Proc Soc Exp Biol Med , vol.137 , pp. 645-652
    • Ginsburg, I.1    Heller, M.2    Gallis, H.A.3
  • 29
    • 0028861654 scopus 로고
    • Purification and characterization of novel glycosidases from the bacterial genus Xanthomonas
    • Wong-Madden S.T., Landry D. Purification and characterization of novel glycosidases from the bacterial genus Xanthomonas. Glycobiology. 5:1995;19-28.
    • (1995) Glycobiology , vol.5 , pp. 19-28
    • Wong-Madden, S.T.1    Landry, D.2
  • 30
    • 0030451823 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel β-N-acetyl-D-glucosaminidase from Vibrio furnissii
    • Chitlaru E., Roseman S. Molecular cloning and characterization of a novel β-N-acetyl-D-glucosaminidase from Vibrio furnissii. J Biol Chem. 271:1996;33433-33439.
    • (1996) J Biol Chem , vol.271 , pp. 33433-33439
    • Chitlaru, E.1    Roseman, S.2
  • 31
    • 0001558035 scopus 로고
    • Purification and some properties of β-N-acetylglucosaminidase from Aeromonas sp. 10S-24
    • Ueda M., Arai M. Purification and some properties of β-N-acetylglucosaminidase from Aeromonas sp. 10S-24. Biosci Biotech Biochem. 56:1992;1204-1207.
    • (1992) Biosci Biotech Biochem , vol.56 , pp. 1204-1207
    • Ueda, M.1    Arai, M.2
  • 32
    • 0028795512 scopus 로고
    • Molecular cloning of the gene which encodes β-N-acetylglucosaminidase from a marine bacterium. Alteromonas sp. strain O-7
    • Tsujibo H., Fujimoto K., Tanno H., Miyamoto Y., Imada C., Okami Y., Inamori Y. Molecular cloning of the gene which encodes β-N-acetylglucosaminidase from a marine bacterium. Alteromonas sp. strain O-7. Appl Environ Microbiol. 61:1995;804-806.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 804-806
    • Tsujibo, H.1    Fujimoto, K.2    Tanno, H.3    Miyamoto, Y.4    Imada, C.5    Okami, Y.6    Inamori, Y.7
  • 33
    • 0028000419 scopus 로고
    • Gene sequence, purification, and characterization of N-acetyl-β-glucosaminidase from a marine bacterium, Alteromonas sp. strain O-7
    • Tsujibo H., Fujimoto K., Tanno H., Miyamoto K., Imada C., Okami Y., Inamori Y. Gene sequence, purification, and characterization of N-acetyl-β-glucosaminidase from a marine bacterium, Alteromonas sp. strain O-7. Gene. 146:1994;111-115.
    • (1994) Gene , vol.146 , pp. 111-115
    • Tsujibo, H.1    Fujimoto, K.2    Tanno, H.3    Miyamoto, K.4    Imada, C.5    Okami, Y.6    Inamori, Y.7
  • 34
    • 49749153849 scopus 로고
    • The chitinase system of a strain of Streptomyces griseus
    • Berger L.R., Reynolds D.M. The chitinase system of a strain of Streptomyces griseus. Biochim Biophys Acta. 29:1958;522-533.
    • (1958) Biochim Biophys Acta , vol.29 , pp. 522-533
    • Berger, L.R.1    Reynolds, D.M.2
  • 35
    • 0026708939 scopus 로고
    • Thermostable, salt tolerant, wide pH range novel chitobiase from Vibrio parahemolyticus: Isolation, characterization, molecular cloning, and expression
    • Zhu B.C.R., Lo J.-Y., Li Y.-T., Li S.-C., Jaynes J.M., Gildemeister O.S., Laine R.A., Ou C-Y. Thermostable, salt tolerant, wide pH range novel chitobiase from Vibrio parahemolyticus Isolation, characterization, molecular cloning, and expression . J Biochem. 112:1992;163-167.
    • (1992) J Biochem , vol.112 , pp. 163-167
    • Zhu, B.C.R.1    Lo, J.-Y.2    Li, Y.-T.3    Li, S.-C.4    Jaynes, J.M.5    Gildemeister, O.S.6    Laine, R.A.7    Ou, C.-Y.8
  • 36
    • 0014670217 scopus 로고
    • Glycosidases of Aspergillus niger
    • Bahl O.P., Agrawal K.M.L. Glycosidases of Aspergillus niger. J Biol Chem. 244:1969;2970-2978.
    • (1969) J Biol Chem , vol.244 , pp. 2970-2978
    • Bahl, O.P.1    Agrawal, K.M.L.2
  • 37
    • 0019289005 scopus 로고
    • Purification, properties, kinetics, and mechanism of β-N-acetylglucosaminidase from Aspergillus niger
    • Jones C.S., Kosman D.J. Purification, properties, kinetics, and mechanism of β-N-acetylglucosaminidase from Aspergillus niger. J Biol Chem. 255:1980;11861-11869.
    • (1980) J Biol Chem , vol.255 , pp. 11861-11869
    • Jones, C.S.1    Kosman, D.J.2
  • 38
    • 0021200940 scopus 로고
    • The secretion of N-acetylhexosaminidase during germ-tube formation in Candida albicans
    • Sullivan P.A., McHugh N.J., Romana L.K., Shepherd M.G. The secretion of N-acetylhexosaminidase during germ-tube formation in Candida albicans. J Gen Microbiol. 130:1984;2213-2218.
    • (1984) J Gen Microbiol , vol.130 , pp. 2213-2218
    • Sullivan, P.A.1    McHugh, N.J.2    Romana, L.K.3    Shepherd, M.G.4
  • 39
    • 0028301746 scopus 로고
    • Molecular cloning and expression of the Candida albicans β-N-acetylhexosaminidase (HEX1) gene
    • Cannon R.D., Niimi K., Jenkinson H.F., Shepherd M.G. Molecular cloning and expression of the Candida albicans β-N-acetylhexosaminidase (HEX1) gene. J Bacteriol. 176:1994;2640-2647.
    • (1994) J Bacteriol , vol.176 , pp. 2640-2647
    • Cannon, R.D.1    Niimi, K.2    Jenkinson, H.F.3    Shepherd, M.G.4
  • 40
    • 0028166467 scopus 로고
    • Extracellular β-N-acetylhexosaminidases of Gliocladium virens RV14
    • van Tilburg A.-U.B., Thomas M.D. Extracellular β-N-acetylhexosaminidases of Gliocladium virens RV14. Enzyme Microb Technol. 16:1994;849-854.
    • (1994) Enzyme Microb Technol , vol.16 , pp. 849-854
    • Van Tilburg, A.-U.B.1    Thomas, M.D.2
  • 41
    • 0017838045 scopus 로고
    • Purification and characterization of β-D-mannosidase and β-N-acetylhexosaminidase of Tremella fuciformis
    • Sone Y., Misaki A. Purification and characterization of β-D-mannosidase and β-N-acetylhexosaminidase of Tremella fuciformis. J Biochem. 83:1978;1135-1144.
    • (1978) J Biochem , vol.83 , pp. 1135-1144
    • Sone, Y.1    Misaki, A.2
  • 42
    • 0026248355 scopus 로고
    • Purification and characterization of β-N-acetylhexosaminidase from Trichoderma harzianum
    • Koga K., Iwamoto Y., Sakamoto H., Hatano K., Sano M., Kato I. Purification and characterization of β-N-acetylhexosaminidase from Trichoderma harzianum. Agric Biol Chem. 55:1991;2817-2823.
    • (1991) Agric Biol Chem , vol.55 , pp. 2817-2823
    • Koga, K.1    Iwamoto, Y.2    Sakamoto, H.3    Hatano, K.4    Sano, M.5    Kato, I.6
  • 43
    • 0020694740 scopus 로고
    • The chitin-degrading enzyme system of a Streptomyces species
    • Charpentier M., Percheron F. The chitin-degrading enzyme system of a Streptomyces species. Int J Biochem. 15:1983;289-292.
    • (1983) Int J Biochem , vol.15 , pp. 289-292
    • Charpentier, M.1    Percheron, F.2
  • 44
    • 0030447616 scopus 로고    scopus 로고
    • The chitin catabolic cascade in the marine bacterium Vibrio furnissii
    • Keyhani N.O., Roseman S. The chitin catabolic cascade in the marine bacterium Vibrio furnissii. J Biol Chem. 271:1996;33425-33432.
    • (1996) J Biol Chem , vol.271 , pp. 33425-33432
    • Keyhani, N.O.1    Roseman, S.2
  • 45
    • 0001330973 scopus 로고
    • Purification, properties, and transglycosylation reaction of β-N-acetylhexosaminidase from Nocardia orientalis
    • Nanjo F, Ishikawa, Katsumi R, Sakai K. Purification, properties, and transglycosylation reaction of β-N-acetylhexosaminidase from Nocardia orientalis. Agric Biol Chem 1990;54:899-906.
    • (1990) Agric Biol Chem , vol.54 , pp. 899-906
    • Nanjo, F.1    Ishikawa Katsumi, R.2    Sakai, K.3
  • 46
    • 0024757890 scopus 로고
    • β-N-acetylglucosaminidase from Aspergillus nidulans which degrades chitin oligomers during autolysis
    • Reyes F., Calatayud J., Vazquez C., Martínez M.J. β-N-acetylglucosaminidase from Aspergillus nidulans which degrades chitin oligomers during autolysis. FEMS Microbiol Lett. 65:1989;83-88.
    • (1989) FEMS Microbiol Lett , vol.65 , pp. 83-88
    • Reyes, F.1    Calatayud, J.2    Vazquez, C.3    Martínez, M.J.4
  • 47
    • 0000424066 scopus 로고
    • Characterization of chitinase and chitobiase produced by the entomopathogenic fungus Metarhizium anisopliae
    • St. Leger R.J., Cooper R.M., Charnley A.K. Characterization of chitinase and chitobiase produced by the entomopathogenic fungus Metarhizium anisopliae. J Invertebr Pathol. 58:1991;415-426.
    • (1991) J Invertebr Pathol , vol.58 , pp. 415-426
    • St. Leger, R.J.1    Cooper, R.M.2    Charnley, A.K.3
  • 48
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B., Bairoch A. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. J Biochem. 293:1993;781-788.
    • (1993) J Biochem , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 49
    • 0029940470 scopus 로고    scopus 로고
    • Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease
    • Tews I., Perrakis A., Oppenheim A., Dauter Z., Wilson K.S., Vorgias C.E. Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease. Nature Struct Biol. 3:1996;638-648.
    • (1996) Nature Struct Biol , vol.3 , pp. 638-648
    • Tews, I.1    Perrakis, A.2    Oppenheim, A.3    Dauter, Z.4    Wilson, K.S.5    Vorgias, C.E.6
  • 50
    • 0027197513 scopus 로고
    • Sequence analysis of the β-N-acetylhexosaminidase gene of Vibrio vulnificus: Evidence for a common evolutionary origin of hexosaminidases
    • Somerville C.C., Colwell R.R. Sequence analysis of the β-N-acetylhexosaminidase gene of Vibrio vulnificus evidence for a common evolutionary origin of hexosaminidases . Proc Natl Acad Sci USA. 90:1993;6751-6755.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 6751-6755
    • Somerville, C.C.1    Colwell, R.R.2
  • 51
    • 0023709331 scopus 로고
    • Molecular cloning of the cDNA which encodes β-N-acetylhexosaminidase A from Dictyostelium discoideum
    • Graham T.R., Zassenhaus H.P., Kaplan A. Molecular cloning of the cDNA which encodes β-N-acetylhexosaminidase A from Dictyostelium discoideum. J Biol Chem. 263:1988;16823-16829.
    • (1988) J Biol Chem , vol.263 , pp. 16823-16829
    • Graham, T.R.1    Zassenhaus, H.P.2    Kaplan, A.3
  • 52
    • 0014824951 scopus 로고
    • Studies on N-acetyl-β-D-glucosaminidase of Aspergillus oryzae. Purification and characterization of N-acetyl-β-D-glucosaminidase obtained from Takadiastase
    • Mega T., Ikenaka T., Matsushima Y. Studies on N-acetyl-β-D-glucosaminidase of Aspergillus oryzae. Purification and characterization of N-acetyl-β-D-glucosaminidase obtained from Takadiastase. J Biochem. 68:1970;109-117.
    • (1970) J Biochem , vol.68 , pp. 109-117
    • Mega, T.1    Ikenaka, T.2    Matsushima, Y.3
  • 53
    • 0025473788 scopus 로고
    • Purification and characterization of β-N-acetylhexosaminidase from Aspergillus tamarii
    • Tao Y., Yan Z.-Z., Sun J.-W., Cheng X.-L., Zhang S-Z. Purification and characterization of β-N-acetylhexosaminidase from Aspergillus tamarii. Acta Microbiol Sin. 30:1990;259-266.
    • (1990) Acta Microbiol Sin , vol.30 , pp. 259-266
    • Tao, Y.1    Yan, Z.-Z.2    Sun, J.-W.3    Cheng, X.-L.4    Zhang, S.-Z.5
  • 54
    • 0028608789 scopus 로고
    • Cloning and expression in Escherichia coli of the nahA gene from Porphyromonas gingivalis indicates that β-N-acetylhexosaminidase is an outer-membrane-associated lipoprotein
    • Lovatt A., Roberts I.S. Cloning and expression in Escherichia coli of the nahA gene from Porphyromonas gingivalis indicates that β-N-acetylhexosaminidase is an outer-membrane-associated lipoprotein. Microbiology. 140:1994;3399-3406.
    • (1994) Microbiology , vol.140 , pp. 3399-3406
    • Lovatt, A.1    Roberts, I.S.2
  • 55
    • 0024962415 scopus 로고
    • N,N′-Diacetylchitobiase of Vibrio harveyi
    • Soto-Gill R.W., Zyskind J.W. N,N′-Diacetylchitobiase of Vibrio harveyi. J Biol Chem. 264:1989;14778-14783.
    • (1989) J Biol Chem , vol.264 , pp. 14778-14783
    • Soto-Gill, R.W.1    Zyskind, J.W.2
  • 56
    • 0028988019 scopus 로고
    • Cloning and expression of the β-N-acetylglucosaminidase gene from Streptococcus pneumoniae
    • Clarke V.A., Platt N., Butters T.D. Cloning and expression of the β-N-acetylglucosaminidase gene from Streptococcus pneumoniae. J Biol Chem. 270:1995;8805-8814.
    • (1995) J Biol Chem , vol.270 , pp. 8805-8814
    • Clarke, V.A.1    Platt, N.2    Butters, T.D.3
  • 57
    • 0029988664 scopus 로고    scopus 로고
    • N-acetylglucosaminidase (chitobiase) from Serratia marcescens: Gene sequence, and protein production and purification in Escherichia coli
    • Tews I., Vincentelli R., Vorgias C.E. N-acetylglucosaminidase (chitobiase) from Serratia marcescens gene sequence, and protein production and purification in Escherichia coli . Gene. 170:1996;63-67.
    • (1996) Gene , vol.170 , pp. 63-67
    • Tews, I.1    Vincentelli, R.2    Vorgias, C.E.3
  • 58
    • 11944256494 scopus 로고
    • Catalytic mechanisms of enzymic glycosyl transfer
    • Sinnot M.L. Catalytic mechanisms of enzymic glycosyl transfer. Chem Rev. 90:1990;1171-1202.
    • (1990) Chem Rev , vol.90 , pp. 1171-1202
    • Sinnot, M.L.1
  • 59
    • 0027297246 scopus 로고
    • Chitinases of fungi and plants: Their involvement in morphogenesis and host-parasite interaction
    • Sahai A.S., Manocha M.S. Chitinases of fungi and plants their involvement in morphogenesis and host-parasite interaction . FEMS Microbiol Rev. 11:1993;317-338.
    • (1993) FEMS Microbiol Rev , vol.11 , pp. 317-338
    • Sahai, A.S.1    Manocha, M.S.2
  • 60
    • 0000966243 scopus 로고
    • Chitin as a nitrogen source for mycorrhizal fungi
    • Leake J.R., Read D.J. Chitin as a nitrogen source for mycorrhizal fungi. Mycological Res. 94:1990;993-995.
    • (1990) Mycological Res , vol.94 , pp. 993-995
    • Leake, J.R.1    Read, D.J.2
  • 61
    • 0027535156 scopus 로고
    • Regulation of extracellular N-acetyl-D-glucosaminidase production in the entomopathogenic fungus Beauveria bassiana
    • Bidochka M.J., Khachatourians G.G. Regulation of extracellular N-acetyl-D-glucosaminidase production in the entomopathogenic fungus Beauveria bassiana. Can J Microbiol. 39:1993;6-12.
    • (1993) Can J Microbiol , vol.39 , pp. 6-12
    • Bidochka, M.J.1    Khachatourians, G.G.2
  • 62
    • 0000113161 scopus 로고
    • Chitinolytic enzymes produced by Trichoderma harzianum: Antifungal activity of purified endochitinase and chitobiosidase
    • Lorito M., Harman G.E., Hayes C.K., Broadway R.M., Trosmo A., Woo S.L., Di Pietro A. Chitinolytic enzymes produced by Trichoderma harzianum antifungal activity of purified endochitinase and chitobiosidase . Phytopathology. 83:1993;302-307.
    • (1993) Phytopathology , vol.83 , pp. 302-307
    • Lorito, M.1    Harman, G.E.2    Hayes, C.K.3    Broadway, R.M.4    Trosmo, A.5    Woo, S.L.6    Di Pietro, A.7
  • 63
    • 0026315591 scopus 로고
    • Purification and characterization of an extracellular chitobiase from Trichoderma harzianum
    • Uhloa C.J., Peberdy J.F. Purification and characterization of an extracellular chitobiase from Trichoderma harzianum. Curr Microbiol. 23:1991;285-289.
    • (1991) Curr Microbiol , vol.23 , pp. 285-289
    • Uhloa, C.J.1    Peberdy, J.F.2
  • 64
    • 0015584248 scopus 로고
    • Partial purification and properties of a β-N-acetylglucosaminidase from the fungus Sclerotinia fructigena
    • Reyes F., Byrde R.J. Partial purification and properties of a β-N-acetylglucosaminidase from the fungus Sclerotinia fructigena. J Biochem. 131:1973;381-388.
    • (1973) J Biochem , vol.131 , pp. 381-388
    • Reyes, F.1    Byrde, R.J.2
  • 65
    • 0016286437 scopus 로고
    • Vegetative isozyme of N-acetylglucosaminidase in Dictyostelium discoideum
    • Dimond R.L., Loomis W.F. Vegetative isozyme of N-acetylglucosaminidase in Dictyostelium discoideum. J Biol Chem. 249:1974;5628-5632.
    • (1974) J Biol Chem , vol.249 , pp. 5628-5632
    • Dimond, R.L.1    Loomis, W.F.2
  • 66
    • 0023709331 scopus 로고
    • Molecular cloning of the cDNA which encodes β-N-acetylhexosaminidase A from Dictyostelium discoideum
    • Graham T.R., Zassenhaus H.P., Kaplan A. Molecular cloning of the cDNA which encodes β-N-acetylhexosaminidase A from Dictyostelium discoideum. J Biol Chem. 263:1988;16823-16829.
    • (1988) J Biol Chem , vol.263 , pp. 16823-16829
    • Graham, T.R.1    Zassenhaus, H.P.2    Kaplan, A.3
  • 67
    • 0020646412 scopus 로고
    • Degradation of biogene oligosaccharides by β-N-acetylglucosaminidase secreted by Entamoeba histolytica
    • Werries E., Nebinger P., Franz A. Degradation of biogene oligosaccharides by β-N-acetylglucosaminidase secreted by Entamoeba histolytica. Mol Biochem Parasitol. 7:1983;127-140.
    • (1983) Mol Biochem Parasitol , vol.7 , pp. 127-140
    • Werries, E.1    Nebinger, P.2    Franz, A.3
  • 68
    • 0344247528 scopus 로고
    • Adhesion of Candida albicans to host surfaces
    • E. Timbay, H.P.R. Seeliger, & Ö. Ang. New York: Plenum Press
    • Douglas L.J. Adhesion of Candida albicans to host surfaces. Timbay E., Seeliger H.P.R., Ang Ö. Candida and Candidamycosis. 1991;43-47 Plenum Press, New York.
    • (1991) Candida and Candidamycosis , pp. 43-47
    • Douglas, L.J.1
  • 69
    • 0025411041 scopus 로고
    • Screening and cultivation conditions for microbial β-N-acetylhexosaminidase
    • Yan Z.Z., Tao Y., Cheng X.L., Sun J.W., Zhang S.Z. Screening and cultivation conditions for microbial β-N-acetylhexosaminidase. Acta Microbiol Sin. 30:1990;122-128.
    • (1990) Acta Microbiol Sin , vol.30 , pp. 122-128
    • Yan, Z.Z.1    Tao, Y.2    Cheng, X.L.3    Sun, J.W.4    Zhang, S.Z.5
  • 70
    • 0028896923 scopus 로고
    • Chitinolytic enzymes of pathogenic and ectomycorrhizal fungi
    • Hodge A., Alexander I.J., Gooday G.W. Chitinolytic enzymes of pathogenic and ectomycorrhizal fungi. Mycol Res. 99:1995;935-941.
    • (1995) Mycol Res , vol.99 , pp. 935-941
    • Hodge, A.1    Alexander, I.J.2    Gooday, G.W.3
  • 72
    • 78651135059 scopus 로고
    • Studies on glucosaminidase. 6. N-Acetyl-β-glucosaminidase and N-acetyl-β-galactosaminidase activities of a variety of enzyme preparations
    • Woolen J.W., Walker P.G., Heyworth R. Studies on glucosaminidase. 6. N-Acetyl-β-glucosaminidase and N-acetyl-β-galactosaminidase activities of a variety of enzyme preparations. J Biochem. 79:1961;294-298.
    • (1961) J Biochem , vol.79 , pp. 294-298
    • Woolen, J.W.1    Walker, P.G.2    Heyworth, R.3
  • 74
    • 33748907883 scopus 로고    scopus 로고
    • Glycosidase-catalyzed oligosaccharide synthesis of di-, tri-, and tetra-saccharides using the N-acetylhexosaminidase from Aspergillus oryzae and the β-galactosidase from Bacillus circulans
    • Singh S., Scigelova M., Vic G., Crout D.H.G. Glycosidase-catalyzed oligosaccharide synthesis of di-, tri-, and tetra-saccharides using the N-acetylhexosaminidase from Aspergillus oryzae and the β-galactosidase from Bacillus circulans. J Chem Soc Perkin Trans. 1:1996;1921-1926.
    • (1996) J Chem Soc Perkin Trans , vol.1 , pp. 1921-1926
    • Singh, S.1    Scigelova, M.2    Vic, G.3    Crout, D.H.G.4
  • 76
    • 0016839229 scopus 로고
    • The purification and properties of a β-N-acetylhexosaminidase from Trichomonas foetus
    • Edwards R.G., Thomas P., Westwood J.H. The purification and properties of a β-N-acetylhexosaminidase from Trichomonas foetus. J Biochem. 151:1975;145-148.
    • (1975) J Biochem , vol.151 , pp. 145-148
    • Edwards, R.G.1    Thomas, P.2    Westwood, J.H.3
  • 77
    • 38249041600 scopus 로고
    • β-N-acetylglucosaminidase from Phycomyces blakesleeanus
    • Cohen R.J. β-N-acetylglucosaminidase from Phycomyces blakesleeanus. Plant Sci. 43:1986;93-101.
    • (1986) Plant Sci , vol.43 , pp. 93-101
    • Cohen, R.J.1
  • 81
    • 73549090379 scopus 로고
    • Purification and characterization of chitinase and chitobiase produced by Aeromonas hydrophila subsp. anaerogenes A52
    • Yabuki M., Mizushina K., Amatatsu T., Ando A., Fujii T., Shimada M., Yamashita M. Purification and characterization of chitinase and chitobiase produced by Aeromonas hydrophila subsp. anaerogenes A52. J Gen Appl Microbiol. 32:1986;25-38.
    • (1986) J Gen Appl Microbiol , vol.32 , pp. 25-38
    • Yabuki, M.1    Mizushina, K.2    Amatatsu, T.3    Ando, A.4    Fujii, T.5    Shimada, M.6    Yamashita, M.7
  • 82
    • 0027787733 scopus 로고
    • Purification and some characterization of β-N-acetylglucosaminidase produced by Vibrio sp
    • Takahashi M., Mashiyama T., Suzuki T. Purification and some characterization of β-N-acetylglucosaminidase produced by Vibrio sp. J Ferment. Bioeng. 76:1993;356-360.
    • (1993) J Ferment. Bioeng , vol.76 , pp. 356-360
    • Takahashi, M.1    Mashiyama, T.2    Suzuki, T.3
  • 83
    • 0344678939 scopus 로고
    • Partial purification and some properties of two chitobiases from Vibrio sp
    • Ohtakara A., Totoki M., Mitsutomi M., Uchida Y. Partial purification and some properties of two chitobiases from Vibrio sp. Agric Bull Saga Uni. 48:1980;65-72.
    • (1980) Agric Bull Saga Uni , vol.48 , pp. 65-72
    • Ohtakara, A.1    Totoki, M.2    Mitsutomi, M.3    Uchida, Y.4
  • 84
    • 0027197513 scopus 로고
    • Sequence analysis of the β-N-acetylhexosaminidase gene of Vibrio vulnificus: Evidence for a common evolutionary origin of hexosaminidases
    • Somerville C.C., Colwell R.R. Sequence analysis of the β-N-acetylhexosaminidase gene of Vibrio vulnificus evidence for a common evolutionary origin of hexosaminidases . Proc Natl Acad Sci USA. 90:1993;6751-6755.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 6751-6755
    • Somerville, C.C.1    Colwell, R.R.2
  • 85
    • 0020421854 scopus 로고
    • Gratuitous induction by N-acetylmannosamine of germ-tube formation and enzymes for N-acetylglucosamine utilization in Candida albicans
    • Sullivan P.A., Shepherd M.G. Gratuitous induction by N-acetylmannosamine of germ-tube formation and enzymes for N-acetylglucosamine utilization in Candida albicans. J Bacteriol. 151:1982;1118-1122.
    • (1982) J Bacteriol , vol.151 , pp. 1118-1122
    • Sullivan, P.A.1    Shepherd, M.G.2
  • 86
    • 0024041235 scopus 로고
    • Cloning of the genes of the chitin utilization regulon of Serratia liquefaciens
    • Joshi S., Kozlowski M., Selvaraj G., Iyer V.N., Davies R.W. Cloning of the genes of the chitin utilization regulon of Serratia liquefaciens. J Bacteriol. 170:1988;2984-2988.
    • (1988) J Bacteriol , vol.170 , pp. 2984-2988
    • Joshi, S.1    Kozlowski, M.2    Selvaraj, G.3    Iyer, V.N.4    Davies, R.W.5
  • 87
    • 0030447616 scopus 로고    scopus 로고
    • The chitin catabolic cascade in the marine bacterium Vibrio furnissii. Molecular cloning, isolation, and characterization of a periplasmic β-N-acetylglucosaminidase
    • Keyhani N.O., Roseman S. The chitin catabolic cascade in the marine bacterium Vibrio furnissii. Molecular cloning, isolation, and characterization of a periplasmic β-N-acetylglucosaminidase. J Biol Chem. 271:1996;33425-33432.
    • (1996) J Biol Chem , vol.271 , pp. 33425-33432
    • Keyhani, N.O.1    Roseman, S.2
  • 88
    • 0001250943 scopus 로고
    • β-N-acetylglucosaminidase, α-N-acetylgalactosaminidase, and β-galactosidase from Clostridium perfringens
    • McGuire E.J., Chipowsky S., Roseman S. β-N-acetylglucosaminidase, α-N-acetylgalactosaminidase, and β-galactosidase from Clostridium perfringens. Methods Enzymol. 28:1972;755-763.
    • (1972) Methods Enzymol , vol.28 , pp. 755-763
    • McGuire, E.J.1    Chipowsky, S.2    Roseman, S.3
  • 89
    • 0344678938 scopus 로고
    • β-Acetylglucosaminidase in the cockroach (Periplaneta americana) and in the puffball (Lycoperdon perlatum)
    • Powning R.F., Irzykiewicz H. β-Acetylglucosaminidase in the cockroach (Periplaneta americana) and in the puffball (Lycoperdon perlatum). Comp Biochem Physiol. 12:1964;405-415.
    • (1964) Comp Biochem Physiol , vol.12 , pp. 405-415
    • Powning, R.F.1    Irzykiewicz, H.2
  • 90
    • 0025782244 scopus 로고
    • N-acetylglucosaminono-1,5-lactone oxime and the corresponding (phenylcarbamoyl)oxime. Novel and potent inhibitors of β-N-acetylglucosaminidase
    • Horsch M., Hoesch L., Vasella A., Rast D.M. N-acetylglucosaminono-1,5-lactone oxime and the corresponding (phenylcarbamoyl)oxime. Novel and potent inhibitors of β-N-acetylglucosaminidase. Eur J Biochem. 197:1991;815-818.
    • (1991) Eur J Biochem , vol.197 , pp. 815-818
    • Horsch, M.1    Hoesch, L.2    Vasella, A.3    Rast, D.M.4
  • 91
    • 0027164473 scopus 로고
    • Inhibition of β-N-acetylglucosaminidase by glycon-related analogues of the substrate
    • Horsch M., Hoesch L., Fleet G.W.J., Rast D.M. Inhibition of β-N-acetylglucosaminidase by glycon-related analogues of the substrate. J Enzyme Inhibition. 7:1993;47-55.
    • (1993) J Enzyme Inhibition , vol.7 , pp. 47-55
    • Horsch, M.1    Hoesch, L.2    Fleet, G.W.J.3    Rast, D.M.4
  • 92
    • 0015252140 scopus 로고
    • Studies on N-acetyl-β-D-glucosaminidase of Aspergillus oryzae. II. Substrate specificity of the enzyme
    • Mega T., Ikenaka T., Matsushima Y. Studies on N-acetyl-β-D-glucosaminidase of Aspergillus oryzae. II. Substrate specificity of the enzyme. J Biochem. 71:1972;107-114.
    • (1972) J Biochem , vol.71 , pp. 107-114
    • Mega, T.1    Ikenaka, T.2    Matsushima, Y.3
  • 94
    • 0019880919 scopus 로고
    • Substrate specificity of diplococcal β-N-acetylhexosaminidase, a useful enzyme for the structural studies of complex type asparagine-linked sugar chains
    • Yamashita K., Ohkura T., Yoshima H., Kobata A. Substrate specificity of diplococcal β-N-acetylhexosaminidase, a useful enzyme for the structural studies of complex type asparagine-linked sugar chains. Biochem Biophys Res Commun. 100:1981;226-232.
    • (1981) Biochem Biophys Res Commun , vol.100 , pp. 226-232
    • Yamashita, K.1    Ohkura, T.2    Yoshima, H.3    Kobata, A.4
  • 95
    • 0028262949 scopus 로고
    • Glycosidases in structural analysis
    • Jacob G.S., Scudder P. Glycosidases in structural analysis. Methods Enzymol. 230:1994;280-299.
    • (1994) Methods Enzymol , vol.230 , pp. 280-299
    • Jacob, G.S.1    Scudder, P.2
  • 97
    • 0029560623 scopus 로고
    • Glycosidase-catalyzed oligosaccharide synthesis: Preparation of N-acetylchitooligosaccharides using the β-N-acetylhexosaminidase of Aspergillus oryzae
    • Singh S., Packwood J., Samuel C.J., Critchley P., Crout D.H.G. Glycosidase-catalyzed oligosaccharide synthesis Preparation of N-acetylchitooligosaccharides using the β-N-acetylhexosaminidase of Aspergillus oryzae . Carbohydr Res. 279:1995;293-305.
    • (1995) Carbohydr Res , vol.279 , pp. 293-305
    • Singh, S.1    Packwood, J.2    Samuel, C.J.3    Critchley, P.4    Crout, D.H.G.5
  • 98
    • 0028853934 scopus 로고
    • Glycosidase-catalyzed oligosaccharide synthesis: Preparation of N-acetylchitooligosaccharides penta-N-acetylchitopentaose and hexa-N-acetylchitohexaose using the β-N-acetylhexosaminidase of Aspergillus oryzae
    • Singh S., Gallagher R., Derrick P.J., Crout D.H.G. Glycosidase-catalyzed oligosaccharide synthesis Preparation of N-acetylchitooligosaccharides penta-N-acetylchitopentaose and hexa-N-acetylchitohexaose using the β-N-acetylhexosaminidase of Aspergillus oryzae . Tetrahedron Assymetry. 6:1995;2803-2810.
    • (1995) Tetrahedron Assymetry , vol.6 , pp. 2803-2810
    • Singh, S.1    Gallagher, R.2    Derrick, P.J.3    Crout, D.H.G.4
  • 99
    • 0025941648 scopus 로고
    • Biotransformation in carbohydrate synthesis. N-acetylgalactosaminyl and N-acetylglucosaminyl transfer onto methyl α- And β-glucosides catalyzed by the β-N-acetylhexosaminidase from Aspergillus oryzae
    • Crout D.H.G., Howarth O.W., Singh S., Swoboda B.E.P., Critchley P., Gibson W.T. Biotransformation in carbohydrate synthesis. N-acetylgalactosaminyl and N-acetylglucosaminyl transfer onto methyl α- and β-glucosides catalyzed by the β-N-acetylhexosaminidase from Aspergillus oryzae. J Chem Soc Chem Commun. 1991;1550-1551.
    • (1991) J Chem Soc Chem Commun , pp. 1550-1551
    • Crout, D.H.G.1    Howarth, O.W.2    Singh, S.3    Swoboda, B.E.P.4    Critchley, P.5    Gibson, W.T.6
  • 100
    • 37049070324 scopus 로고
    • Kinetic control of regioselectivity in glycosidase-catalyzed disaccharide synthesis: Preparation of 2-acetamido-4-O-(2-acetamido-2-deoxy-β-D-glucopyranosyl)-2-deoxy-D- glucopyranose (N,N′-diacetylchitobiose) and 2-acetamido-6-O-(2-acetamido-2-deoxy-β-D-glucopyranosyl)-2-deoxy-D- glucopyranose
    • Singh S., Packwood J., Crout D.H.G. Kinetic control of regioselectivity in glycosidase-catalyzed disaccharide synthesis Preparation of 2-acetamido-4-O-(2-acetamido-2-deoxy-β-D-glucopyranosyl)-2-deoxy-D- glucopyranose (N,N′-diacetylchitobiose) and 2-acetamido-6-O-(2-acetamido-2-deoxy-β-D-glucopyranosyl)-2-deoxy-D- glucopyranose . J Chem Soc Chem Commun. 1994;2227-2228.
    • (1994) J Chem Soc Chem Commun , pp. 2227-2228
    • Singh, S.1    Packwood, J.2    Crout, D.H.G.3
  • 101
    • 0029561116 scopus 로고
    • Enzymatic synthesis of 2-acetamido-4-O-(2-acetamido- 2-deoxy-β-D-galactopyranosyl)-2-deoxy-D-glucopyranose and 2-acetamido-6-O-(2-acetamido-2-deoxy-β-D-galactopyranosyl)-2-deoxy-D- glucopyranose catalysed by the β-N-acetylhexosaminidase from Aspergillus oryzae
    • Singh S., Crout D.H.G., Packwood J. Enzymatic synthesis of 2-acetamido-4-O-(2-acetamido- 2-deoxy-β-D-galactopyranosyl)-2-deoxy-D-glucopyranose and 2-acetamido-6-O-(2-acetamido-2-deoxy-β-D-galactopyranosyl)-2-deoxy-D- glucopyranose catalysed by the β-N-acetylhexosaminidase from Aspergillus oryzae. Carbohydr Res. 279:1995;321-325.
    • (1995) Carbohydr Res , vol.279 , pp. 321-325
    • Singh, S.1    Crout, D.H.G.2    Packwood, J.3
  • 102
    • 0031395398 scopus 로고    scopus 로고
    • Trisaccharide synthesis by glycosyl transfer from p-nitrophenyl β-D-N-acetylgalactosaminide on to disaccharide acceptors catalysed by the β-N-acetylhexosaminidase from Aspergillus oryzae
    • Singh S., Scigelova M., Critchley P., Crout D.H.G. Trisaccharide synthesis by glycosyl transfer from p-nitrophenyl β-D-N-acetylgalactosaminide on to disaccharide acceptors catalysed by the β-N-acetylhexosaminidase from Aspergillus oryzae. Carbohydr Res. 305:1997;363-370.
    • (1997) Carbohydr Res , vol.305 , pp. 363-370
    • Singh, S.1    Scigelova, M.2    Critchley, P.3    Crout, D.H.G.4
  • 103
    • 0015454812 scopus 로고
    • Studies on N-acetyl-β-D-glucosaminidase of Aspergillus oryzae. IV. Acceptor specificity and quantitative representation of the transglycosylation reaction
    • Mega T., Ikenaka T., Matsushima Y. Studies on N-acetyl-β-D-glucosaminidase of Aspergillus oryzae. IV. Acceptor specificity and quantitative representation of the transglycosylation reaction. J Biochem. 72:1972;1391-1396.
    • (1972) J Biochem , vol.72 , pp. 1391-1396
    • Mega, T.1    Ikenaka, T.2    Matsushima, Y.3
  • 105
    • 0028055658 scopus 로고
    • Purification, characterization, and synergistic activity of a glucan 1,3-β-glucosidase and an N-acetyl-β-glucosaminidase from Trichoderma harzianum
    • Lorito M., Hayes C.K., Di Pietro A., Woo S.L., Harman G.E. Purification, characterization, and synergistic activity of a glucan 1,3-β-glucosidase and an N-acetyl-β-glucosaminidase from Trichoderma harzianum. Phytopathology. 84:1994;398-405.
    • (1994) Phytopathology , vol.84 , pp. 398-405
    • Lorito, M.1    Hayes, C.K.2    Di Pietro, A.3    Woo, S.L.4    Harman, G.E.5
  • 106
    • 0026271126 scopus 로고
    • Seed treatments for biological control of plant disease
    • Harman G.E. Seed treatments for biological control of plant disease. Crop Prot. 10:1991;166-171.
    • (1991) Crop Prot , vol.10 , pp. 166-171
    • Harman, G.E.1
  • 107
    • 0002096967 scopus 로고
    • Trichoderma and Gliocladium: Biology, ecology, and potential for biocontrol
    • Papavizas G.C. Trichoderma and Gliocladium Biology, ecology, and potential for biocontrol . Ann Rev Phytopathol. 23:1985;23-54.
    • (1985) Ann Rev Phytopathol , vol.23 , pp. 23-54
    • Papavizas, G.C.1
  • 108
    • 0001820032 scopus 로고
    • Trichoderma - Application, mode of action, and potential as a biocontrol agent of soilborn plant pathogenic fungi
    • I. Chet. New York: John Wiley
    • Chet I. Trichoderma - Application, mode of action, and potential as a biocontrol agent of soilborn plant pathogenic fungi. Chet I. Innovative Approaches to Plant Disease Control. 1987;137-160 John Wiley, New York.
    • (1987) Innovative Approaches to Plant Disease Control , pp. 137-160
    • Chet, I.1
  • 109
    • 0001428140 scopus 로고
    • Rhizosphere competence of Trichoderma harzianum
    • Ahmad J.S., Baker R. Rhizosphere competence of Trichoderma harzianum. Phytopathology. 77:1987;182-189.
    • (1987) Phytopathology , vol.77 , pp. 182-189
    • Ahmad, J.S.1    Baker, R.2
  • 110
    • 0026097376 scopus 로고
    • Improved rhizosphere competence in a protoplast fusion progeny of Trichoderma harzianum
    • Sivan A., Harman G.E. Improved rhizosphere competence in a protoplast fusion progeny of Trichoderma harzianum. J Gen Microbiol. 137:1991;23-29.
    • (1991) J Gen Microbiol , vol.137 , pp. 23-29
    • Sivan, A.1    Harman, G.E.2
  • 111
    • 0011931442 scopus 로고
    • Production and use of biological pest control agents
    • Khachatourians G.G. Production and use of biological pest control agents. Trends Biotechnol. 4:1986;120-124.
    • (1986) Trends Biotechnol , vol.4 , pp. 120-124
    • Khachatourians, G.G.1
  • 112
    • 0001338550 scopus 로고
    • Fungi as microbial insecticides against pests
    • D.K. Arora, K.G. Mukerji, & E. Drouhet. New York: Marcel Dekker
    • Ferron J.P., Pargues J., Riba G. Fungi as microbial insecticides against pests. Arora D.K., Mukerji K.G., Drouhet E. Handbook of applied mycobiology, Vol. 2. 1991;665-706 Marcel Dekker, New York.
    • (1991) Handbook of Applied Mycobiology, Vol. 2 , pp. 665-706
    • Ferron, J.P.1    Pargues, J.2    Riba, G.3
  • 113
    • 0025321708 scopus 로고
    • Enzymatic activity profiling as a potential biotyping method for Ajellomyces dermatitidis
    • Summerbell R.C., Kane J., Pincus D.H. Enzymatic activity profiling as a potential biotyping method for Ajellomyces dermatitidis. J Clinical Microbiol. 28:1990;1054-1056.
    • (1990) J Clinical Microbiol , vol.28 , pp. 1054-1056
    • Summerbell, R.C.1    Kane, J.2    Pincus, D.H.3
  • 114
    • 0027199789 scopus 로고
    • 4-Methylumbelliferyl-β-N-acetylglucosaminide hydrolysis by a high-affinity enzyme, a putative marker of protozoan herbivory
    • Vrba J., Simek K., Nedoma J., Hartman P. 4-Methylumbelliferyl-β-N-acetylglucosaminide hydrolysis by a high-affinity enzyme, a putative marker of protozoan herbivory. Appl Environ Microbiol. 59:1993;3091-3101.
    • (1993) Appl Environ Microbiol , vol.59 , pp. 3091-3101
    • Vrba, J.1    Simek, K.2    Nedoma, J.3    Hartman, P.4
  • 115
    • 84986468418 scopus 로고
    • Bioconversion of shellfish chitin waste: Waste treatment, enzyme production, process design, and economic analysis
    • Cosio I.G., Fisher R.A., Carroad P.A. Bioconversion of shellfish chitin waste Waste treatment, enzyme production, process design, and economic analysis . J Food Sci. 47:1982;901-905.
    • (1982) J Food Sci , vol.47 , pp. 901-905
    • Cosio, I.G.1    Fisher, R.A.2    Carroad, P.A.3
  • 116
    • 0345541249 scopus 로고
    • Studies on the chitinolytic enzymes of black-koji mold. Part V. Participation of two different enzymes in the decomposition of glycol chitin to constituent aminosugars
    • Ohtakara A. Studies on the chitinolytic enzymes of black-koji mold. Part V. Participation of two different enzymes in the decomposition of glycol chitin to constituent aminosugars. Agric Biol Chem. 27:1963;454-460.
    • (1963) Agric Biol Chem , vol.27 , pp. 454-460
    • Ohtakara, A.1
  • 117
    • 0344247522 scopus 로고
    • Studies on the chitinolytic enzymes of black-koji mould. Part VI. Isolation and some properties of N-acetyl-β-glucosaminidase
    • Ohtakara A. Studies on the chitinolytic enzymes of black-koji mould. Part VI. Isolation and some properties of N-acetyl-β-glucosaminidase. Agr Biol Chem. 28:1964;741-745.
    • (1964) Agr Biol Chem , vol.28 , pp. 741-745
    • Ohtakara, A.1
  • 118
    • 0018433371 scopus 로고
    • Comparative studies of three exo-β-glycosidases of Aspergillus oryzae
    • Mega T., Matsushima Y. Comparative studies of three exo-β-glycosidases of Aspergillus oryzae. J Biochem. 85:1979;335-341.
    • (1979) J Biochem , vol.85 , pp. 335-341
    • Mega, T.1    Matsushima, Y.2
  • 119
    • 0029555549 scopus 로고
    • Molecular cloning and expression in S. cerevisiae of two exochitinases from Trichoderma harzianum
    • Draborg H., Kauppingen S., Dalbøge H., Christgau S. Molecular cloning and expression in S. cerevisiae of two exochitinases from Trichoderma harzianum. Biochem Mol Biol Int. 36:1995;781-791.
    • (1995) Biochem Mol Biol Int , vol.36 , pp. 781-791
    • Draborg, H.1    Kauppingen, S.2    Dalbøge, H.3    Christgau, S.4
  • 120
    • 0029799714 scopus 로고    scopus 로고
    • Molecular cloning and expression of the nag1 gene (N-acetyl-β-D-glucosaminidase-encoding gene) from Trichoderma harzianum P1
    • Peterbauer C.K., Lorito M., Hayes C.K., Harman G.E., Kubicek C.P. Molecular cloning and expression of the nag1 gene (N-acetyl-β-D-glucosaminidase-encoding gene) from Trichoderma harzianum P1. Curr Genet. 30:1996;325-331.
    • (1996) Curr Genet , vol.30 , pp. 325-331
    • Peterbauer, C.K.1    Lorito, M.2    Hayes, C.K.3    Harman, G.E.4    Kubicek, C.P.5
  • 122
    • 0015502004 scopus 로고
    • An exo-β-N-acetylglucosaminidase from Bacillus subtilis B: Extraction and purification
    • Ortiz J.M., Gillespie J., Berkeley R.C.W. An exo-β-N-acetylglucosaminidase from Bacillus subtilis B extraction and purification . Biochim Biophys Acta. 289:1974;174-180.
    • (1974) Biochim Biophys Acta , vol.289 , pp. 174-180
    • Ortiz, J.M.1    Gillespie, J.2    Berkeley, R.C.W.3
  • 124
    • 0029372446 scopus 로고
    • The primary structure of an Entamoeba histolytica β-hexosaminidase A subunit
    • Beanan M.J., Bailey G.B. The primary structure of an Entamoeba histolytica β-hexosaminidase A subunit. J Euk Microbiol. 42:1995;632-636.
    • (1995) J Euk Microbiol , vol.42 , pp. 632-636
    • Beanan, M.J.1    Bailey, G.B.2
  • 125
    • 0024662890 scopus 로고
    • Chitinase and chitobiase production during fermentation of genetically improved Serratia liquefaciens
    • Joshi S., Kozlowski M., Richens S., Comberbach D.M. Chitinase and chitobiase production during fermentation of genetically improved Serratia liquefaciens. Enzyme Microb Technol. 11:1989;289-296.
    • (1989) Enzyme Microb Technol , vol.11 , pp. 289-296
    • Joshi, S.1    Kozlowski, M.2    Richens, S.3    Comberbach, D.M.4
  • 126
    • 51249172482 scopus 로고
    • Cloning of the gene coding for chitobiase of Serratia marcescens
    • Kless H., Sitrit Y., Chet I., Oppenheim A.B. Cloning of the gene coding for chitobiase of Serratia marcescens. Mol Gen Genet. 217:1989;471-473.
    • (1989) Mol Gen Genet , vol.217 , pp. 471-473
    • Kless, H.1    Sitrit, Y.2    Chet, I.3    Oppenheim, A.B.4
  • 127
    • 0017153218 scopus 로고
    • Purification and characterization of β-N-acetylhexosaminidase and β-galactosidase from Streptococcus 6646 K
    • Kiyohara T., Terao T., Shioiri-Nakano K., Osawa T. Purification and characterization of β-N-acetylhexosaminidase and β-galactosidase from Streptococcus 6646 K. J Biochem. 80:1976;9-17.
    • (1976) J Biochem , vol.80 , pp. 9-17
    • Kiyohara, T.1    Terao, T.2    Shioiri-Nakano, K.3    Osawa, T.4
  • 128
    • 0023387947 scopus 로고
    • Translocation of Vibrio harveyi N,N′-diacetylchitobiase to the outer membrane of Escherichia coli
    • Jannatipour M., Soto-Gill R.W., Childers L.C., Zyskind J.W. Translocation of Vibrio harveyi N,N′-diacetylchitobiase to the outer membrane of Escherichia coli. J Bacteriol. 169:1987;3785-3791.
    • (1987) J Bacteriol , vol.169 , pp. 3785-3791
    • Jannatipour, M.1    Soto-Gill, R.W.2    Childers, L.C.3    Zyskind, J.W.4
  • 129
    • 0022516180 scopus 로고
    • Chitinase determinants of Vibrio vulnificus: Gene cloning and applications of a chitinase probe
    • Wortman A.T., Somerville C.C., Colwell R.R. Chitinase determinants of Vibrio vulnificus gene cloning and applications of a chitinase probe . Appl Environ Microbiol. 52:1986;142-145.
    • (1986) Appl Environ Microbiol , vol.52 , pp. 142-145
    • Wortman, A.T.1    Somerville, C.C.2    Colwell, R.R.3


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