Microbial dextran-hydrolyzing enzymes: Fundamentals and applications

Microbiology and Molecular Biology Reviews

Volumn 69, Issue 2, 2005, Pages 306-325

  Khalikova, Elvira ^a,b   Susi, Petri ^a,c   Korpela, Timo ^a,c  

^a UNIVERSITY OF TURKU   (Finland)

^b INSTITUTE OF BIOLOGY   (Russian Federation)

^c Department of Virology ^*  (Finland)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; COSMETIC; CRYOPROTECTIVE AGENT; DEXTRAN; DEXTRANASE; DEXTRANSUCRASE; FUNGAL ENZYME; HYDROLASE; ISOENZYME; ISOMALTOSE; ISOMALTOTRIOSE; STABILIZING AGENT; TRANSFERASE; TRIOSE; UNCLASSIFIED DRUG;

BACTERIUM; DRUG STRUCTURE; FOOD INDUSTRY; FUNGUS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; LEUCONOSTOC MESENTEROIDES; MOULD; NEPHELOMETRY; NONHUMAN; PENICILLIUM; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; REVIEW; SOLID PHASE SYNTHESIS; STRUCTURE ACTIVITY RELATION; SUGAR INDUSTRY; TOOTH PLAQUE;

BACTERIA; BACTEROIDES; DEXTRANASE; DEXTRANS; FUNGI; GLUCOSIDASES; GLYCOSIDE HYDROLASES; INDUSTRIAL MICROBIOLOGY; MODELS, MOLECULAR; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 20544444776     PISSN: 10922172     EISSN: None     Source Type: Journal    
DOI: 10.1128/MMBR.69.2.306-325.2005     Document Type: Review

References (233)

1. Abbott, D., and H. Weigel. 1966. Studies on dextran and dextranases. Part VII. Structures from an α-1→4-branched dextran. J. Chem. Soc. C:821-827.
2. Abbott, D., E. J. Bourne, and H. Weigel. 1966. Studies on dextran and dextranases. Part VIII. Size and distribution of branches in some dextrans. J. Chem. Soc. C:827-831.
3. Abdel-Naby, M. A., S. Ismail, A. M. Abdel-Fattah, and A. F. Abdel-Fattah. 1999. Preparation and some properties of immobilized Penicillium funiculosum. Process Biochem. 34:391-398.
4. Ajdic, D., W. M. McShan, R. E. McLaughlin, G. Savic, J. Chang, M. B. Carson, C. Primeaux, R. Tian, S. Kenton, J. Honggui, S. Lin, Y. Qian, S. Li, H. Zhu, F. Najar, H. Lai, J. White, B. A. Roe, and J. J. Ferretti. 2002. Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen. Proc. Natl. Acad. Sci. USA 99:14434-14439.
5. Aoki, H., and Y. Sakano. 1997. A classification of dextran-hydrolyzing enzymes based on amino-acid-sequence similarities. Biochem. J. 323:859-861.
6. Arnold, W. N., T. B. P. Nguyen, and L. C. Mann. 1998. Purification and characterization of a dextranase from Sporothrix schenckii. Arch. Microbiol. 170:91-98.
7. Bailey, R. W., and R. T. J. Clarke. 1959. A bacterial dextranase. Biochem. J. 72:49-54.
8. Bailey, R. W., D. H. Hutson, and H. Weigel. 1961. The action of a Lactobacillus bifidus dextranase on a branched dextran. Biochem. J. 80:514-519.
9. Barret, J. F., and R. Curtiss III. 1986. Renaturation of dextranase activity from culture supernatant fluids of Streptococcus sobrinus after sodium dodecylsulfate polyacrylamide gel electrophoresis. Anal. Biochem. 158:365-370.
10. Barret, J. F., T. A. Barret, and R. Curtiss. 1987. Purification and partial characterization of the multicomponent dextranase complex of Streptococcus sobrinus and cloning of the dextranase gene. Infect. Immun. 55:792-802.
11. Beighton, D., and H. Hayday. 1984. The establishment of the bacterium Strepotcoccus mutans in dental plaque and the induction of caries in macaque monkeys (Macaca fascicularis) fed a diet containing cooked wheat flour. Arch. Oral Biol. 29:269-372.
12. Beldarrain, A.,' N. Acosta, L. Betancourt, J. Gonzales, and T. Pens. 2003. Enzymic, spectroscopic and calorimetric studies of a recombinant dextranase expressed in Pichia pastoris. Biotechnol. Appl. Biochem. 38:211-221.
13. Birkhed, D., K.-G. Rosell, and K.Granath. 1979. Structure of extracellular water-soluble polysaccharides synthesized from sucrose by oral strains of Streptococcus mutans, Streptococcus salivarius, Streptococcus sanguis and Actinomyces viscosus. Arch. Oral Biol. 24:53-61.
14. Bourne, E. J., R. L. Sidebotham, and H. Weigel. 1972. Studies on dextrans and dextranases. Part X. Types and percentages of secondary linkages in the dextrans elaborated by Leuconostoc mesenteroides NRRL B-1299. Carbohydr. Res. 22:13-22.
15. Bourne, E. J., R. L. Sidebotham, and H. Weigel. 1974. Studies on dextrans and dextranases. Part XI. The structure of a dextran elaborated by Leuconostoc mesenteroides NRRL B-1299. Carbohydr. Res. 34:279-288.
16. Bourne, Y., and B. Henrissat. 2001. Glycoside hydrolases and glycosyltransferases: families and functional modules. Curr. Opin. Struct. Biol. 11:593-600.
17. Bruyn, J. M. 2000. Processing of frost damaged beets at CSM and the use of dextranase. Zuckerindustrie 125:898-902.
18. Brown, C. F., and P. A. Inkerman. 1992. Specific method for quantitative measurement of the total dextran content of raw sugar. J. Agric. Food Chem. 40:227-233.
19. Bucke, C., M. Adlard, V. Singleton, and J. Horn. 2001. Assay method. U.S. patent application 20030100041.
20. Chaiet, L., A. J. Kempf, R. Harman, E. Kaczka, R. Weston, K. Nollstadt, and F. J. Wolf. 1970. Isolation of a pure dextranase from Penicillium funiculosum. Appl. Microbiol. 20:421-426.
21. Charles, A. F., and L. N. Farrell. 1957. Preparation and use of enzymatic material from Penicillium lilacinum to yield clinical dextran. Can. J. Microbiol. 3:239-247.
22. Chavan, S. M., S. D. Borawake, and G. D. Patil. 2001. Enzymatic hydrolysis of starch and dextran during sugar manufacturing process: warana experience. Sugar Ind. Abstr. 63:848.
23. Cheetham, N. W. H., M. E. Slodki, and G. J. Walker. 1991. Structure of linear, low molecular weight dextran synthesized by a D-glycosyltransferase (GTF-S3) of Streptococcus sobrinus. Carbohydr. Polymers 16:341-353.
24. Colby, S. M., G. C. Whiting, L. Tao, and R. R. B. Russell. 1995. Insertional inactivation of the Streptococcus mutans dexA (dextranase) gene results in altered adherence and dextran catabolism. Microbiology 141:2929-2936.
25. Colby, S. M., and R. R. B. Russell. 1997. Sugar metabolism by mutans streptococci. J. Appl. Microbiol. Symp. Suppl. 83:80-88.
26. Costa, T., L. C. Bier, and F. Gaida. 1974. Dextran hydrolysis by a Fusobacterium strain isolated from human dental plaque. Arch. Oral Biol. 19: 341-342.
27. Cote, G. L., and J. F. Robyt. 1983. The formation of α-(1, 3) branch linkages by an exocellular glucansucrase from Leuconostoc mesenteroides NRRL B-742. Carbohydr. Res. 119:141-156.
28. Cote, G. L., J. A. Ahlgren, and M. R. Smith. 1999. Some structural features of an insoluble α-D-glucan from a mutant strain of Leuconostoc mesenteroides NRRL B-1355. J. Ind. Microbiol. Biotechnol. 23:656-660.
29. Covacevich, M. T., and G. N. Richards. 1978. Purification of intracellular dextranases and D-glucosidases from Pseudomonas UQM 733. Carbohydr. Res. 64:169-180.
30. Covacevich, M. T., and G. N. Richards. 1979. Modes of action of intracellular dextranase and three oligoglucanases from Pseudomonas UQM 733. Carbohydr. Res. 70:283-293.
31. Crepon, B., J. Jozefonvicz, V. Chytry, B. Rihova, and J. Kopecek. 1991. Enzymatic degradation and immunogenic properties of derived dextrans. Biomaterials 12:550-554.
32. Cuddihy, J. A., J. S. Rauh, F. Mendez, and C. Bernhard. 1999. Dextranase in sugar production: factory experience. http://www.midlandresearchlabsinc .com/dodib/dexexper.pdf.
33. Dali, L., M. Keilhofner, B. Herndon, W. Barnes, and J. Lane. 1990. Clindamycin effect on glycocalyx production in experimental viridans streptococcal endocarditis. J. Infect. Dis. 161:1221-1224.
34. Danilova, T. I., V. I. Maksimov, A. I. Chukhrova, and G. A. Molodova. 1983. The carbohydrate component of Penicillium funiculosum dextranase. Prikl. Biokhim. Mikrobiol. 19:104-110. (In Russian.)
35. Das, D. K., and S. K. Dutta. 1996. Purification, biochemical characterisation and mode of action of an extracellular endodextranase from the culture filtrate of Penicillium lilacinum. Int. J. Biochem. Cell. Biol. 28:107-113.
36. Day, D. F., and D. Kim. 1993. A process for the production of dextran polymers of controlled molecular size and molecular size distributions-mixed culture fermentation of Leuconostoc mesenteroides and mutant microorganism producing dextranase in presence of sucrose. U.S. patent 5,229,277.
37. Demchuk, E., M. Vihinen, R. Wade, and T. Korpela. 1993. Modeling three-dimensional structure and electrostatics of alkali-stable cyclomaltodextrin glucanotransferase. p. 10. In W. J. J. van den Tweel, A. Harder, and R. M. Buitelaar (ed.), Stability and stabilization of enzymes. Elsevier Science Publishers B.V., Amsterdam, The Netherlands.
38. Dois, M., M. Remaud-Simeon, and P. F. Monsan. 1997. Dextransucrase production by Leuconostoc mesenteroides NRRL B-1299. Comparison with L. mesenteroides NRRL B-512F. Enzyme Microb. Technol. 20:523-530.
39. Dowzer, C. E. A., and J. M. Kelly. 1991. Analysis of the CreA gene from Aspergillus nidulans: a gene involved in carbon catabolite repression. Mol. Cell. Biol. 11:5701-5709.
40. Dragan-Bularda, M., and S. Kiss. 1972. Dextranase activity in soil. Soil Biol. Biochem. 4:413-416.
41. Ebusi, S., A. Misaki, K. Kato, and S. Kotani. 1974. The structure of water-insoluble glucans of cariogenic Streptococcus mutans, formed in the absence and presence of dextranase. Carbohydr. Res. 38:374-381.
42. Edman, P., and I. Sjöholm. 1982. Treatment of artificially induced storage disease with lysosomotropic microparticles. Life Sci. 30:327-330.
43. Eifuku, H., A. Yoshimitsu-Narita, S. Sato, T. Yakushiji, and M. Inoue. 1989. Production and partial characterization of the extracellular polysaccharides from oral Streptococcus salivarius. Carbohydr. Res. 194:247-260.
44. Ellis, D. W., and C. H. Miller. 1977. Extracellular dextran hydrolase from Streptococcus mutons strain 6715. J. Dent. Res. 56:57-69.
45. Enzyme Nomenclature Committee of the International Union of Biochemistry and Molecular Biology. 1992. Enzyme nomenclature 1992: recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology on the Nomenclature and Classification of Enzymes. Prepared for NC-IUBMB by Edwin C. Webb. Academic Press, San Diego, Calif.
46. Felgenhauer, B., and K. Trautner. 1982. A comparative study of extracellular glucanhydrolase and glucosyltransferase enzyme activities of five different serotypes of oral Streptococcus mutants. Arch. Oral Biol. 27:455-461.
47. Fukimoto, J., H. Tsuji, and D. I. Tsuru. 1971. Penicillium luteum dextranase: its production and some enzymatic properties. J. Biochem. 69:1113-1121.
48. Garcia, B., E. Margolles, H. Roca, D. Mateu, M. Raices, M. E. Gonzales, L. Herrera, and J. Delgado. 1996. Cloning and sequencing of a dextranase-encoding cDNA from Penicillium minioluteiim. FEMS Microbiol. Lett. 143: 175-183.
49. Garcia, B., and E. Rodriguez. 2000. Carbon source regulation of a dextranase gene from the filamentous fungus Penicillium minioluteum. Curr. Genet. 37:396-402.
50. Garcia, B., A. Castellanos, J. Menendez, and T. Pons. 2001. Molecular cloning of an α-glucosidase-like gene from Penicillium minioluteum and structure prediction of its gene product. Biochem. Biophys. Res. Commun. 281:151-158.
51. Gianfreda, L., E. Tosti, and V. Scardi. 1979. A comparison of α- and β-glucanase activities in fourteen species of marine molluscs. Biochem. Syst. Ecol. 7:57-59.
52. Gibbons, R. J., and J. Houte. 1975. Bacterial adherence in oral microbial ecology. Annu. Rev. Microbiol. 29:19-44.
53. Goldstein-Litschitz, B., and S. Bauer. 1976. Comparison of dextranases for their possible use in eliminating dental plaque. J. Dent. Res. 55:886-892.
54. Guggenheim, B. 1970. Enzymatic hydrolysis and structure of water-insoluble glucan produced by glucosyltransferases from a strain of Streptococcus mutons. Helv. Odont. Acta 14:89-108.
55. Hamada, S., and H. D. Slade. 1980. Biology, immunology, and cariogenicity of Streptococcus mutans. Microbiol. Rev. 44:331-384.
56. Hamada, S., M. Torii, S. Kotani, and Y. Tsuchitani. 1981. Adherence of Streptococcus sanguis clinical isolates to smooth surfaces and interaction of isolates with Streptococcus mutans glycosyltransferase. Infect. Immun. 32: 364-372.
57. Hansen, H. J. 1998. Method for antibody targeting of therapeutic agents. U.S. patent 5,851,527.
58. Hare, M. D., S. Svensson, and G. J. Walker. 1978. Characterization of the extracellular, water-insoluble α-D-glucans of oral streptococci by methylation analysis and by enzymic synthesis and degradation. Carbohydr. Res. 66:245-264.
59. Hattori, A., and K. Ishibashi. 1981. Screening of dextranase producing microorganisms. Agric. Biol. Chem. 45:2347-2349.
60. Hattori, A., K. Ishibashi, and S. Minato. 1981. The purification and characterisation of the dextranase of Chaetomium gracile. Agric. Biol. Chem. 45: 2409-2416.
61. Henrissat, B. 1991. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280:309-316.
62. Henrissat, B., and A. Bairoch. 1993. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 293:781-788.
63. Henrissat, B., and A. Bairoch. 1996. Updating the sequence-based classification of glycosyl hydrolases. Biochem. J. 316:695-696.
64. Henrissat, B., and G. J. Davies. 2000. Glycoside hydrolases and glycosyl-transferases. Families, modules, and implications for genomics. Plant Physiol. 124:1515-1519.
65. Heyn, A. N. J. 1970. Dextranase activity and auxin-induced cell elongation in coleoptiles of Avena. Biochem. Biophys. Res. Commun. 38:831-837.
66. Heyn, A. N. J. 1981. Molecular basis of auxin-regulated extension growth and role of dextranase. Proc. Natl. Acad. Sci. USA 78:6608-6612.
67. Hiraoka, N., J. Fukimoto, and D. Tsuru. 1972. Purification and some enzymatic properties of Aspergillus cameus dextranase. J. Biochem. 71:57-64.
68. Hiraoka, N., H. Tsuji, J. Fukimoto, T. Yamamoto, and D. Tsuru. 1973. Studies on mould dextranases. Some physicochemical properties and substrate specificity of dextranases obtained from Aspergillus cameus and Penicillium luteum. Int. J. Peptide Protein Res. 5:161-169.
69. Hoster, F., R. Daniel, and G. Gottschalk. 2001. Isolation of a new Thermoanaerobacterium thermosaccharolyticum strain (FH1) producing a termostable dextranase. J. Gen. Appl. Microbiol. 47:187-192.
70. Huang, J. S., and J. Tang. 1976. Sensitive assay for cellulase and dextranase. Anal. Biochem. 73:369-377.
71. Hultin, E., and L. Nordström. 1949. Investigation on dextranase I. On the occurrence and the assay of dextranase. Acta Chem. Scand. 3:1405-1417.
72. Hutson, D. H., and H. Weigel. 1963. Studies on dextrans and dextranases. Mechanism of the actions of intra- and extracellular mould dextranases. Biochem J. 88:588-591.
73. Igarashi, T., and A. Yamamoto. 1988. Purification and characterization dextranase of Bacteroides oralis Ig 4a. Showa Shigakkai Zasshi. 8:405-412.
74. Igarashi, T., A. Yamamoto, and N. Goto. 1995. Characterization of the dextranase gene (dex) of Streptococcus mutans and its recombinant product in an Escherichia coli host. Microbiol. Immunol. 39:387-391.
75. Igarashi, T., A. Yamamoto, and N. Goto. 1995. Sequence analysis of the Streptococcus mutans Ingbritt dexA gene encoding extracellular dextranase. Microbiol. Immunol. 39:853-860.
76. Igarashi, T., A. Yamamoto, and N. Goto. 1998. Detection of dextranase-producing gram-negative oral bacteria. Oral Microbiol. Immunol. 13:382-386.
77. Igarashi, T., A. Yamamoto, and N. Goto. 2001. Nudeotide sequence and molecular characterization of a dextranase gene from Streptococcus downei. Microbiol. Immunol. 45:341-348.
78. Igarashi, T., H. Morisaki, A. Yamamoto, and N. Goto. 2002. An essential amino acid residue for catalytic activity of the dextranase of Streptococcus mutans. Oral Microbiol. Immunol. 17:193-196.
79. Igarashi, T., H. Morisaki, and N. Goto. 2004. Molecular characterisation of dextranase from Streptococcus rattus. Microbiol. Immunol. 48:155-162.
80. Ingelman, B. 1948. Enzymatic breakdown of dextran. Acta Chem. Scan. 2: 803-812.
81. Inkerman, P. A., and L. Riddell. 1977. Dextranase III. Refinements to the enzyme process for the treatment of deteriorated cane. Proc. Oueensl. Soc. Sugar Cane Technol. 44:215-233.
82. Iwai, A., H. Ito, T. Mizuno, H. Mori, H. Matsui, M. Honma, G. Okada, and S. Chiba. 1994. Molecular cloning and expression of an isomalto-dextranase gene from Arthrobacter globiformis T6. J. Bacteriol. 176:7730-7734.
83. Janson, J.-C., and J. Porath. 1966. A bacterial dextranase. Methods Enzymol. 8:615-621.
84. Jeanes, A., W. C. Haynes, C. A. Wilham, J. C. Rankin, E. H. Melvin, M. J. Austin, J. E. Cluskey, B. E. Fisher, H. M. Tsuchiya, and C. E. Rist. 1954. Characterization and classification of dextrans from 96 strains of bacteria. J. Am. Chem. Soc. 76:5041-5052.
85. Jensen, B., and J. Olsen. 1996. Extracellular a-glucosidase with dextranhydrolysing activity from the thermophilic fungus, Thermomyces lanuginosus. Curr. Microbiol. 33:152-155.
86. Kaster, A. G., and L. R. Brown. 1983. Extracellular dextranase activity produced by human oral strains of genus Bifidobacterium. Infect. Immun. 42:716-720.
87. Kawamoto, H., T. Oguma, H. Sekine, and M. Kobayashi. 2001. Immobilization of cycloisomaltooligosaccharide glucanotransferase for the production of cydoisomaltooligosaccharides from dextran. Enzyme Microb. Technol. 28:515-521.
88. Khalikova, E. F., and N. G. Usanov. 2002. An insoluble colored substrate for dextranase assay. Appl. Biochem. Microbiol. 38:89-93.
89. Khalikova, E., P. Susi, N. Usanov, and T. Korpela. 2003. Purification and properties of extracellular dextranase from a Bacillus sp. J. Chromatogr. B 796:315-326.
90. Kim, D., and D. F. Day. 1994. A new process for the production of clinical dextran by mixed-culture fermentation of Lipomyces starkeyi and Leuconostoc mesenteroides. Enzyme Microb. Technol. 16:844-848.
91. Kim, D., and J. F. Robyt. 1995. Production, selection, and characteristics of mutants of Leuconostoc mesenteroides B-742 constitutive for dextransucrases. Enzyme Microb. Technol. 17:689-695.
92. Kim, D., and J. F. Robyt. 1995. Dextransucrase constitutive mutans of Leuconostoc mesenteroides B-1299. Enzyme Microb. Technol. 17:1050-1056.
93. Kim, D., and D. F. Day. 1995. Isolation of a dextranase constitutive mutant of Lipomyces starkeyi and its use for the production of clinical size dextran. Lett. Appl. Microbiol. 20:268-270.
94. Kim, Y.-K., Y. Tsumuraya, and Y. Sakano. 1995. Enzymatic preparation of novel non-reducing oligosaccharides having an isomaltosyl residue by using the transfer action of isomaltodextranase from Arthrobacter globiformis T6. Biosci. Biotechnol. Biochem. 59:1367-1369.
95. Kim, D.-W., S.-J. Heo, and S.-J. Ryu. 2001. Enzyme capable of hydrolyzing plaque, microorganism producing the same, and a composition comprising the same. WO patent publication 01/66570.
96. Kim, D., J. F. Robyt, S. Y. Lee, J. H. Lee, and Y.-M. Kim. 2003. Dextran molecular size and degree of branching as a function of sucrose concentration, pH, and temperature of reaction of Leuconostoc mesenteroides B-512FMCM dextransucrase. Carbohydr. Res. 338:1183-1189.
97. Kitahata, S., C. F. Brewer, D. S. Genghof, T. Sawai, and E. J. Hehre. 1981. Scope and mechanism of carbohydrase action. J. Biol. Chem. 256:6017-6026.
98. Kitaoka, M., and J. F. Robyt. 1998. Large-scale preparation of highly purified dextrasucrase from a high producing constitutive mutant of Leuconostoc mesenteroides B -512FMC. Enzyme Microb. Technol. 23:386-391.
99. Ko, W., C. Wong, H. Yeung, M. Yung, P. Shaw, and S. Tam. 1991. Increas-ing the plasma half-life of trichosanthin by coupling to dextran. Biochem. Pharmacol. 42:1721-1728.
100. Kobayashi, M., Y. Mitsuishi, and K. Matsuda. 1978. Pronounced hydrolysis of highly branched dextrans with a new type of dextranase. Biochem. Biophys. Res. Commun. 80:306-312.
101. Kobayashi, M., S. Tagaki, M. Shiota, Y. Mitsuishi, and K. Matsuda. 1983. An isomaltotriose-producing dextranase from Flavobacierium sp. M-73: Purification and properties. Agric. Biol. Chem. 47:2585-2593.
102. Kobayashi, M., H. Utsugi, and K. Matsuda. 1986. Intensive UV absorption of dextrans and its application to enzyme reactions. Agric. Biol. Chem. 50: 1051-1053.
103. Kobayashi, M., H. Utsugi, and K. Matsuda. 1987. Fluorospectral intensity of high-molecular-weight dextrans: application to the enzyme reactions. Agric. Biol. Chem. 51:2073-2079.
104. Kobayashi, M., K. Funane, and T. Oguma. 1995. Inhibition of dextran and mutan synthesis by cycloisomaltooligosaccharides. Biosci. Biotechnol. Biochem. 59:1861-1865.
105. Koenig, D. W., and D. F. Day. 1989. Induction of Lipomyces starkeyi dextranase. Appl. Environ. Microbiol. 55:2079-2081.
106. Koenig, D. W., and D. F. Day. 1989. The purification and characterization of a dextranase from Lipomyces starkeyi. Eur. J. Biochem. 183:161-167.
107. Koh, T. Y., and B. T. Khouw. 1970. Rapid method for the assay of dextranase. Can. J. Biochem. 48:225-227.
108. Kolenbrander, P. E., R. N. Andersen, D. S. Blehert, P. G. Egland, J. S. Foster, and R. J. Palmer, Jr. 2002. Communication among oral bacteria. Microbiol. Mol. Biol. Rev. 66:486-505.
109. Kubik, C., B. Sikora, and S. Bielecki. 2004. Immobilization of dextransucrase and its use with soluble dextranase for glucooligosaccharides synthesis. Enzyme Microb. Technol. 34:555-560.
110. Kubo, S., H. Kubota, Y. Ohnishi, T. Morita, T. Matsuya, and A. Matsushiro. 1993. Expression and secretion of an Arthrobacter dextranase in the oral bacterium Streptococcus gordonii. Infect. Immun. 61:4375-4381.
111. Larsson, A. M., R. Andersson, J. Stahlberg, L. Kenne, and T. A. Jones. 2003. Dextranase from Penicillium minioluteum: reaction course, crystal structure, and product complex. Structure. 11:1111-1121.
112. Lawman, P., and A. S. Bleiweis. 1991. Molecular cloning of the extracellular endodextranase of Streptococcus salivarius. J. Bacteriol. 173:7423-7428.
113. Lee, J. M., and P. F. Fox. 1985. Purification and characterization of Paecilomyces lilacinus dextranase. Enzyme Microb. Technol. 7:573-577.
114. Lee, S.-Y., J.-H. Lee, J. F. Robyt, E.-S. Seo, H.-J. Park, and D. Kim. 2003. Demonstration of two independent dextranase and amylase active sites on a single enzyme elaborated by Lipomyces starkeyi KSM 22. J. Microbiol. Biotechnol. 13:313-316.
115. Linder, L., and M.-L. Sund. 1981. Characterization of dextran glucosidase (1,6-α-D-glucan glucohydrolase) of Streptococcus mitis. Caries Res. 15:436-444.
116. Loesche, W. J. 1986. Role of Streptococcus mutans in human dental decay. Microbiol. Rev. 50:353-380.
117. Madhu, and K. A. Prabhu. 1984. Studies on dextranase from Penicillium aculeatum. Enzyme Microb. Technol. 6:217-220.
118. Madhu, G. L. Shukla, and K. A. Prabhu. 1984. Application of dextranase in the removal of dextran from cane juice. Int. Sugar J. 86:136-138.
119. Mäkelä, M., and T. Korpela. 1998. Determination of the catalytic activity of cyclomaltodextrin glucanotransferase by maltotriose-methylorange assay. J. Biochem. Biophys. Methods 15:307-318.
120. Mäkinen, K. K., and I. K. Paunio. 1971. Exploitation of Blue dextran as a dextranase substrate. Anal. Biochem. 39:202-207.
121. Marotta, M., A. Martine, A. Rosa, E. Farina, M. Carteni, and M. Rosa. 2002. Degradation of dental plaque glucans and prevention of glucan formation using commercial enzymes. Process Biochem. 38:101-108.
122. Matsushiro, A. 1986. Dental caries preventive preparations and method for preparing said preparations. European patent application 86302044.2.
123. Mattiasson, B. 1980. A simple method involving aqueous separation-systems for activity determination of enzymes hydrolyzing macromolecular substrates. Anal. Lett. 13:851-860.
124. Mattsson, P., Battchikova, N., Sippola, K., and T. Korpela. 1995. The role of histidine residues in the catalytic act of cyclomaltodextrin glucanotransferase from Bacillus circulons var. alcalophilus. Biochim. Biophys. Acta 1247:97-103.
125. Mattsson, P., Korpela, T., Paavilainen, S., and M. Mäkelä. 1990. Enhanced conversation of starch to cyclodextrins in ethanolic solutions by Bacillus circulons var. alcalophilus cyclomaltodextrin glucanotransferase. Appl. Biochem. Biotechnol. 30:17-28.
126. McCabe, M. M., and R. M. Hamelik. 1982. An enzyme from Streptococcus mutans forms branches on dextran in the absence of sucrose. Biochem. Biophys. Res. Commun. 115:287-294.
127. Mehvar, R. 2000. Dextrans for targeted and sustained delivery of therapeutic and imaging agents. J. Control. Release 69:1-25.
128. Mghir, A. S., A. C. Cremieux, R. Jambou, M. Muffat-Joly, J. J. Pocidalo, and C. Carbon. 1994. Dextranase enhances antibiotic efficacy in experimental viridans streptococcal endocarditis. Antimicrob. Agents Chemother. 38: 953-958.
129. Miller, G. L., R. Blum, W. E. Glennon, and A. L. Burton. 1960. Measurement of carboxymethylcellulase activity. Anal. Chem. 1:127-132.
130. Misaki, A., M. Torii, T. Sawai, and I. J. Goldstein. 1980. Structure of the dextran of Leuconostoc mesenteroides. Carbohydr. Res. 84:273-285.
131. Mitsuishi, Y., M. Kobayashi, and K. Matsuda. 1979. Dextran α-1,2 de-branching enzyme from Flavobacterium sp. M-73: its production and purification. Agric. Biol. Chem. 43:2283-2290.
132. Mitsuishi, Y., M. Kobayashi, and K. Matsuda. 1980. Dextran α-(1→2)-debranching enzyme from Flavobacterium sp. M-73. Properties and mode of action. Carbohydr. Res. 83:303-313.
133. Mizuno, T., H. Mori, H. Ito, H. Matsui, A. Kimura, and S. Chiba. 1999. Molecular cloning of isomalto-dextranase gene from Brevibacterium fuscum var. dextranlyticum strain 0407 and its expression in Escherihia coli. Biosci. Biotechnol. Biochem. 63:1582-1588.
134. Mizuno, M., T. Tonozuka, S Suzuki, R. Uotsu-Tomita, S. Kamitori, A. Nishikawa, and Y. Sakano. 2004. Structural insights into substrate specificity and function of glucodextranase. J. Biol. Chem. 279:10575-10583.
135. Monchois, V., R.-M. Willemot, and P. Monsan. 1999. Glucansucrases: mechanism of action and structure-function relationships. FEMS Microbiol. Rev. 23:131-151.
136. Monsan, P., S. Bozonnet, C. Albenne, G. Joucla, R.-M. Willemot, and M. Remaund-Siméon. 2001. Homopolysaccharides from lactic acid bacteria. Int. Dairy J. 11:675-685.
137. Morisaki, H., T. Igarashi, A. Yamamoto, N. Goto. 2002. Analysis of a dextran-binding domain of the dextranase of Streptococcus mutans. Lett. Appl. Microbiol. 35:223-227.
138. Moriyama, K., and N. Yui. 1996. Regulated insulin release from biodegradable dextran hydrogels containing poly(ethylene glycol). J. Control. Release 42:237-248.
139. Mumtaz, S., and B. K. Bachhawat. 1994. Enhanced imracellular stability and efficacy of PEG modified dextranase in the treatment of a model storage disorder. Biochem. Biophys. Acta 1199:175-182.
140. Newbrun, E., and M. Sharma. 1976. Further studies on extracellular glucans synthesized by glucosyltransferases of oral streptococci. Caries Res. 10: 255-272.
141. Novak, L. J., and G. S. Stoycos. 1958. Method for producing clinical dextran. U.S. patent 2,841,578.
142. Novak, L. J., and G. S. Stoycos. 1961. Method of producing clinical dextran. U.S. patent 2,972,567.
143. Oguma, T., T. Horiuchi, and M. Kobayashi. 1993. Novel cyclic dextrans, cycloisomaltooligosaccharides, from Bacillus sp. T-3040 culture. Biosci. Biotechnol. Biochem. 57:1225-1227.
144. Oguma, T., K. Tobe, and M. Kobayashi. 1994. Purification and properties of a novel enzyme from Bacillus spp. T-3044, which catalyzes the conversion of dextran to cyclic isomaltooligosaccharides. FEBS Lett. 345:135-138.
145. Oguma, T., T. Kurokawa, K. Tobe, and M. Kobayashi. 1995. Cloning and sequence analysis of the cycloisomaltooligosaccharide glucanotransferase gene from Bacillus circulans T-3040 and expression in Eschenchia coli cells. Oyo Toshitsu Kagaku 42:415-419. (In Japanese.)
146. Oguma, T., T. Kurokawa, K. Tobe, S. Kitao, and M. Kobayashi. 1996. Purification and some properties of glucodextranase from Arthrobacter globifomis T-3044. J. Appl. Glycosci. 43:73-78.
147. Oguma, T., T. Kurokawa, K. Tobe, S. Kitao, and M. Kobayashi. 1999. Cloning and sequence analysis of the gene for glucodextranase from Arthrobacter globiformis T-3044 and expression in Eschenchia coli cells. Biosci. Biotechnol. Biochem. 63:2174-2182.
148. Oguma, T., and K. Hiroshi. 2003. Production of cyclodextran and its application. Trends Glycosci. Glycotech. 15:91-99.
149. Ohnishi, Y. S. Kubo, Y. Ono, M. Nozaki, Y. Gonda, H. Okano, T. Matsuya, A. Matsushiro, and T. Morita. 1995. Cloning and sequencing of the gene coding for dextranase from Streptococcus salivarius. Gene 156:93-96.
150. Okada, G., T. Takayanagi, and T. Sawai. 1988. Improved purification and further characterization of an isomaltodextranase from Arthrobacter globiformis T6. Agric. Biol. Chem. 52:495-502.
151. Okada, G., T. Takayanagi, S. Miyahara, and T. Sawai. 1988. An isomaltodextranase accompanied by isopullulanase activity from Arthrobacter globiformis T6. Agric. Biol. Chem. 52:829-836.
152. Okada, G., T. Unno, and T. Sawai. 1988. A simple purification for and further characterization of a glucodextranase from Arthrobacter globiformis 142. Agric. Biol. Chem. 52:2169-2176.
153. Okada, G., and T. Unno. 1989. Glucodextranase accompanied by glucoamylase activity from Arthrobacter globiformis 142. Agric. Biol. Chem. 53:223-228.
154. Okami, Y., S. Kurasava, and Y. Hirose. 1980. A new glucanase produced by a marine Bacillus. Agric. Biol. Chem. 44:1191-1192.
155. Okushima, M., D. Sugino, Y. Kouno, S. Nakano, J. Miyahara, H. Toda, S. Kubo, and A. Matsushiro. 1991. Molecular cloning and nucleotide sequencing of the Arthrobacter dextranase gene and its expression in Escherichia coli and Streptococcus sanguis. Jpn. J. Genet. 66:173-187.
156. Padmanabhan, P. A., and D.-S. Kim. 2002. Production of insoluble dextran using cell-bound dextransucrase of Leuconostoc mesenteroides NRRL-523. Carbohydr. Res. 337:1529-1523.
157. Pleszczynska, M., J. Rogalski, J. Szczodrak, and J. Fiedurek. 1996. Purification and some properties of an extracellular dextranase from Penicillium notatum. Mycol. Res. 100:681-686.
158. Pleszczynska, M., J. Szczodrak, J. Rogalski, and J. Fiedurek. 1997. Hydrolysis of dextran by Penicillium notatum dextranase and indentification of final digestion products. Mycol. Res. 101:69-72.
159. Pons, T., G. Chinea, O. Olmea, A. Beldarrain, H. Roca, G. Padron, and A. Valencia. 1998. Structural model of Dex protein from Penicillium minioluteum and its implications in the mechanism of catalysis. Proteins 31:345-354.
160. Pons, T., B. Garcia, and A. Castellanos. 2000. Sequence analysis and structure prediction of dexB, dexC and dexD genes induced in dextran-containing cultures of Penicillium minioluteum. Biotechnol. Apl. 17:195-197.
161. Preobrazhenskaya, M. E., A. L. Minakova, and E. L. Rozenfel'd. 1974. Studies on the dextranase activity of pig-spleen acid α-D-glucosidase. Car-bohydr. Res. 38:267-277.
162. Pulkownik, A., and G. J. Walker. 1977. Purification and substrate specificity of an endo-dextranase Streptococcus mutons K1-R. Carbohydr. Res. 54: 237-251.
163. Ramos, A., and I. Spencer-Martins. 1983. Extracellular glucose-producing exodextranase of the Lipomyces lipofer. Antonie van Leeuwenhoek 49: 183-190.
164. Richards, G. N., and M. Streamer. 1972. Studies on dextranases. Part I. Isolation of extracellular, bacterial dextranases. Carbohydr. Res. 25:323-332.
165. 1 on oligosaccharides. Carbohydr. Res. 32: 251-260.
166. 2 from Pseudomonas UQM 733 on oligosaccharides. Carbohydr. Res. 62: 191-196.
167. Riffer, R. 1982. Enzyme electrode and method for dextran analysis. U.S. patent 4,552,840.
168. Robyt, J. F., and T. F. Walseth. 1979. Production, purification, and properties of dextransucrase from Leuconostoc mesenteroides NRRL B-512F. Carbohydr. Res. 68:95-111.
169. Rogalski, J., J. Szczodrak, G. Gl'owiak, M. Pleszczynska, Z. Szczodrak, and A. Wiater. 1998. Purification and immobilization of dextranase. Acta Biotechnol. 18:63-75.
170. Rozenfel'd, E. L., and A. S. Saenko. 1964. Metabolism in vivo of clinical dextran. Clin. Chim. Acta 10:223-228.
171. Russell, R. R. B., and J. J. Ferretti. 1990. Nucleotide sequence of the dextran glucosidase (dexB) gene of Streptococcus mutons. J. Gen. Microbiol. 136:803-810.
172. Ryu, S.-J., D. Kim, H. J. Ryu, S. Chiba, A. Kimura, and D. F. Day. 2000. Purification and partial characterization of a novel glucanhydrolase from Lipomyces starkeyi KSM 22 and its use for inhibition of insoluble glucan formation. Biosci. Biotechnol. Biochem. 64:223-228.
173. Safanik, I. 1990. Rapid detection of dextranases in liquid samples. Biomed. Biochim. Acta 49:625-628.
174. Šafaøik, I., and M. Safarikova. 1992. A new substrate for the determination of dextranase activity in colored samples. Biotechnol. Appl. Biochem. 16: 263-268.
175. Sankpal, N. V., A. P. Joshi, S. R. Sainkar, and B. D. Kulkarni. 2001. Production of dextran by Rhizopus sp. Immobilized on porous cellulose support. Process Biochem. 37:395-403.
176. Santos, M., J. Teixeira, and A. Rodrigues. 2000. Production of dextransucrase, dextran and fructose from sucrose using Leuconostoc mesenteroides NRRL B512(f). Biochem. Eng. J. 4:177-188.
177. Sawai, T., K. Toriyama, and K. Yano. 1974. A Bacterial dextranase releasing only isomaltose from dextrans. J. Biochem. 75:105-112.
178. Sawai, T., and Y. Niwa. 1975. Transisomaltosylation activity of a bacterial isomaltodextranase. Agric. Biol. Chem. 39:1077-1083.
179. Sawai, T., Y. Ukigai, and A. Nawa. 1976. Identification of an isomalto-dextranase producing bacterium, Arthrobacter globiformis T6. Agric. Biol. Chem. 40:1246-1250.
180. Sawai, T., T. Yamaki, and T. Ohya. 1976. Purification and some properties of Arthrobacter globiformis exo-1,6-α-glucosidase. Agric. Biol. Chem. 40: 1293-1299.
181. Sawai, T., T. Tohyama, and T. Natsume. 1978. Hydrolysis of fourteen native dextrans by Arthrobacter isomaltodextranase and correlation with dextran structure. Carbohydr. Res. 66:195-205.
182. Sawai, T., S. Ohara, Y. Ichimi, S. Okaji, K. Hisada, and N. Fukaya. 1981. Purification and some properties of the isomaltodextranase of Actinomadura strain R10 and comparison with that of Arthrobacter globiformis T6. Carbohydr. Res. 89:289-299.
183. Schachtele, C. F., R. H. Staat, and S. K. Harlander. 1975. Dextranases from oral bacteria. Inhibition of water-insoluble glucan production and
184. Schilling, K. M., and W. H. Bowen. 1992. Glucans synthesized in situ in experimental salivary pellicle function as specific binding sites for Streptococcus mutans. Infect. Immun. 60:284-295.
185. Serhir, B., D. Dugourd, M. Jacques, R. Higgins, and J. Harel. 1997. Cloning and characterization of a dextranase gene (dexS) from Streptococcus suis. Gene 190:257-261.
186. Sery, T. W., and E. J. Hehre. 1956. Degradation of dextrans by enzymes of intestinal bacteria. J. Bacteriol. 71:373-380.
187. Seymour, F. R., and R. D. Knapp. 1980. Structural analysis of dextrans, from strains of Leuconostoc and related genera that contain 3-O-α-D- glucosylated α-D-glucopyranosyl residues at the branch points, or in consecutive, linear positions. Carbohydr. Res. 81:105-129.
188. Shimada, K., M. Akiyama, and M. Sudo. 1984. Oral composition containing dextranase and α-1,3 glucanase and a method for preventing and suppress-ing oral diseases using the same. U.S. patent 4,438,093.
189. Shimizu, E., T. Unno, M. Ohba, and G. Okada. 1998. Purification and characterization of an isomaltotriose-producing endo-dextranase from a Fusarium sp. Biosci. Biotechnol. Biochem. 62:117-122.
190. Shiroza, T., N. Shinozaki, M. Hayakawa, T. Fujii, T. Oguma, M. Kobayashi, K. Fukushima, and Y. Abiko. 1998. Application of the resident plasmid integration technique to construct a strain of Streptococcus gordonii able to express the Bacillus circulons cycloisomaltooligosaccharide glucanotransferase gene, and secrete its active gene product. Gene 207:119-126.
191. Sidebotham, R. L. 1974. Dextrans. Adv. Carbohydr. Chem. Biochem. 30: 371-444.
192. Sims, I. M., A. Thomson, U. Hubl, N. G. Larasen, and R. H. Furneaux. 2001. Characterization of polysaccharides synthesized by Gluconobacter oxydans NCIMB 4943. Carbohydr. Polym. 45:285-292.
193. Sinha, V. R., and R. Kumria. 2001. Colonic drug delivery: prodrug approach. Pharm. Res. 18:557-564.
194. Singlenton, V., J. Horn, C. Bucke, and M. Adlard. 2001. A new polarimetric method for the analysis of dextran and sucrose. Int. Sugar J. 103:251-254.
195. Somogyi, M. 1945. Determination of blood sugar. J. Biol. Chem. 160:69-73.
196. Staat, R. H., and C. F. Schachtele. 1976. Analysis of the dextranase activity produced by an oral strain of Bacteroides ochraceus. J. Dent. Res. 55: 1103-1110.
197. Steels, J. D., R.-M. Schoth, and J. P, Jensen. 2001. A simple, quick enzymatic spectrophotometric assay specific for dextran. Zuckerindustrie 126: 264-268.
198. Sugiura, M., A. Ito, T. Ogiso, K. Kato, and H. Asano. 1973. Purification of dextranase from Penicillium funiculosum and its enzymatic properties. Biochim. Biophis. Acta 309:357-362.
199. Sugiura, M., A. Ito, and T. Yamaguchi. 1974. Studies on dextranase II. New exo-dextranase from Brevibactenum fuscum var. dextranlyticum. Biochim. Biophys. Acta 350:61-70.
200. Sugiura, M., and A. Ito. 1975. Enzymes. IC. Dextranase. VI. Physicochemical properties and amino acid composition of dextranases from Brevibacterium fuscum var. dextranlyticum and Penicillium funiculosum IAM. Chem. Pharm. Bull. 23:1304-1308.
201. Sun, J.-W., S.-Y. Wanda, R. Curtiss. 1995. Purification, characterization, and specificity of dextranase inhibitor (Dei) expressed from Streptococcus sobrinus UAB108 gene cloned in Escherichia coli J. Bacteriol. 176:7213-7222.
202. Takagi, S., M. Shiota, Y. Mitsuishi, M. Kobayashi, and K. Matsuda. 1984. An isomaltotriose-producing dextranase from Flavobacterium sp. M-73: action pattern of the enzyme. Carbohydr. Res. 129:167-177.
203. Takagia, K., R. Ioroib, T. Uchimuraa, M. Kozakic, and K. Komagataa. 1994. Purification and some properties of dextransucrase from Streptococcus bovis 148. J. Ferment. Bioeng. 77:551-553.
204. Takahashi, N. 1982. Isolation and properties of dextranase from Bacte-roides oralis Ig4a. Microbiol. Immunol. 26:375-386.
205. Takahashi, N., Y. Saton, and K. Takamori. 1985. Subcellular localization of D-glucanases in Bacteroides oralis Ig4a. J. Gen. Microbiol. 131:1077-1082.
206. Takayanagi, T., A. Kimura, H. Matsui, G. Okada, and Chiba, S. 2001. Evidence for a single active site on isomalto-dextranase with hydrolysis activities of a-exodextran-and α-1,4-glucosidic linkages. J. Appl. Glycosci. 48:55-61.
207. Tallgren, A. H., U. Airaksinen, R. Weissenberg, H. Ojamo, J. Kuusisto, and M. Leisola. 1999. Exopolysaccharide-producing bacteria from sugar beets. Appl. Environ. Microbiol. 65:862-864.
208. Taylor, C., N. W. H. Cheetham, M. E. Slodki, and G. J. Walker. 1990. Action of endo-(1→6)-α-D-glucanases on the soluble dextrans produced by three extracellular α-D-glucosyltransferases of Streptococcus sobrinus. Carbohydr. Polym. 13:423-436.
209. Tirtaatmadja, V., D. E. Dunstan, and D. V. Boger. 2001. Rheology of dextran solutions. J. Non-Newtonian Fluid Mech. 97:295-301.
210. Tochihara, T., K. Sasaki, O. Araki, N. Morimoto, K. Watanabe, Y. Hatada, S. Ito, H. Ito, and H. Matsui. 2004. Site-directed mutagenesis establishes aspartic acids-227 and -342 as essential for enzyme activity in an isomalto-dextranase from Arthrobacter globiformis. Biotechnol. Lett. 26:659-664.
211. Torii, M., K. Sakakibara, A. Misaki, and T. Sawai. 1976. Degradation of alpha-linked D-gluco-oiigosaccharides and dextrans by an isomalto-dextranase preparation from Arthrobacter globiformis T6. Biochem. Biophys. Res. Commun. 70:459-464.
212. Tsuchiya, R. 2001. Composition for the removal of dental plaque. U.S. patent 6,254,856.
213. Tsuru, D., N. Hiraoka, and J. Fukimoto. 1972. Studies on mould dextranases IV. Substrate specificity of Aspergillus carneus dextranase. J. Biochem. 71:653-660.
214. Ulitzsch, M., and C. Scholzf. 1988. Dextranase treatment of dextran for manufacture of dextran with better pharmaceutical properties. German patent 255,953.
215. Walker, G. J. 1972. Some properties of a dextranglucosidase isolated from oral streptococci and its use in studies on dextran synthesis. J. Dent. Res. 51:409-414.
216. Walker, G. J., and A. Pulkownik. 1973. Degradation of dextrans by α-exodextran-glucan glucohydrolase from Streptococcus mitis. Carbohydr. Res. 29: 1-14.
217. Walker, G. J., and A. Pulkownik. 1974. Action of α-1,6-glucan glucohydrolase on oligosaccharides derived from dextran. Carbohydr. Res. 36:53-66.
218. Walker, G. J., and M. D. Dewar. 1975. The action pattern of Penicillium lilacinum dextranase. Carbohydr. Res. 39:303-315.
219. Walker, G. J., and M. D. Hare. 1977. Metabolism of the polysaccharides of human plaque. Part II. Purification and properties of Cladosporium resinae α-1,3-D glucanase, and the enzymatic hydrolysis of glucans synthesized by extracellular D-glucosyltransferases of oral streptococci. Carbohydr. Res. 58:415-432.
220. Walker, G. J., A. Pulkownik, and J. G. Morrey-Jones. 1981. Metabolism of the polysaccharides of human dental plaque: release of dextranase in batch cultures of Streptococcus mutons. J. Gen. Microbiol. 127:201-208.
221. Walker, G. J., N. W. H. Cheetham, C. Taylor, B. J. Pearce, and M. E. Slodki. 1990. Productivity of four α-D-glucosyltransferases released by Streptococcus sobrinus under defined conditions in continuous culture. Carbohydr. Polym. 13:399-421.
222. Wanda, S.-Y., and R. Curtiss. 1994. Purification and characterization of Streptococcus sobrinus dextranase produced in recombinant Escherichia coli and sequence analysis of the dextranase gene. J. Bacteriol. 176:839-3850.
223. Wanda, S.-Y., and R. Curtiss. 1995. Purification, characterization, and specificity of dextranase inhibitor (Dei) expressed from Streptococcus sobrinus UAB108 gene cloned in Escherichia coli. J. Bacteriol. 177:1703-1711.
224. Webb, E., and I. Spencer-Martins. 1983. Extracellular endodextranase from the yeast Lipomyces starkeyi. Can. J. Microbiol. 29:1092-1095.
225. Wheatley, M. A., and M. Moo-Young. 1977. Degradation of polysaccharides by endo- and exoenzymes: dextran-dextranase mould system. Biotechnol. Bioeng. 19:219-233.
226. Whiting, G. C., I. C. Sutcliffe, and R. R. B. Russell. 1993. Metabolism of polysaccharides by the Streptococcus mutans dexB gene product. J. Gen. Microbiol. 139:2019-2026.
227. Wynter, C., B. K. C. Patel, P. Bain, J. De Jersey, S. Hamilton, and P. A. Inkerman. 1996. A novel thermostable dextranase from a Thermoanaerobacter species cultured from the geothermal waters of the Great Artesian Basin of Australia. FEMS Microbiol. Lett. 140:271-276.
228. Wynter, C., M. Chang, J. De Jersey, B. Patel, P. A. Inkerman, and S. Hamilton. 1997. Isolation and characterization of a thermostable dextranase. Enzyme Microb. Technol. 20:242-247.
229. Yamamoto, K., K. Yoshikawa, and S. Okada. 1993. Effective dextran production from starch by dextrin dextranase with debranching enzyme. J Ferment. Bioeng. 76:411-413.
230. Yamashita, Y., W. H. Bowen, R. A. Burne, and H. K. Kuramitsu. 1993. Role of Streptococcus mutans gtf genes in caries induction in the specific-pathogen-free rat model. Infect. Immun. 61:3811-3817.
231. Zevenhuizen, L. P. T. 1968. Cell-bound exodextranase of Bacillus species. Carbohydr. Res. 6:310-318.
232. Zhou, M., C. Zhang, R. H. Upson, and R. P. Haugland. 1998. Two fluorometric approaches to the measurement of dextranase activity. Anal. Biochem. 260:257-259.
233. Zinchenko, O. N., V. I. Shishlo, O. V. Krivosheeva, and A. G. Lobanok. 1993. Fungal and yeast dextranases: properties and prospects for application in sugar industry. Prikl. Biokh. Mikrobiol. 29:851-855. (In Russian.)