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. 1971 May;106(2):561–570. doi: 10.1128/jb.106.2.561-570.1971

Extracellular Transglucosylase and α-Amylase of Streptococcus equinus1

Ernest W Boyer a,2, Paul A Hartman a
PMCID: PMC285131  PMID: 4995651

Abstract

Culture filtrates of Streptococcus equinus 1091 contained α-amylase and transglucosylase. The effects of calcium carbonate, age of inoculum, concentration of maltose, and duration of the fermentation on α-amylase and transglucosylase production were determined. The extracellular α-amylase was purified 48-fold and was free of transglucosylase activity. The α-amylase (amylose substrate) required Cl− for maximum activity; ethylenediaminetetraacetic acid (EDTA) partially inhibited activity, but CaCl2 prevented EDTA inhibition. The temperature optimum was 38 C at pH 7.0, and the pH optimum was 7.0 at 37 C in the presence of CaCl2. Predominant final products of amylose hydrolysis, in order of decreasing prevalence, were maltose, maltotriose, maltotetraose, and glucose. The α-amylase showed no evidence of multiple attack. The extracellular transglucosylase was purified 27-fold, but a small amount of α-amylase remained. Transglucosylase activity (amylose substrate) was not increased in the presence of CaCl2. The temperature optimum was 37 C at pH 6.5, and the pH optimum was 6.0 at 37 C. Carbohydrates that served as acceptors for the transglucosylase to degrade amylose were, in order of decreasing acceptor efficiency: d-glucose, d-mannose, l-sorbose, maltose, sucrose, and trehalose. The extracellular transglucosylase of S. equinus 1091 synthesized higher maltodextrins in the medium when the cells were grown in the presence of maltose.

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Selected References

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  1. Abdullah M., French D., Robyt J. F. Multiple attack by alpha-amylases. Arch Biochem Biophys. 1966 Jun;114(3):595–598. doi: 10.1016/0003-9861(66)90385-7. [DOI] [PubMed] [Google Scholar]
  2. DEIBEL R. H. THE GROUP D STREPTOCOCCI. Bacteriol Rev. 1964 Sep;28:330–366. doi: 10.1128/br.28.3.330-366.1964. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. DUNICAN L. K., SEELEY H. W. Starch hydrolysis by Strepto-coccus equinus. J Bacteriol. 1962 Feb;83:264–269. doi: 10.1128/jb.83.2.264-269.1962. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. French D., Mancusi J. L., Abdullah M., Brammer G. L. Separation of starch oligosaccharides by high temperature paper chromatography. J Chromatogr. 1965 Aug;19(2):445–447. doi: 10.1016/s0021-9673(01)99480-4. [DOI] [PubMed] [Google Scholar]
  5. Greenwood C. T., Milne E. A. Starch degrading and synthesizing enzymes: a discussion of their properties and action pattern. Adv Carbohydr Chem Biochem. 1968;23:281–366. doi: 10.1016/s0096-5332(08)60171-x. [DOI] [PubMed] [Google Scholar]
  6. HOBSON P. N., MACPHERSON M. Amylases of Clostridium butyricum and a Streptococcus isolated from the rumen of the sheep. Biochem J. 1952 Dec;52(4):671–679. doi: 10.1042/bj0520671. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. LEVVY G. A., MARSH C. A. Preparation and properties of beta-glucuronidase. Adv Carbohydr Chem. 1959;14:381–428. doi: 10.1016/s0096-5332(08)60227-1. [DOI] [PubMed] [Google Scholar]
  8. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  9. Narayanan A. S., Shanmugasundaram E. R. Studies on amylase of Fusarium vasinfectum. Arch Biochem Biophys. 1967 Feb;118(2):317–322. doi: 10.1016/0003-9861(67)90355-4. [DOI] [PubMed] [Google Scholar]
  10. Niven C. F., Smiley K. L., Sherman J. M. The Hydrolysis of Arginine by Streptococci. J Bacteriol. 1942 Jun;43(6):651–660. doi: 10.1128/jb.43.6.651-660.1942. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Plapp B. V., Cole R. D. Purification and characterization of bovine liver beta-glucuronidase. Arch Biochem Biophys. 1966 Sep 26;116(1):193–206. doi: 10.1016/0003-9861(66)90027-0. [DOI] [PubMed] [Google Scholar]
  12. ROBYT J., FRENCH D. Action pattern and specificity of an amylase from Bacillus subtilis. Arch Biochem Biophys. 1963 Mar;100:451–467. doi: 10.1016/0003-9861(63)90112-7. [DOI] [PubMed] [Google Scholar]
  13. Robyt J. F., French D. Multiple attach hypothesis of alpha-amylase action: action of porcine pancreatic, human salivary, and Aspergillus oryzae alpha-amylases. Arch Biochem Biophys. 1967 Oct;122(1):8–16. doi: 10.1016/0003-9861(67)90118-x. [DOI] [PubMed] [Google Scholar]
  14. SEELEY H. W., DAIN J. A. Starch hydrolyzing streptococci. J Bacteriol. 1960 Feb;79:230–235. doi: 10.1128/jb.79.2.230-235.1960. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. SMITH D. G., SHATTOCK P. M. The serological grouping of Streptococcus equinus. J Gen Microbiol. 1962 Dec;29:731–736. doi: 10.1099/00221287-29-4-731. [DOI] [PubMed] [Google Scholar]
  16. WALKER G. J. A TRANSGLUCOSYLASE OF STREPTOCOCCUS BOVIS. Biochem J. 1965 Feb;94:299–308. doi: 10.1042/bj0940299. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. WALKER G. J. THE CELL-BOUND ALPHA-AMYLASES OF STREPTOCOCCUS BOVIS. Biochem J. 1965 Feb;94:289–298. doi: 10.1042/bj0940289. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. WALKER G. J., WHELAN W. J. The mechanism of carbohydrase action. 4. The mechanism of D-enzyme action. Biochem J. 1957 Dec;67(4):548–551. doi: 10.1042/bj0670548. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. WIESMEYER H., COHN M. The characterization of the pathway of maltose utilization by Escherichia coli. II. General properties and mechanism of action of amylomaltase. Biochim Biophys Acta. 1960 Apr 22;39:427–439. doi: 10.1016/0006-3002(60)90195-5. [DOI] [PubMed] [Google Scholar]
  20. Walker G. J., Hope P. M. Degradation of starch granules by some amylolytic bacteria from the rumen of sheep. Biochem J. 1964 Feb;90(2):398–408. doi: 10.1042/bj0900398. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Walker G. J. Metabolism of the reserve polysaccharide of Streptococcus mitis: Properties of a transglucosylase. Biochem J. 1966 Dec;101(3):861–872. doi: 10.1042/bj1010861. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. van Houte J., Winkler K. C., Jansen H. M. Iodophilic polysaccharide synthesis, acid production and growth in oral streptococci. Arch Oral Biol. 1969 Jan;14(1):45–61. doi: 10.1016/0003-9969(69)90020-x. [DOI] [PubMed] [Google Scholar]

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