Abstract
1. The cell-bound α-amylase of Streptococcus bovis has been isolated from other carbohydrases in the cell extract by chromatography on DEAE-cellulose. The enzyme has been compared with the extracellular α-amylase produced by this organism. 2. The two amylases had similar action patterns on amylose, the main product being maltotriose with smaller amounts of maltose and a little glucose. 3. The cell-bound amylase hydrolysed maltopentaose and maltohexaose at a similar rate to the hydrolysis of amylose. Maltotetraose was hydrolysed six times more slowly, and maltotriose 280 times more slowly, than amylose. 4. Studies with end-labelled maltodextrins revealed that the cell-bound α-amylase preferentially hydrolysed the third linkage from the non-reducing end, liberating maltotriose. The linkage at the reducing end of maltotriose was more easily hydrolysed than the other. 5. Egg-white lysozyme and the extracellular enzymes of Streptomyces albus lysed the cell walls of Streptococcus bovis, releasing amylase into the medium. In the presence of 0·6 m-sucrose 10% of the maximal amylase activity was released by lysozyme. Suspension of the spheroplasts in dilute buffer caused the rupture of the cytoplasmic membrane and the liberation of amylase. 6. A sensitive method for determining the ability of amylases to degrade starch granules is described.
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Selected References
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- ABRAMS A. Reversible metabolic swelling of bacterial protoplasts. J Biol Chem. 1959 Feb;234(2):383–388. [PubMed] [Google Scholar]
- BIBB W. R., STRAUGHN W. R. Formation of protoplasts from Streptococcus faecalis by lysozyme. J Bacteriol. 1962 Nov;84:1094–1098. doi: 10.1128/jb.84.5.1094-1098.1962. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- HUGGETT A. S., NIXON D. A. Use of glucose oxidase, peroxidase, and O-dianisidine in determination of blood and urinary glucose. Lancet. 1957 Aug 24;273(6991):368–370. doi: 10.1016/s0140-6736(57)92595-3. [DOI] [PubMed] [Google Scholar]
- MCCARTY M. The lysis of group A hemolytic streptococci by extracellular enzymes of Streptomyces albus. I. Production and fractionation of the lytic enzymes. J Exp Med. 1952 Dec;96(6):555–568. doi: 10.1084/jem.96.6.555. [DOI] [PMC free article] [PubMed] [Google Scholar]
- PAZUR J. H., BUDOVICH T. Hydrolysis of amylotriose by crystalline salivary amylase. Science. 1955 May 13;121(3150):702–703. doi: 10.1126/science.121.3150.702. [DOI] [PubMed] [Google Scholar]
- 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]
- TREVELYAN W. E., PROCTER D. P., HARRISON J. S. Detection of sugars on paper chromatograms. Nature. 1950 Sep 9;166(4219):444–445. doi: 10.1038/166444b0. [DOI] [PubMed] [Google Scholar]
- 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]
- WALKER G. J., HOPE P. M. The action of some alpha-amylases on starch granules. Biochem J. 1963 Mar;86:452–462. doi: 10.1042/bj0860452. [DOI] [PMC free article] [PubMed] [Google Scholar]
- WELKER N. E., CAMPBELL L. L. EFFECT OF CARBON SOURCES ON FORMATION OF ALPHA-AMYLASE BY BACILLUS STEAROTHERMOPHILUS. J Bacteriol. 1963 Oct;86:681–686. doi: 10.1128/jb.86.4.681-686.1963. [DOI] [PMC free article] [PubMed] [Google Scholar]