This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Satoh, E Articles by Komagata, K Search for Related Content PubMed PubMed Citation Articles by Satoh, E Articles by Komagata, K Agricola Articles by Satoh, E Articles by Komagata, K

 Previous Article  |  Next Article 

Appl Environ Microbiol. 1993 November; 59(11): 3669-3673

Molecular cloning and expression of two alpha-amylase genes from Streptococcus bovis 148 in Escherichia coli.

Department of Agricultural Chemistry, Tokyo University of Agriculture, Japan.

ABSTRACT

The alpha-amylase genes of Streptococcus bovis 148 were cloned in Escherichia coli MC1061, using pBR322. The recombinant plasmids were classified into two groups on the basis of their restriction maps. Southern blot analysis did not show homology between the two types of alpha-amylase genes, and the two alpha-amylase genes existed on the chromosomal DNA of S. bovis 148. The enzymatic properties and N-terminal amino acid sequences of the two purified enzymes produced by the cloned E. coli strains were quite different from each other. Particularly, one alpha-amylase (Amy I) was adsorbed on raw corn starch and hydrolyzed raw corn starch, and another (Amy II) was not adsorbed on raw corn starch and did not hydrolyze raw corn starch. Amy I was considered to be the same as the extracellular alpha-amylase of S. bovis 148 in raw starch absorbability, ability to hydrolyze raw corn starch, enzymatic characteristics, N-terminal amino acid sequence, and mode of action on soluble starch. Amy II showed a unique pattern of oligosaccharide production from soluble starch compared with the extracellular alpha-amylase of S. bovis 148. Amy II was suggested to be an intracellular alpha-amylase of S. bovis 148.

This article has been cited by other articles:

• Okano, K., Zhang, Q., Shinkawa, S., Yoshida, S., Tanaka, T., Fukuda, H., Kondo, A. (2009). Efficient Production of Optically Pure D-Lactic Acid from Raw Corn Starch by Using a Genetically Modified L-Lactate Dehydrogenase Gene-Deficient and {alpha}-Amylase-Secreting Lactobacillus plantarum Strain. Appl. Environ. Microbiol. 75: 462-467 [Abstract] [Full Text]  
• Okano, K., Zhang, Q., Kimura, S., Narita, J., Tanaka, T., Fukuda, H., Kondo, A. (2008). System Using Tandem Repeats of the cA Peptidoglycan-Binding Domain from Lactococcus lactis for Display of both N- and C-Terminal Fusions on Cell Surfaces of Lactic Acid Bacteria. Appl. Environ. Microbiol. 74: 1117-1123 [Abstract] [Full Text]  
• Shigechi, H., Koh, J., Fujita, Y., Matsumoto, T., Bito, Y., Ueda, M., Satoh, E., Fukuda, H., Kondo, A. (2004). Direct Production of Ethanol from Raw Corn Starch via Fermentation by Use of a Novel Surface-Engineered Yeast Strain Codisplaying Glucoamylase and {alpha}-Amylase. Appl. Environ. Microbiol. 70: 5037-5040 [Abstract] [Full Text]  
• Simpson, C. L., Russell, R. R. B. (1998). Intracellular alpha -Amylase of Streptococcus mutans. J. Bacteriol. 180: 4711-4717 [Abstract] [Full Text]