Abstract
Lactobacillus brevis is found together with the yeast Brettanomyces lambicus during the overattenuation process in spontaneously fermented lambic beer. An isolated L. brevis strain has been shown to produce an α-glucosidase with many similarities to the glucosidase earlier found in B. lambicus. The enzyme was purified by ammonium sulfate precipitation, gel (Sephadex G-150 and Ultrogel AcA-44) filtration, and ion-exchange chromatography (DEAE-Sephadex A-50). The molecular weights of the enzyme, as determined by gel chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis, were about 50,000 and 60,000, respectively. Optimum catalytic activity was obtained at 40°C and pH 6.0. The enzyme showed a decrease of hydrolysis with an increase in the degree of polymerization of the substrate. The Km values for p-nitrophenyl-α-d-glucopyranoside, maltose, and maltotriose were 0.51, 3.0, and 5.2 mM, respectively. There was lack of inhibition by 0.15 mM acarbose and 0.5 M turanose, but the enzyme was inhibited by Tris (Ki value of 25 mM). The α-glucosidase of L. brevis together with the enzyme of B. lambicus seems to be a key factor in the overattenuation of lambic beer, although the involvement of other lactic acid bacteria (pediococci) cannot be excluded.
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- Banno Y., Nozawa Y. Purification and characterization of lysosomal alpha-glucosidase secreted by eukaryote Tetrahymena. J Biochem. 1985 Feb;97(2):409–418. doi: 10.1093/oxfordjournals.jbchem.a135075. [DOI] [PubMed] [Google Scholar]
- Champ M., Szylit O., Raibaud P., Aït-Abdelkader N. Amylase production by three Lactobacillus strains isolated from chicken crop. J Appl Bacteriol. 1983 Dec;55(3):487–493. doi: 10.1111/j.1365-2672.1983.tb01689.x. [DOI] [PubMed] [Google Scholar]
- Guffanti A. A., Corpe W. A. Maltose metabolism of Pseudomonas fluorescens. J Bacteriol. 1975 Oct;124(1):262–268. doi: 10.1128/jb.124.1.262-268.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Guffanti A. A., Corpe W. A. Partial purification and characterization of alpha-glucosidase from Pseudomonas fluorescens W. Arch Microbiol. 1976 Apr 1;107(3):269–276. doi: 10.1007/BF00425338. [DOI] [PubMed] [Google Scholar]
- Kumara H. M., De Cort S., Verachtert H. Localization and Characterization of alpha-Glucosidase Activity in Brettanomyces lambicus. Appl Environ Microbiol. 1993 Aug;59(8):2352–2358. doi: 10.1128/aem.59.8.2352-2358.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
- McWethy S. J., Hartman P. A. Extracellular Maltase of Bacillus brevis. Appl Environ Microbiol. 1979 Jun;37(6):1096–1102. doi: 10.1128/aem.37.6.1096-1102.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Urlaub H., Wöber G. alpha-Glucosidase, a membrane-bound enzyme of alpha-glucan metabolism in Bacillus amyloliquefaciens. Purification and partial characterization. Biochim Biophys Acta. 1978 Jan 12;522(1):161–173. doi: 10.1016/0005-2744(78)90332-7. [DOI] [PubMed] [Google Scholar]
- Vihinen M., Mäntsälä P. Microbial amylolytic enzymes. Crit Rev Biochem Mol Biol. 1989;24(4):329–418. doi: 10.3109/10409238909082556. [DOI] [PubMed] [Google Scholar]
- Wang L. H., Hartman P. A. Purification and some properties of an extracellular maltase from Bacillus subtilis. Appl Environ Microbiol. 1976 Jan;31(1):108–118. doi: 10.1128/aem.31.1.108-118.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]