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A study of cornstarch granule digestion by an unusually high molecular weightα-amylase secreted byLactobacillus amylovorus

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Abstract

The cells ofLactobacillus amylovorus (NRRL B-4540), grown in a medium containing 2% cornstarch as the sole carbon source, secreted an amylase activity that rapidly solubilized cornstarch. Fourier transform infrared (FTIR) spectroscopic analyses showed that 80–90% of starch was consumed by bacteria in a 10-day-old culture medium. The remnant of starch granules digested in the culture medium inoculated with the cells ofL. amylovorus have also lost their characteristic iodine-binding capacity as visualized by starch dye-binding microplate assay and light microscopy. Scanning electron miscroscopy (SEM) of granules from a 48-h culture medium showed hollow and fragmented granules with a pitting phenomenon characteristically produced byα-amylase activity. Analysis of an enzyme preparation from a culture medium ofL. amylovorus revealed that the putative enzyme appears to be a single protein band of unusually high Mr (150,000) on SDS gels stained for amylase activity. Analysis of starch digestion products by thin layer chromatography (TLC) showed enzyme activity typical ofα-amylase.

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Imam, S.H., Burgess-Cassler, A., Cote, G.L. et al. A study of cornstarch granule digestion by an unusually high molecular weightα-amylase secreted byLactobacillus amylovorus . Current Microbiology 22, 365–370 (1991). https://doi.org/10.1007/BF02092156

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