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- W2510168357 abstract "A strain of Lactobacillus fermentum producing two isozymes of a 20 kDa β-amylase was isolated from the faecal sample of a newborn. The starin was identified by sequencing its 16S rRNA gene. The two β-amylase isozymes were resolved and visualized by two dimensional protein gel electrophoresis (2-D gel electrophoresis). Some of the physical and biochemical properties of the enzymes were characterized. The β-amylase displayed two optimum pH s, 5.0 and 10.0 and two optimum temperatures, 45 °C and 37 °C, respectively. The isozymes hydrolyzed different substrates: glycogen at pH 5.0, and corn starch at pH 10.0. The activity did not require Ca2+, though the activity at pH 10.0 was enhanced in the presence of 5.0 mM and 10.0 mM CaCl2, 110% and 130%, respectively." @default.
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- W2510168357 date "2016-12-01" @default.
- W2510168357 modified "2023-10-17" @default.
- W2510168357 title "Characterization of thermostable β-amylase isozymes from Lactobacillus fermentum" @default.
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- W2510168357 doi "https://doi.org/10.1016/j.ijbiomac.2016.08.078" @default.
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