Characterization of thermostable ß-amylase isozymes from Lactobacillus fermentum.
Int J Biol Macromol
; 93(Pt A): 195-202, 2016 Dec.
Article
em En
| MEDLINE
| ID: mdl-27581558
ABSTRACT
A strain of Lactobacillus fermentum producing two isozymes of a 20kDa ß-amylase was isolated from the faecal sample of a newborn. The starin was identified by sequencing its 16S rRNA gene. The two ß-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 ß-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 5.0mM and 10.0mM CaCl2, 110% and 130%, respectively.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Temperatura
/
Beta-Amilase
/
Limosilactobacillus fermentum
Idioma:
En
Revista:
Int J Biol Macromol
Ano de publicação:
2016
Tipo de documento:
Article
País de afiliação:
Turquia