Characterization of thermostable beta-amylase isozymes from Lactobacillus fermentum

KOCABAY S., ÇETİNKAYA S., AKKAYA B., YENİDÜNYA A. F.

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, cilt.93, ss.195-202, 2016 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 93
  • Basım Tarihi: 2016
  • Doi Numarası: 10.1016/j.ijbiomac.2016.08.078
  • Dergi Adı: INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.195-202
  • Anahtar Kelimeler: Beta-amylase, Isozyme, Lactobacillus fermentum, Purification, Two dimentional protein electrophoresis, ALPHA-AMYLASE, RAW-STARCH, PURIFICATION, PROTEIN, ALKALINE, MALTOSE
  • Sivas Cumhuriyet Üniversitesi Adresli: Evet

Özet

A strain of Lactobacillus fermentum producing two isozymes of a 20 kDa beta-amylase was isolated from the faecal sample of a newborn. The starin was identified by sequencing its 16S rRNA gene. The two beta-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 beta-amylase displayed two optimum pH s, 5.0 and 10.0 and two optimum temperatures, 45 degrees C and 37 degrees 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. (C) 2016 Elsevier B.V. All rights reserved.