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Evaluation of β-galactosidase from Lactobacillus acidophilus as biocatalyst for galacto-oligosaccharides synthesis: Product structural characterization and enzyme immobilization

Journal Article · · Journal of Bioscience and Bioengineering
 [1];  [1];  [1];  [2];  [2];  [3];  [1]
  1. Univ. of Belgrade, Belgrade (Serbia)
  2. INRA, Nantes (France)
  3. Pacific Northwest National Lab. (PNNL), Richland, WA (United States)
β-Galactosidase is an important industrial enzyme that catalyzes reaction of lactose hydrolysis and recently more interesting reaction of transgalactosylation, yielding a highly valuable group of prebiotic compounds named galacto-oligosaccharides (GOS). In this paper, parameters for achieving high yields of tailor-made GOS using crude β-galactosidase obtained from Lactobacillus acidophilus ATCC 4356, probiotic bacteria regarded as safe for human consumption, were optimized. At the same time, detailed structural elucidation of obtained GOS was conducted, and it was concluded that β-galactosidase from L. acidophilus shows a particular specificity towards the formation of β-(1 → 6) glycosidic bonds. In order to develop more stable and economically cost-effective preparation, crude enzyme was successfully immobilized on a methacrylic polymer carrier Lifetech ECR8409, leading to its simultaneous 2-fold purification. In conclusion, this immobilized preparation showed unchanged specificity towards the transgalactosylation reaction, thus yielding 86 g/l GOS under the previously optimized conditions (lactose concentration 400 g/l in 0.1 M sodium phosphate buffer, pH 6.8 and temperature 50°C).
Research Organization:
Pacific Northwest National Laboratory (PNNL), Richland, WA (United States)
Sponsoring Organization:
USDOE
Grant/Contract Number:
AC05-76RL01830
OSTI ID:
1459008
Journal Information:
Journal of Bioscience and Bioengineering, Journal Name: Journal of Bioscience and Bioengineering Journal Issue: 6 Vol. 126; ISSN 1389-1723
Publisher:
Society for Bioscience and Bioengineering, c/o Osaka University., Faculty of Engineering, Yamadaoka 2-1, Suita-shi, Osaka JapanCopyright Statement
Country of Publication:
United States
Language:
English

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Cited By (2)

A new β-galactosidase extracted from the infant feces with high hydrolytic and transgalactosylation activity journal September 2019
Whey valorization using transgalactosylation activity of immobilized β‐galactosidase journal May 2019

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