当前位置： SCI文献检索 > INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES期刊下所有文献 > Biochemical characterization of a novel β-galactosidase from Paenibacillus barengoltzii suitable for lactose hydrolysis and galactooligosaccharides synthesis.

Biochemical characterization of a novel β-galactosidase from Paenibacillus barengoltzii suitable for lactose hydrolysis and galactooligosaccharides synthesis.

Abstract：

:A β-galactosidase gene (PbBGal2A) was cloned from Paenibacillus barengoltzii and expressed in Escherichia coli. The in silico analysis of the deduced amino acid sequences revealed that PbBGal2A shared the highest identity of 40% with the characterized glycoside hydrolase (GH) family 2 β-galactosidase from Actinobacillus pleuropneumoniae. The recombinant β-galactosidase (PbBGal2A) was purified with a molecular mass of 124.2kDa on SDS-PAGE. The optimal pH and temperature of PbBGal2A were determined to be pH 7.5 and 45°C, respectively. PbBGal2A was stable within pH 6.0-8.0 and up to 45°C. It completely hydrolyzed the lactose in milk and whey powder solution. In addition, PbBGal2A exhibited high transglycosylation activity and a maximum yield of 47.9% (w/w) for galactooligosaccharides (GOS) production was obtained in 8h at a lactose concentration of 350g/L. These properties make PbBGal2A an ideal candidate for commercial use in the production of lactose-free milk and GOS.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Liu Y,Chen Z,Jiang Z,Yan Q,Yang S

doi

10.1016/j.ijbiomac.2017.06.073

subject

Has Abstract

pub_date

2017-11-01 00:00:00

pages

1055-1063

issue

Pt A

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(17)30507-X

journal_volume

104

pub_type

杂志文章

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