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β-Galactosidase from Exiguobacterium acetylicum: Cloning, expression, purification and characterization
- Source :
- Bioresource Technology. 277:211-215
- Publication Year :
- 2019
- Publisher :
- Elsevier BV, 2019.
-
Abstract
- The main goal of this work was to evaluate the performance of β-galactosidase from Exiguobacterium acetylicum MF03 in both hydrolysis and transgalactosylation reactions from different substrates. The enzyme gene was expressed in Escherichia coli BL21 (DE3), sequenced, and subjected to bioinformatic and kinetic assessment. Results showed that the enzyme was able to hydrolyze lactulose and o-nitrophenyl-β-d-galactopyranoside, but unable to hydrolyze lactose, o-nitrophenyl-β-d-glucopyranoside, butyl- and pentyl-β-d-galactosides. This unique and novel substrate specificity converts the E. acetylicum MF03 β-galactosidase into an ideal catalyst for the formulation of an enzymatic kit for lactulose quantification in thermally processed milk. This is because costly steps to eliminate glucose (resulting from hydrolysis of lactose when a customary β-galactosidase is used) can be avoided.
- Subjects :
- 0106 biological sciences
Hot Temperature
Environmental Engineering
Gene Expression
Bioengineering
010501 environmental sciences
medicine.disease_cause
01 natural sciences
Substrate Specificity
Lactulose
Hydrolysis
chemistry.chemical_compound
Exiguobacterium acetylicum
010608 biotechnology
Escherichia coli
medicine
Cloning, Molecular
Lactose
Bacillaceae
Waste Management and Disposal
0105 earth and related environmental sciences
Cloning
Enzyme Gene
chemistry.chemical_classification
Renewable Energy, Sustainability and the Environment
Chemistry
General Medicine
beta-Galactosidase
Kinetics
Enzyme
Biochemistry
Biocatalysis
medicine.drug
Subjects
Details
- ISSN :
- 09608524
- Volume :
- 277
- Database :
- OpenAIRE
- Journal :
- Bioresource Technology
- Accession number :
- edsair.doi.dedup.....00d8b5e9cb7a82f87a10f6a4d8de38c9