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Characterization of a Glycoside Hydrolase Family 27 α-Galactosidase from Pontibacter Reveals Its Novel Salt–Protease Tolerance and Transglycosylation Activity
- Source :
- Journal of Agricultural and Food Chemistry. 64:2315-2324
- Publication Year :
- 2016
- Publisher :
- American Chemical Society (ACS), 2016.
-
Abstract
- α-Galactosidases are of great interest in various applications. A glycoside hydrolase family 27 α-galactosidase was cloned from Pontibacter sp. harbored in a saline soil and expressed in Escherichia coli. The purified recombinant enzyme (rAgaAHJ8) was little or not affected by 3.5-30.0% (w/v) NaCl, 10.0-100.0 mM Pb(CH3COO)2, 10.0-60.0 mM ZnSO4, or 8.3-100.0 mg mL(-1) trypsin and by most metal ions and chemical reagents at 1.0 and 10.0 mM concentrations. The degree of synergy on enzymatic degradation of locust bean gum and guar gum by an endomannanase and rAgaAHJ8 was 1.22-1.54. In the presence of trypsin, the amount of reducing sugars released from soybean milk treated by rAgaAHJ8 was approximately 3.8-fold compared with that treated by a commercial α-galactosidase. rAgaAHJ8 showed transglycosylation activity when using sucrose, raffinose, and 3-methyl-1-butanol as the acceptors. Furthermore, potential factors for salt adaptation of the enzyme were presumed.
- Subjects :
- 0301 basic medicine
Sucrose
Glycosylation
medicine.medical_treatment
Gene Expression
Sodium Chloride
03 medical and health sciences
chemistry.chemical_compound
Pentanols
Raffinose
Escherichia coli
medicine
Trypsin
Glycoside hydrolase
Cloning, Molecular
chemistry.chemical_classification
Guar gum
Protease
Alpha-galactosidase
biology
Bacteroidetes
General Chemistry
Recombinant Proteins
030104 developmental biology
Enzyme
chemistry
Biochemistry
alpha-Galactosidase
biology.protein
Locust bean gum
General Agricultural and Biological Sciences
medicine.drug
Subjects
Details
- ISSN :
- 15205118 and 00218561
- Volume :
- 64
- Database :
- OpenAIRE
- Journal :
- Journal of Agricultural and Food Chemistry
- Accession number :
- edsair.doi.dedup.....bb878691411c2286195b7eb8b5942fd6