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Glycoside Hydrolase Family 39 β-Xylosidase of Sphingomonas Showing Salt/Ethanol/Trypsin Tolerance, Low-pH/Low-Temperature Activity, and Transxylosylation Activity.
- Source :
-
Journal of agricultural and food chemistry [J Agric Food Chem] 2018 Sep 12; Vol. 66 (36), pp. 9465-9472. Date of Electronic Publication: 2018 Aug 30. - Publication Year :
- 2018
-
Abstract
- Mining for novel enzymes from new microorganisms is a way to obtain β-xylosidases with promising applications. A Sphingomonas β-xylosidase was expressed in Escherichia coli. The purified recombinant enzyme (rJB13GH39) was most active at pH 4.5 and 50 °C, retaining 10%-50% of its maximum activity at 0-20 °C. Most salts and chemical reagents including 3.0%-20.0% (w/v) NaCl showed little or no effect on the enzymatic activity. rJB13GH39 exhibited 71.9% and 55.2% activity in 10.0% and 15.0% (v/v) ethanol, respectively. rJB13GH39 was stable below 60 °C in 3.0%-30.0% (w/v) NaCl, 3.0%-20.0% (v/v) ethanol, and 2.2-87.0 mg/mL trypsin. The enzyme transferred one xylosyl moiety to certain sugars and alcohols. The salt/ethanol tolerance and low-temperature activity of the enzyme may be attributed to its high structural flexibility caused by high proportions of small amino acids ACDGNSTV and random coils.
- Subjects :
- Bacterial Proteins genetics
Cold Temperature
Enzyme Stability
Hydrogen-Ion Concentration
Sodium Chloride metabolism
Sphingomonas chemistry
Sphingomonas genetics
Substrate Specificity
Xylose metabolism
Xylosidases genetics
Bacterial Proteins chemistry
Bacterial Proteins metabolism
Ethanol metabolism
Sphingomonas enzymology
Trypsin metabolism
Xylosidases chemistry
Xylosidases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1520-5118
- Volume :
- 66
- Issue :
- 36
- Database :
- MEDLINE
- Journal :
- Journal of agricultural and food chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 30132665
- Full Text :
- https://doi.org/10.1021/acs.jafc.8b03327