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Molecules ; 20(10): 19372-92, 2015 Oct 23.
Article in English | MEDLINE | ID: mdl-26512637

ABSTRACT

ß-Glucosidase (EC 3.2.1.21) is a prominent member of the GH1 family of glycoside hydrolases. The properties of this ß-glucosidase appear to include resistance to temperature, urea, and iodoacetamide, and it is activated by 2-ME, similar to other members. ß-Glucosidase from chayote (Sechium edule) was purified by ionic-interchange chromatography and molecular exclusion chromatography. Peptides detected by LC-ESI-MS/MS were compared with other ß-glucosidases using the BLAST program. This enzyme is a 116 kDa protein composed of two sub-units of 58 kDa and shows homology with Cucumis sativus ß-glucosidase (NCBI reference sequence XP_004154617.1), in which seven peptides were found with relative masses ranging from 874.3643 to 1587.8297. The stability of ß-glucosidase depends on an initial concentration of 0.2 mg/mL of protein at pH 5.0 which decreases by 33% in a period of 30 h, and then stabilizes and is active for the next 5 days (pH 4.0 gives similar results). One hundred µg/mL ß-D-glucose inhibited ß-glucosidase activity by more than 50%. The enzyme had a Km of 4.88 mM with p-NPG and a Kcat of 10,000 min(-1). The optimal conditions for the enzyme require a pH of 4.0 and a temperature of 50 °C.


Subject(s)
Cucurbitaceae/enzymology , beta-Glucosidase/isolation & purification , Amino Acid Sequence , Chemical Precipitation , Chromatography, Ion Exchange , Enzyme Stability , Glucose/chemistry , Hydrogen-Ion Concentration , Kinetics , Molecular Sequence Data , Plant Proteins , Sequence Homology, Amino Acid , Substrate Specificity , beta-Glucosidase/chemistry
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