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Molecules 2015, 20(10), 19372-19392;

Purification and Partial Characterization of β-Glucosidase in Chayote (Sechium edule)

Unidad de Bioquímica e Inmunología, Instituto Tecnológico de Oaxaca, Oaxaca 68030, Mexico
Centro de Investigación Medicina-UNAM-UABJO, Facultad de Medicina y Cirugía, Universidad Autónoma “Benito Juárez” de Oaxaca, Oaxaca 68050, Mexico
Facultad de Medicina de la, Universidad Nacional Autónoma de México, Distrito Federal 04510, Mexico
Unité Mixte de Recherche CNRS/USTL 8576, Glycobiologie Structurale et Fonctionnelle, Université des Sciences et Technologies de Lille 1, Villeneuve d’Ascq 59655, France
Author to whom correspondence should be addressed.
Academic Editor: Thomas J. Schmidt
Received: 17 August 2015 / Revised: 7 October 2015 / Accepted: 10 October 2015 / Published: 23 October 2015
(This article belongs to the Section Natural Products Chemistry)
Full-Text   |   PDF [1250 KB, uploaded 23 October 2015]   |  


β-Glucosidase (EC is a prominent member of the GH1 family of glycoside hydrolases. The properties of this β-glucosidase appear to include resistance to temperature, urea, and iodoacetamide, and it is activated by 2-ME, similar to other members. β-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 β-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 β-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 β-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 β-D-glucose inhibited β-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. View Full-Text
Keywords: β-glucosidase; Cucurbitaceae; Sechium edule; glycosyl hydrolases β-glucosidase; Cucurbitaceae; Sechium edule; glycosyl hydrolases

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Mateos, S.E.; Cervantes, C.A.M.; Zenteno, E.; Slomianny, M.-C.; Alpuche, J.; Hernández-Cruz, P.; Martínez-Cruz, R.; Canseco, M.S.P.; Pérez-Campos, E.; Rubio, M.S.; Mayoral, L.P.-C.; Martínez-Cruz, M. Purification and Partial Characterization of β-Glucosidase in Chayote (Sechium edule). Molecules 2015, 20, 19372-19392.

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