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Molecules 2015, 20(10), 19372-19392; doi:10.3390/molecules201019372

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

1
Unidad de Bioquímica e Inmunología, Instituto Tecnológico de Oaxaca, Oaxaca 68030, Mexico
2
Centro de Investigación Medicina-UNAM-UABJO, Facultad de Medicina y Cirugía, Universidad Autónoma “Benito Juárez” de Oaxaca, Oaxaca 68050, Mexico
3
Facultad de Medicina de la, Universidad Nacional Autónoma de México, Distrito Federal 04510, Mexico
4
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)
View Full-Text   |   Download PDF [1250 KB, uploaded 23 October 2015]   |  

Abstract

β-Glucosidase (EC 3.2.1.21) 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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MDPI and ACS Style

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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