| Autor: |
Mateos SE; Unidad de Bioquímica e Inmunología, Instituto Tecnológico de Oaxaca, Oaxaca 68030, Mexico. sespindolam@hotmail.com., Cervantes CA; Unidad de Bioquímica e Inmunología, Instituto Tecnológico de Oaxaca, Oaxaca 68030, Mexico. carloscervantes.ox@outlook.com., Zenteno E; Facultad de Medicina de la, Universidad Nacional Autónoma de México, Distrito Federal 04510, Mexico. ezenteno@servidor.unam.mx., Slomianny MC; Unité Mixte de Recherche CNRS/USTL 8576, Glycobiologie Structurale et Fonctionnelle, Université des Sciences et Technologies de Lille 1, Villeneuve d'Ascq 59655, France. Marie-Christine.Slomianny@univ-lille1.fr., Alpuche J; Centro de Investigación Medicina-UNAM-UABJO, Facultad de Medicina y Cirugía, Universidad Autónoma 'Benito Juárez' de Oaxaca, Oaxaca 68050, Mexico. juan_alpuche@hotmail.com., Hernández-Cruz P; Centro de Investigación Medicina-UNAM-UABJO, Facultad de Medicina y Cirugía, Universidad Autónoma 'Benito Juárez' de Oaxaca, Oaxaca 68050, Mexico. fuegoblanco68@yahoo.com.mx., Martínez-Cruz R; Centro de Investigación Medicina-UNAM-UABJO, Facultad de Medicina y Cirugía, Universidad Autónoma 'Benito Juárez' de Oaxaca, Oaxaca 68050, Mexico. rmc.azul@gmail.com., del Socorro Pina Canseco M; Centro de Investigación Medicina-UNAM-UABJO, Facultad de Medicina y Cirugía, Universidad Autónoma 'Benito Juárez' de Oaxaca, Oaxaca 68050, Mexico. socopina12@hotmail.com., Pérez-Campos E; Unidad de Bioquímica e Inmunología, Instituto Tecnológico de Oaxaca, Oaxaca 68030, Mexico. perezcampos123@yahoo.es.; Centro de Investigación Medicina-UNAM-UABJO, Facultad de Medicina y Cirugía, Universidad Autónoma 'Benito Juárez' de Oaxaca, Oaxaca 68050, Mexico. perezcampos123@yahoo.es., Rubio MS; Unidad de Bioquímica e Inmunología, Instituto Tecnológico de Oaxaca, Oaxaca 68030, Mexico. jmsanchezrubio@gmail.com., Mayoral LP; Centro de Investigación Medicina-UNAM-UABJO, Facultad de Medicina y Cirugía, Universidad Autónoma 'Benito Juárez' de Oaxaca, Oaxaca 68050, Mexico. laurapcm@prodigy.net.mx., Martínez-Cruz M; Unidad de Bioquímica e Inmunología, Instituto Tecnológico de Oaxaca, Oaxaca 68030, Mexico. martinezcu9@hotmail.com. |
| Abstrakt: |
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. |
