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Total edentulism is the loss of all teeth for any cause by a multifactorial process that involves biological and patient-related factors. Studies on edentulism and risk factors in Mexico are limited, and the epidemiological surveillance data is scarce and controversial since official governmental reports are not statistically representative of the country. We estimate the distribution for edentulism according to sociodemographic and socioeconomic variables in adults from a low-income state in 2003 and its progress in Mexico. We analyzed data from the National Performance Evaluation Survey in Oaxaca, Mexico, and the annual reports of the Epidemiological Surveillance System of Oral Pathologies in 2009–2019 using X2. Oaxacan patients older than 75 y.o. (17.9%, p < 0.05), those with lower schooling (11.2%), and diabetes (14.5%) presented the highest percentage of edentulism. We do not observe differences in edentulism between sex or residence (p > 0.05). From 2009 to 2019, country data reports the lowest rate of edentulism in adults over 20 y.o. (0.32%; 95% CI 0.18–0.48%) and the most affected population over 79 y.o. (7.29%; 95% CI 5.2–9.30%). As it is a cumulative phenomenon, it is necessary to establish better surveillance, prevention, and treatment programs to improve the oral health of older thus reducing edentulism.

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.