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Revista Chapingo serie ciencias forestales y del ambiente
On-line version ISSN 2007-4018Print version ISSN 2007-3828
Abstract
VILLANUEVA-ALONZO, Hernán de J. et al. Proteolytic activity of wild fruits of Bromelia karatas L. of Yucatán, Mexico. Rev. Chapingo ser. cienc. for. ambient [online]. 2019, vol.25, n.2, pp.157-168. Epub Feb 19, 2021. ISSN 2007-4018. https://doi.org/10.5154/r.rchscfa.2018.08.062.
Introduction:
Bromeliads are a source of proteases that have not been fully studied.
Objectives:
To evaluate the proteolytic activity of wild fruits of Bromelia karatas L. under different temperature, pH and NaCl conditions, and to estimate the thermal stability of their proteases.
Materials and methods:
The effect of pH (6, 7, 8, 9, 10 and 12), incubation temperatures (30, 40, 50, 60 and 70 °C) and NaCl concentrations (5, 10 and 20 %) on the proteolytic activity of the fruits was compared. The thermal stability of the proteases was assessed at 30, 50 and 70 °C for 240 minutes. The molecular weights and isoelectric points of the proteases were estimated by non-reducing two-dimensional zymography. The data were analyzed using a one-factor ANOVA and Tukey's test (α = 0.05).
Results and discussion:
The proteolytic activity of B. karatas fruit extract (8.59 U·mg-1) was greater than that of Ananas comosus (L.) Merr. variety comosus (3.42 U·mg-1). The activity was higher at pH 6 and 7 and in concentrations lower than 5 % NaCl. Proteases were stable at 30 and 50 °C for 210 minutes. The two-dimensional zymogram, under non-reducing conditions, showed at least 40 light zones with apparent molecular weights between 27.3 and 290 kDa, potentially representing proteases.
Conclusion:
The proteases of B. karatas have potential for application in the food industry.
Keywords : Bromeliaceae; proteases; karatasin; 2D zymography.