Abstract
This research aimed to preserve the chitinase catalytic activity using alginate and zinc oxide nanoparticles (ZnO-NPs), to evaluate its thermal stability at 37 ºC, 50 ºC, and 70 ºC and its ability to detect Rhizopus stolonifer, Colletotrichum fragariae, and Alternaria alternata in a capacitive transducer-based biosensor. The ZnO-NPs measured less than 100 nm. The phosphate buffer-citric acid was a better solvent than water. Al+ZnONPs Ch showed the highest thermal stability at 37 ºC and 50 ºC (2 IU) for 45 d. Conversely, the free enzyme lost its activity from day 1–28 at 37 ºC (3.3 IU-2.8 IU), and alginate-encapsulated chitinase (AlCh) had the lowest activity at 50 ºC during 45 d (1.3 IU). Chitinase, alginate, and the ZnO-NPs were confirmed for FTIR spectra. The Al+ZnONPs Ch had the best response in the biosensor, observing a decrease in electrical frequency when the concentration of the tested fungi increased (106 spores mL−1 =100–250 kHz and 104 spores mL−1 = 400 kHz). In conclusion, at 37 ºC and 50 ºC, the chitinase had a stable catalytic activity compared to the remaining treatments, and it could be used to detect fungi in a biosensor at concentrations from 103 to 106 spores mL−1.
Published Version
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