Abstract
Chitinases are important protective enzymes in plants and belong to a special group of pathogenesisrelated (PR) proteins. The main target of these enzymes is various pathogenic fungi that contain chitin
in their cell walls. Under the influence of fungi, chitinases produced by plants, hydrolyze chitin, which
leads to suppression of the growth and death of the pathogen. Considering their important protective
role, much attention is paid to the studies of these enzymes. Individual isozymes of chitinase are often
used in testing and breeding agricultural plants for resistance to fungal diseases. In this work, we studied
the isoenzyme composition and a number of physicochemical properties of wheat chitinases, which are
important for a better understanding of their functioning in this grain crop. It was found that in seedlings
of 7 days old, chitinases are localized both inside and outside the cells. Intracellular chitinase is
represented only by basic components, whereas extracellular - by acidic ones. Using an affinity sorbent,
the forms of the enzyme with a chitin-binding domain (CBD) were determined, which had isoelectric
points (pI) of 9.3, 9.0, 8.6, 8.2, 8.0, 7.6, 5.7 and 4.6. According to SDS-PAG electrophoresis, the
molecular weight (M.w.) of these enzymes corresponded to the values of 33, 35 and 56 kDa and they
were not the glycoproteins. In the spectrum of isoelectric focusing (IEF) of chitinases, exochitinases
were identified, which had pI values exclusively in the acidic range of 4.3-5.2. Significant differences
were revealed in the thermal stability of chitinases. The acidic components were most resistant to
elevated temperatures.
Aidar Khakimzhanov, Vladimir Kuzovlev, Aset Abaildayev. (2021) Chitinases of wheat seedling and their biochemical properties, Asian Journal of Agriculture and Biology, Volume-09, Issue-2.
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