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Updated: May 17, 2026

Elucidating β-1,3-Glucanase and Peroxidase Physicochemical Properties of Wheat Cell Wall Defense Mechanism Against Diuraphis noxia Infestation
Published on: July 26, 2024
Enzymatic analyses demonstrate thermal adaptation of α-glucosidase activity in starch amended gully waste
1Environmental Technologies Centre for Industrial Collaboration, University of Hull, Hull HU6 7RX, UK. j.d.adams@hull.ac.uk
Abstract:
In this study we investigated the effect of starch amendment on α-glucosidase activity in an organic waste environment, treated under both mesophilic and thermophilic conditions. The relative effects of temperature on α-glucosidase activity with regard to in situ and assay conditions were investigated under a reciprocal design. The decline in dry matter under the different thermal regimes was consistent with the temperature independent degradation of starch. The results of extra-cellular enzyme analysis showed a significant relationship between starch addition and α-glucosidase activity, with evidence of thermal adaptation to the in situ temperature. A weaker, but significant, effect of starch addition on β-glucosidase activity was observed, with no evidence for thermal adaptation. Thus, our data is consistent with a substrate adaptive response to temperature, albeit under potentially a high selective pressure.

