Enzymatic analyses demonstrate thermal adaptation of α-glucosidase activity in starch amended gully waste

• Published in: Bioresource technology Vol. 127; pp. 231 - 235
• Main Authors: Adams, J.D.W., Scott, K.M.
• Format: Journal Article
• Language: English
• Published: Kidlington Elsevier Ltd 01.01.2013; Elsevier
• Subjects: Adaptation; alpha-Glucosidases - metabolism; Analysis of Variance; Applied sciences; Biological and medical sciences; Degradation; Design engineering; Drying; Enzymes; Exact sciences and technology; Extra-cellular enzyme analysis; Fundamental and applied biological sciences. Psychology; Gullies; Mesophilic; organic wastes; Pollution; Selection; starch; Starch - metabolism; Starches; Temperature; thermal analysis; Thermophilic; Waste Management - methods; Waste Products - analysis; Wastes; Mesophilic; Thermophilic; Extra-cellular enzyme analysis; Selection; Starch; Enzyme; Thermophily; Extracellular; Glycosylases; α-Glucosidase; Glycosidases; Mesophily; Hydrolases; Wastes; Adaptation
• ISSN: 0960-8524; 1873-2976
• DOI: 10.1016/j.biortech.2012.09.052

► Starch degradation was confirmed as temperature independent. ► α-glucosidase responded positively to starch addition. ► Evidence for α-glucosidase adaptation to in situ temperature. 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.