ABSTRACT
Death anxiety has been linked to several psychopathological conditions. However, the causes, comorbidity, and differential diagnosis of death anxiety is unexplored. This paper stands out by identifying common predictors of death anxiety and exploring the potential of death anxiety as a predictor for other psychological conditions. The paper reports the findings of four consecutive studies that involved a total of 2291 conveniently selected participants including 861 men and 1430 women. We focused on clarifying both the predictors of death anxiety and the psychopathological consequences emerging from it. Our findings established depression, anxiety, stress, fear of aging, and reduced life satisfaction as predictors of death anxiety. Psychosocial illness, sleep disturbances, aggression, and daily hassles were established as the adverse outcomes of death anxiety. Fear of aging was the most significant predictor of death anxiety and daily hassles emerged as the most significant adverse consequence of death anxiety.
ABSTRACT
1,4-alpha-D-glucan glucanohydrolase is among the most widely used commercial hydrolytic enzymes acting randomly on the glycosidic linkages of starch resulting in its saccharification and liquefaction. Its applicability in different industries can be improved by enhancing its stability and reusability. Therefore, in the present study attempts have been made to enhance the industrial applicability of 1,4-alpha-D-glucan glucanohydrolase from Bacillus subtilis KIBGE-HAR by adapting immobilization technology. The study developed mechanically stable, enzyme containing gel-frameworks using two support matrices including agar-agar, a natural polysaccharide and polyacrylamide gel, a synthetic organic polymer. These catalytic gel-scaffolds were compared with each other in terms of kinetics and stability of entrapped 1,4-α-D-glucan glucanohydrolase. In case of polyacrylamide gel, Km value for immobilized enzyme increased to 7.95 mg/mL, while immobilization in agar-agar resulted in decreased Km value i.e 0.277 mg/mL as compared to free enzyme. It was found that immobilized enzyme showed maximum activity at 70 °C in both the supports as compared to free enzyme having maximum activity at 60 °C. Immobilized 1,4-α-D-glucan glucanohydrolase exhibited no change in optimal pH 7.0 before and after entrapment in polyacrylamide gel and agar-agar. The enzyme containing gel-scaffold was found suitable for repeated batches of starch liquefaction in industrial processes. Agar-agar entrapped 1,4-α-D-glucanglucanohydrolase was capable to degrade starch up to seven repeated operational cycles whereas polyacrylamide entrapped enzyme conserved its activity up to sixth operational cycle.