Author/Authors :
Parfait Kouadio، Eugène Jean نويسنده Laboratoire de Biocatalyse et des Bioprocédés, Unité de Formation et de recherche des Sciences et Technologie des Aliments, Université Nangui Abrogoua , , Kouassi Konan، Hubert نويسنده Laboratoire de Biocatalyse et des Bioprocédés, Unité de Formation et de recherche des Sciences et Technologie des Aliments, Université Nangui Abrogoua , , Dabonné، Soumaïla نويسنده Laboratoire de Biocatalyse et des Bioprocédés, Unité de Formation et de recherche des Sciences et Technologie des Aliments, Université Nangui Abrogoua , , Ahipo Dué، Edmomd نويسنده Laboratoire de Biocatalyse et des Bioprocédés, Unité de Formation et de recherche des Sciences et Technologie des Aliments, Université Nangui Abrogoua , , Patrice Kouamé، Lucien Patrice Kouamé نويسنده Laboratoire de Biocatalyse et des Bioprocédés, Unité de Formation et de recherche des Sciences et Technologie des Aliments, Université Nangui Abrogoua ,
Abstract :
The thermal stability of ?-amylases Amy A1 and Amy A2 from digestive tract of tropical house cricket G. sigillatus was investigated by studying the effect of heat treatment over a range of 55 to 70 °C. Thermal inactivation of each enzyme, evaluated by loss in activity, was apparently followed by first-order kinetics with k-values comprised between 0.014–0.833 and 0.030–0.219 min-1 for Amy A1 and Amy A2, respectively. D and k-values decreased and increased, respectively, with increasing temperature, indicating faster inactivation of Amy A1 and A2 at higher temperatures. Ea and Z-values were estimated to 245.89 kJ/mol and 8.77 °C for Amy A1, 182.92 kJ/mol and 11.63 °C for Amy A2. Thermodynamic parameters were also calculated. All the results suggest that both ?-amylases are relatively resistant to long heat treatments up to 60 °C.
