<b>Temperature and pH conditions for maximum activity of bromelain extracted from pineapple (<em>Ananas Comosus</em> L. Merril)</b> - doi: 10.4025/actascitechnol.v33i2.7928

Abstract

Bromelain, the enzyme found in pineapple, hydrolyzes proteins’ peptide bonds, has several applications in the food industry and in medicine. Temperature and pH conditions for highest activity with casein as substrate were investigated from the bromelain recovered from industrialized pineapple (‘pérola’ variety) fruit residues. Extract was obtained by grinding fruit rind and its internal stem. The activity was expressed in mmol tyrosine L^-1 min. ^-1 by absorbance at 280 nm of aromatic amino acids produced in casein hydrolysis. Assays were undertaken in duplicate for two enzyme/substrate with ratios: 1/25 and 1/125 (mass). Eight-pointed experimental design was undertaken with central value for pH at 7.0 and for temperature at 35°C. Experimental results were processed by MINITAB 15 (Minitab Inc) software which provided model’s equations and surface responses. Equations were mathematically processed by differential calculus producing graphs which exhibit the best activities according to temperatures. Loss of enzyme activity was reported with temperature increase at 1/25 ratio, due to a higher free enzyme, when compared to 1/125 ratio.