Characteristics of Trypsin Isolated From Intestines Different of Fish and Correlation Toward Trypsin Activity

Abstract

Trypsin is a protease that breaks protein peptide bonds. Fish intestines can be used as an alternative raw material for trypsin. Trypsin enzymes from the intestines of different fish species have different characteristics. This study aimed to determine the characteristics and stability of trypsin enzyme in NaCl extracted from fish intestines based on differences in fish species. Trypsin activity was optimal at 50 °C and pH 8, with specific activity values of 0.5993 U/mg in rabbitfish, 0.3880 U/mg in sharks, and 0.6964 U/mg in flatfish. The maximum reaction speed (Vmax) was the highest for trypsin from the intestine of rabbitfish (0.2585 mmol/s), followed by flatfish (0.1042 mmol/s), and shark (0.0599 mmol/s). The lowest Km value was obtained for trypsin from sharks (0.4084 mM), followed by flatfish (1.0253 mM), and rabbitfish (4.5952 mM). Trypsin from the intestines of rabbitfish and flatfish was stable in NaCl solution (concentration 5-30%), as it can maintain a relative activity of more than 50%. In contrast, trypsin extracted from the intestines of milk fish had a relative activity below 21%. The average molecular weights of the three trypsin enzymes were 26.8, 27.2; and 21.9 kDa, respectively. Differences in the type of fish affected trypsin enzyme activity. Flatfish are omnivorous, and rabbitfish, as herbivores, have better enzyme activity values than sharks, as carnivores.

Keywords

• flatfish
• shark
• nacl stability
• rabbitfish
• trypsin enzyme characteristics