Biochemical characterization of fish trypsin enzyme from the larva stadia of Anguilla bicolor as potential candidates of microorganism culturing catalystians for vaccines Available to Purchase

Trypsin enzyme is one type of alkaline protease widely used in various fields, one of which is the manufacture of microorganism culture media for vaccines. The pig trypsin enzyme (porcine-derived trypsin) is still a catalyst commonly used in production. Fish trypsin can be an alternative enzyme because fish resources are abundant in Indonesia but are still minimally utilized in health. One type of fish with a very high protein content is Anguilla bicolor. This study aims to characterize the fish trypsin enzyme from Anguilla bicolor as a potential candidate for vaccine-catalytic microorganism culture. The method used in this study is an experimental study using a completely randomized design (CRD) with 6 types of treatment in the form of temperature differences and repeated four times. The treatment was given to stadia elver/larvae of Anguilla bicolor. This research was conducted through three stages: preparation, and morphometric measurements, then enzyme extraction and enzyme characterization, including measurement of fish trypsin activity and protein content. The results of Body Morphometric Character Measurement (mm) of the Larva Stadia of Anguilla bicolor have values for total length (114.5±6.251 mm), head length (8.34±0.953 mm), head width (2.48±0.582 mm), head height (1.97±0.217 mm), snout length (1.1±0.067 mm), eye diameter (0.48±0.105 mm), eye distance (0.94±0.101 mm), body height (2.3±0.032 mm), body width (4.3±0.054 mm), and body weight (131.5±0.472 mg). Meanwhile, the results of intestinal morphometric measurements showed that the larvae of Anguilla bicolor stadia had an intestinal weight (290±1,223 mg), intestinal length (27,7±7,19 mm), and intestine width (10±0,012 mm). The protein content of the trypsin enzyme extract of the larval stage of Anguilla bicolor was 0893±0,106 g/dL. Meanwhile, the highest total activity and trypsin enzyme activity were obtained at 40°C incubation temperatures of 0.541±0.007 U and 0.212±0.003 U/mL.