Physicochemical and Biochemical Properties of Trypsin-like Enzyme from Two Sturgeon Species

Simple Summary Beluga and sevruga are two highly valuable sturgeon species from the Acipenseride family in Iran. In recent years, research has been focused on commercial rearing of these species. A very important aspect in the sturgeon farming industry is the development of formulated compound diets for promoting growth. However, the ability of fish to digest compound diets is mostly related to the existence of the digestive enzymes in different parts of the gastrointestinal tract. In gastric species, protein digestion is conducted along the gastrointestinal tract by several proteases such as pepsin, trypsin, and chymotrypsin. Trypsin, as an alkaline protease, is able to hydrolyze protein residues and peptides to release free amino acids and small peptides for intestinal absorption; therefore, the activity of trypsin has been widely used as a valuable indicator of digestive capacity in fish. In this work, we aimed to characterize trypsin from beluga and sevruga for the first time. The results of our study show that the physicochemical and biochemical properties of trypsin from beluga and sevruga were in agreement with data reported in bony fish and may be considered a preliminary step to design in vitro tests for the assessment of protein digestibility in these primitive species. This work aimed to determine the physicochemical and biochemical properties of trypsin from beluga Huso huso and sevruga Acipenser stellatus, two highly valuable sturgeon species. According to the results obtained from the methods of casein-zymogram and inhibitory activity staining, the molecular weight of trypsin for sevruga and beluga was 27.5 and 29.5 kDa, respectively. Optimum pH and temperature values for both trypsins were recorded at 8.5 and 55 degrees C by BAPNA (a specific substrate), respectively. The stability of both trypsins was well-preserved at pH values from 6.0 to 11.0 and temperatures up to 50 degrees C. TLCK and SBTI, two specific trypsin inhibitors, showed a significant inhibitory effect on the enzymatic activity of both trypsins (p < 0.05). The enzyme activity was significantly increased in the presence of Ca+2 and surfactants and decreased by oxidizing agents, Cu+2, Zn+2, and Co+2 (p < 0.05). However, univalent ions Na+ and K+ did not show any significant effect on the activity of both trypsins (p > 0.05). The results of our study show that the properties of trypsin from beluga and sevruga are in agreement with data reported in bony fish and can contribute to the clear understanding of trypsin activity in these primitive species.