Zamani Abbas, Khajavi Maryam, Abedian Kenari Abdolmohammad, Haghbin Nazarpak Masoumeh, Solouk Atefeh, Esmaeili Mina, Gisbert Enric
Fisheries Department, Faculty of Natural Resources and Environment, Malayer University, 4th km of Arak Road, Malayer 6574184621, Iran.
New Technologies Research Center, Amirkabir University of Technology, Tehran 1591634653, Iran.
Animals (Basel). 2023 Feb 26;13(5):853. doi: 10.3390/ani13050853.
This work aimed to determine the physicochemical and biochemical properties of trypsin from beluga and sevruga 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 °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 °C. TLCK and SBTI, two specific trypsin inhibitors, showed a significant inhibitory effect on the enzymatic activity of both trypsins ( < 0.05). The enzyme activity was significantly increased in the presence of Ca and surfactants and decreased by oxidizing agents, Cu, Zn, and Co ( < 0.05). However, univalent ions Na and K did not show any significant effect on the activity of both trypsins ( > 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.
这项工作旨在确定白鲸和闪光鲟这两种高价值鲟鱼物种中胰蛋白酶的物理化学和生化特性。根据酪蛋白酶谱法和抑制活性染色法获得的结果，闪光鲟和白鲸胰蛋白酶的分子量分别为27.5 kDa和29.5 kDa。两种胰蛋白酶的最佳pH值和温度值分别通过BAPNA（一种特异性底物）记录为8.5和55℃。两种胰蛋白酶在pH值6.0至11.0以及温度高达50℃时稳定性良好。两种特异性胰蛋白酶抑制剂TLCK和SBTI对两种胰蛋白酶的酶活性均显示出显著抑制作用（P<0.05）。在Ca和表面活性剂存在下酶活性显著增加，而在氧化剂、Cu、Zn和Co存在下酶活性降低（P<0.05）。然而，单价离子Na和K对两种胰蛋白酶的活性均未显示出任何显著影响（P>0.05）。我们的研究结果表明，白鲸和闪光鲟胰蛋白酶的特性与硬骨鱼中报道的数据一致，有助于清晰了解这些原始物种中胰蛋白酶的活性。
