ارزیابی فعالیت آنزیم‌ تریپسین استخراج شده از ضمائم پیلوریک و روده تاسماهی سیبری (Acipenser baerii) تحت تأثیر برخی عوامل فیزیکی و شیمیایی

Abita, J.P., Delaage, M., Lazdunski, M., Savrda, J. 1969. The mechanism of activation of trypsinogen: The role of the four N-Terminal aspartyl residues. European Journal of Biochemistry 8: 314-324. DOI: 10.1111/j.1432-1033.1969.tb00530.x

Asgari, R., Rafiee, G., Eagderi, S., Noori, F., Agh, N., Poorbagher, H., Gisbert, E. 2013. Ontogeny of the digestive enzyme activities in hatchery produced Beluga (Huso huso). Aquaculture 416: 33-40.  DOI: 10.1016/j.aquaculture.2013.08.014

Balti, R., Bougherra, F., Bougatef, A., Hayet, B.K., Nedjar-Arroume, N., Dhulster, P., Guillochon, D., Nasri, M. 2012. Chymotrypsin from the hepatopancreas of cuttlefish (Sepia officinalis) with high activity in the hydrolysis of long chain peptide substrates: Purification and biochemical characterisation. Food Chemistry 130: 475-484. DOI: 10.1016/j.foodchem.2011.07.019

Bolasina, S., Pérez, A.,Yamashita, Y. 2006. Digestive enzymes activity during ontogenetic development and effect of starvation in Japanese flounder, Paralichthys olivaceus. Aquaculture 252: 503-515. DOI: 10.1016/j.aquaculture.2005.07.015

Camacho, S., Carmona, R., Llorente, J.I., Sanz, A., García‐Gallego, M., Domezain, A., Dominguez, N., Ostos‐Garrido, M.V. 2011. Stomach development in the sturgeon Acipenser naccarii: Histoenzymatic and ultrastructural analysis. Journal of Applied Ichthyology 27: 693-700. DOI: 10.1111/j.1439-0426.2010.01581.x

Candiotto, F.B., Freitas-Júnior, A.C.V., Neri, R.C.A., Bezerra, R.S., Rodrigues, R.V., Sampaio, L.A., Tesser, M.B. 2017. Characterization of digestive enzymes from captive Brazilian flounder Paralichthys orbignyanus. Brazilian Journal of Biology 78: 281-288. DOI: 10.1590/ 1519-6984.06616

de Freitas-Júnior, A.C.V., da Costa, H.M.S., Marcuschi, M., Icimoto, M.Y., Machado, M.F., Machado, M.F., Ferreira, J.C., de Oliveira, V.M., Buarque, D.S., Bezerra, R.S. 2021. Substrate specificity, physicochemical and kinetic properties of a trypsin from the giant Amazonian fish pirarucu (Arapaima gigas). Biocatalysis and Agricultural Biotechnology 35: 102073. DOI: 10.1016/j.bcab. 2021.102073

Dos Santos, C.W.V., da Costa Marques, M.E., de Araújo Tenório, H., de Miranda, E.C., Pereira, H.J.V. 2016. Purification and characterization of trypsin from Luphiosilurus alexandri pyloric cecum. Biochemistry and biophysics reports 8: 29-33. DOI: 10.1016/j.bbrep.2016.08.003

dos Santos, D.M.R.C., dos Santos, C.W.V., de Souza, C.B., de Albuquerque, F.S., dos Santos Oliveira, J.M., Pereira, H.J.V. 2020. Trypsin purified from Coryphaena hippurus (common dolphinfish): Purification, characterization, and application in commercial detergents. Biocatalysis and Agricultural Biotechnology 25: 101584. DOI: 10.1016/j.bcab.2020.101584

Erlanger, B.F., Kokowsky, N., Cohen, W. 1961. The preparation and properties of two new chromogenic substrates of trypsin. Archives of Biochemistry and Biophysics 95: 271-278. DOI: 10.1016/0003-9861(61)90145-X

Eun-Sil, O., Jae-Hyeung, P., Deuk-Moon, C., Chang-Bum, A. 1998. Comparative biochemical properties of proteinases from the hepatopancreas of shrimp. I. Purification of protease from the hepatopancreas of Penaeus japonicus. Fisheries and Aquatic Sciences 1: 201-208.

Garcia-Carreno, F.L., Dimes, L.E., Haard, N.F. 1993. Substrate-gel electrophoresis for composition and molecular weight of proteinases or proteinaceous proteinase inhibitors. Analytical Biochemistry 214: 65-69. DOI: 10.1006/abio.1993.1457

Ghasemi, N., Imani, A., Noori, F., Shahrooz, R. 2020. Ontogeny of digestive tract of stellate sturgeon (Acipenser stellatus) from hatching to juvenile stage: Digestive enzymes activity, stomach and proximal intestine. Aquaculture 519: 734751. DOI: 10.1016/j.aquaculture.2019.734751

Ghorbani Vaghei, R., Mohseni, M., Alipour, A., Pajand, Z., Hosseinnia, E. 2022. An overview of sturgeon culture in concrete tanks, recirculating aquaculture system, cage and earthen pond. Sturgeon Extension Journal 5: 1-12.

Gilannejad, N., Martínez-Rodríguez, G., Yúfera, M., Moyano, F.J. 2017. Estimating the effect of different factors on the digestive bioaccessibility of protein by the Senegalese sole (Solea senegalensis); combination of response surface methodology and in vitro assays. Aquaculture 477: 28-34. DOI: 10.1016/j.aquaculture.2017.04.037

Glusker, J.P., Katz, A.K., Bock, C.W. 2001. Two-metal binding motifs in protein crystal structures. Structural Chemistry 12: 323-341. DOI: 10.1023/A:1016636712985

Green, M.M., Gladner, J.A., Cunningham Jr,L.W., Neurath, H., 1952. The effects of divalent cations on the enzymatic activities of trypsin and of α-chymotrypsin1. Journal of the American Chemical Society 74: 2122-2123. DOI: 10.1021/ja01128a523

Iranian Fisheries Organization. 2024. Annual report. Ghorbanzade, R.A., Nazari, S. (editors). Available online: http://www.fisheries.ir/site/vahed_with_shakhes_v.aspx?uc=18.

Jellouli, K., Bougatef, A., Daassi, D., Balti, R., Barkia, A., Nasri, M., 2009. New alkaline trypsin from the intestine of grey triggerfish (Balistes capriscus) with high activity at low temperature: purification and characterization. Food Chemistry 116: 644-650. DOI: 10.1016/j.foodchem.2009.02. 087

Khangembam, B.K., Chakrabarti, R. 2015. Trypsin from the digestive system of carp Cirrhinus mrigala: purification, characterization and its potential application. Food chemistry 175: 386-394. DOI: 10.1016/j.foodchem.2014.11.140

Khantaphant, S., Benjakul, S. 2010. Purification and characterization of trypsin from the pyloric caeca of brownstripe red snapper (Lutjanus vitta). Food Chemistry 120: 658-664. DOI: 10.1016/ j.foodchem.2009.09.098

Klomklao, S., Benjakul, S. 2018. Two trypsin isoforms from albacore tuna (Thunnus alalunga) liver: Purification and physicochemical and biochemical characterization. International Journal of Biological Macromolecules 107: 1864-1870. DOI: 10.1016/j.ijbiomac.2017.10.059

Kolkovski, S. 2001. Digestive enzymes in fish larvae and juveniles-implications and applications to formulated diets. Aquaculture 200: 181-201. DOI: 10.1016/S0044-8486(01)00700-1

Ktari, N., Khaled, H.B., Nasri, R., Jellouli, K., Ghorbel, S., Nasri, M. 2012. Trypsin from zebra blenny (Salaria basilisca) viscera: Purification, characterisation and potential application as a detergent additive. Food Chemistry 130: 467-474. DOI: 10.1016/j.foodchem.2011.07.015

Liu, Z.Y., Wang, Z., Xu, S.Y., Xu, L.N., 2007. Two trypsin isoforms from the intestine of the grass carp (Ctenopharyngodon idellus). Journal of Comparative Physiology 177B: 655-666. DOI: 10.1007/s00360-007-0163-6

Lowry, O., Rosebrough, N., Farr, A.L., Randall, R. 1951. Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193: 265-275.

Lu, B.J., Zhou, L.G., Cai, Q.F., Hara, K., Maeda, A., Su, W.J., Cao, M.J. 2008. Purification and characterization of trypsins from the pyloric caeca of mandarin fish (Siniperca chuatsi). Food Chemistry 110: 352-360. DOI: 10.1016/j.foodchem.2008.02.010

Nazdar, N., Imani, A., Noori, F., Sarvi Moghanlou, K. 2018. Effect of silymarin supplementation on nickel oxide nanoparticle toxicity to rainbow trout (Oncorhynchus mykiss) fingerlings: Pancreas tissue histopathology and alkaline protease activity. Iranian Journal of Science and Technology, Transactions A: Science 42: 353-361. DOI: 10.1007/s40995-016-0052-5

Nolasco‐Soria, H. 2021. Improving and standardizing protocols for alkaline protease quantification in fish. Reviews in Aquaculture 13: 43-65. DOI: 10.1111/raq.12463

Ostaszewska, T., Kolman, R., Kamaszewski, M., Wiszniewski, G., Adamek, D., Duda, A. 2011. Morphological changes in digestive tract of Atlantic sturgeon Acipenser oxyrinchus during organogenesis. International Aquatic Research 3: 101-105.

Patil, U., Baloch, K.A., Nile, S.H., Kim, J.T., Benjakul, S. 2023. Trypsin from pyloric caeca of Asian seabass: Purification, characterization, and its use in the hydrolysis of acid-soluble collagen. Foods 12: 2937. DOI: 10.3390/foods12152937

Rungruangsak-Torrissen, K., Moss, R., Andresen, L.H., Berg, A., Waagbø, R. 2006. Different expressions of trypsin and chymotrypsin in relation to growth in Atlantic salmon (Salmo salar L.). Fish physiology and Biochemistry 32: 7-23. DOI: 10.1007/s10695-005-0630-5

Rungruangsak‐Torrissen, K.R.I.S.N.A. 2007. Digestive efficiency, growth and qualities of muscle and oocyte in Atlantic salmon (Salmo salar L.) fed on diets with krill meal as an alternative protein source. Journal of Food Biochemistry 31: 509-540. DOI: 10.1111/j.1745-4514.2007.00127.x

Senphan, T., Benjakul, S., Kishimura, H. 2015. Purification and Characterization of Trypsin from Hepatopancreas of Pacific White Shrimp. Journal of Food Biochemistry 39: 388-397. DOI: 10.1111/jfbc.12147

Silva, J.F., Espósito, T.S., Marcuschi, M., Ribeiro, K., Cavalli, R.O., Oliveira, V., Bezerra, R.S. 2011. Purification and partial characterization of a trypsin from the processing waste of the silver mojarra (Diapterus rhombeus). Food Chemistry 129: 777-782. DOI: 10.1016/j.foodchem. 2011.05.019

Simpson, B.K. 2000. Digestive proteinases from marine animals. In: Seafood Enzymes: Utilization and Influence on Postharvest Seafood Quality; Haard, N.F., Simpson, B.K. (Eds.). Marcel Dekker: New York, NY, USA, 531-540.

Yúfera, M., Darias, M.J. 2007. The onset of exogenous feeding in marine fish larvae. Aquaculture 268: 53-63. DOI: 10.1016/j.aquaculture.2007.04.050

Zamani, A., Benjakul, S. 2016. Trypsin from unicorn leatherjacket (Aluterus monoceros) pyloric caeca: purification and its use for preparation of fish protein hydrolysate with antioxidative activity. Journal of the Science of Food and Agriculture 96: 962-969. DOI: 10.1002/jsfa.7172

Zamani, A., Khajavi, M., Abedian Kenari, A., Haghbin Nazarpak, M., Solouk, A., Esmaeili, M., Gisbert, E. 2023. Physicochemical and biochemical properties of trypsin-like enzyme from two sturgeon species. Animals 13: 853. DOI: 10.3390/ani13050853

Zamani, A., Rezaei, M., Madani, R., Habibi Rezaie, M. 2014. Trypsin enzyme from viscera of common kilka (Clupeonella cultriventris caspia): purification, characterization, and its compatibility with oxidants and surfactants. Journal of Aquatic Food Product Technology 23: 237-252. DOI: 10.1080/10498850.2012.712630