Molecular weights and optimum temperature and pH for pepsin activity of three sciaenid finfish species from the Gulf of California

Authors

  • Martin Perez-Velazquez Department of Scientific and Technological Research, University of Sonora, Bldg. 7-G, Blvd. Luis Donaldo Colosio s/n, Col. Centro, C.P. 83000, Hermosillo, Sonora, Mexico https://orcid.org/0000-0002-9019-1220
  • Carlos A. Maldonado-Othón Department of Scientific and Technological Research, University of Sonora, Bldg. 7-G, Blvd. Luis Donaldo Colosio s/n, Col. Centro, C.P. 83000, Hermosillo, Sonora, Mexico https://orcid.org/0000-0002-6771-5997
  • Mayra L. González-Félix Department of Scientific and Technological Research, University of Sonora, Bldg. 7-G, Blvd. Luis Donaldo Colosio s/n, Col. Centro, C.P. 83000, Hermosillo, Sonora, Mexico http://orcid.org/0000-0003-1886-4096

DOI:

https://doi.org/10.2298/ABS240104004P

Keywords:

pepsin, enzymatic activity, sciaenids, Cynoscion othonopterus, C. xanthulus, C. parvipinnis

Abstract

Paper description:

  • Byproducts from the processing of finfish from fisheries and aquaculture are often discarded. However, the enzymatic content of viscera has potential biotechnological and industrial applications.
  • The molecular weights and optimum temperature and pH for pepsin activity from the sciaenids Cynoscion othonopterus, Cynoscion xanthulus, and Cynoscion parvipinnis were determined.
  • Pepsins from the three species compare closely with pepsins from other fish in terms of molecular weight, with some variations in temperature and pH optima.
  • Pepsins from othonopterus, C. xanthulus, and C. parvipinnis may have similar applications as other fish pepsins.

Abstract: By-products from finfish processing from fisheries and aquaculture are often discarded. However, the enzymatic content of viscera has potential biotechnological and industrial applications. Such is the case for the sciaenids Cynoscion othonopterus, Cynoscion xanthulus, and Cynoscion parvipinnis, which are food and game fishes from the Gulf of California and whose viscera are commonly discarded after fish dressing. In this study, optimum temperature and pH for activity, as well as molecular weights of pepsin from the stomach of C. othonopterus, C. xanthulus, and C. parvipinnis were evaluated for the first time. Pepsin molecular weights were 30, 32.1, and 32.3 kDa, respectively. The highest activity of pepsin against hemoglobin was recorded between 40 and 45ºC for C. othonopterus and C. xanthulus and at 40°C for C. parvipinnis. The optimum pH was 2.0 for the three sciaenids. Biochemical characteristics were comparable to pepsins from other marine and freshwater fish species, so they could likely be used in some processes using this enzyme, like collagen extraction, fish silage production, or fish processing, among others.

Downloads

Download data is not yet available.

References

Food and Agricultural Organization (FAO). The State of World Fisheries and Aquaculture 2022. Towards Blue Transformation. Rome, FAO. 2022; https://doi.org/10.4060/cc0461en

Klomklao S. Digestive proteinases from marine organisms and their applications. Songklanakarin J Sci Technol. 2008;30:37-46.

Zhao L, Budge SM, Ghaly A, Brooks MS, Dave D. Extraction, purification and characterization of fish pepsin: a critical review. J Food Process Technol. 2011;2(6):1-14. https://doi.org/10.4172/2157-7110.1000126

Raufman J. Encyclopedia of Gastroenterology. 3rd ed. Amsterdam: Academic Press; 2004. Chapter 2, Pepsin; p. 147-8. https://doi.org/10.1016/B0-12-386860-2/00561-X

Fänge R, Grove D. Digestion. In: Fish Physiology, Hoar WS, Randall DJ, Brett JR (Eds.), Academic Press, New York, 1979;161-260. https://doi.org/10.1016/S1546-5098(08)60027-8

Shahidi F, Kamil YVA. Enzymes from fish and aquatic invertebrates and their application in the food industry. Trends Food Sci Technol. 2001;12:435-64. https://doi.org/10.1016/S0924-2244(02)00021-3

Nalinanon S, Benjakul S, Kishimura H. Biochemical properties of pepsinogen and pepsin from the stomach of albacore tuna (Thunnus alalunga). Food Chem. 2010;21:49-55. https://doi.org/10.1016/j.foodchem.2009.11.089

Zhou Q, Fu XP, Zhang LJ, Su WJ, Cao MJ. Purification and characterization of sea bream (Sparus latus Houttuyn) pepsinogens and pepsins. Food Chem. 2007;103:795-801. https://doi.org/10.1016/j.foodchem.2006.09.021

Dimes LE, Haard NF. Estimation of protein digestibility-I. Development of an in vitro method for estimating protein digestibility in salmonids. Comp Biochem Physiol A. 1994;108:349-62. https://doi.org/10.1016/0300-9629(94)90106-6

Rust MB. Nutritional physiology. In: Hardy RW, editor. Fish Nutrition. 3rd ed. Amsterdam: Academic Press; 2002. p. 367-452. https://doi.org/10.1016/B978-012319652-1/50008-2

Nalinanon S, Benjakul S, Visessanguan W, Kishimura H. Use of pepsin for collagen extraction from the skin of bigeye snapper (Priccanthus tayenus). Food Chem. 2007;104:593-601. https://doi.org/10.1016/j.foodchem.2006.12.035

Oliveira VM, Bezerra RS, Assis CRD. Fish pepsin: basic characteristics, extraction, determination and biotechnological applications. Nat. Resour. 2014;4:6-14. https://doi.org/10.6008/SPC2237-9290.2014.001.0001

Gildberg A. Enzymes and bioactive peptides from fish waste related to fish silage, fish feed and fish sauce production. J Aquat Food Prod Technol. 2004a;13:3-11. https://doi.org/10.1300/J030v13n02_02

Goddard JS, Al-Yahyai DSS. Chemical and nutritional characteristics of dried sardine silage. J Aquat Food Prod Technol. 2001;10:39-50. https://doi.org/10.1300/J030v10n04_04

Raa J, Gildberg A. Fish silage: A review. Crit Rev Food Sci Nutr. 1982;16:383-419. https://doi.org/10.1080/10408398209527341

Gildberg A. Digestive enzyme activities in starved pre-slaughter farmed and wild-captured, Atlantic cod (Gadus morhua). Aquaculture 2004b;238:343-353. https://doi.org/10.1016/j.aquaculture.2004.03.021

Almås KA. Utilization of marine biomass for production of microbial growth media and biochemical. In: Voigt MN, Botta JR, editors. 34th Atlantic Fisheries Technological Conference and Seafood Biotechnology Workshop: Advances in Fisheries Technology and Biotechnology for increased profitability; 1989 Aug 27 - Sep 1; St. John's,NF, Canada. Lancaster: Technomic Pub. Co.; 1990. p. 361-72.

Gorgas FJS. Dental medicine. A manual of dental material medica and therapeutics. Washington: Nabu Press; 2012; 682 p.

Murado MA, González MDP, Vázquez JA. Recovery of proteolytic and collagenolytic activities from viscera by-products of rayfish (Raja clavata). Mar Drugs. 2009;7:803-15. https://doi.org/10.3390/md7040803

Villanueva-Gutiérrez E, Maldonado-Othón CA, Perez-Velazquez M, González-Félix ML. Activity and partial characterization of trypsin, chymotrypsin, and lipase in the digestive tract of Totoaba macdonaldi. J Aquat Food Prod Technol. 2020;29:322-34. https://doi.org/10.1080/10498850.2020.1733157

González-Félix ML, De La Reé-Rodríguez C, Perez-Velazquez M. Optimum Activity and Partial Characterization of Chymotrypsin from the Sciaenids Cynoscion othonopterus, Cynoscion parvipinnis, and Cynoscion xanthulus. J Aquat Food Prod Technol. 2021;30:670-82. https://doi.org/10.1080/10498850.2021.1924907

DOF (Official Journal of the Federation)[Internet]. SEGOB. 2022 Apr - [cited 2023 Dec 27]. Permissible fisheries quota of the Gulf corvina Scinoscion othonopterhus for the year 2022. Available from: https://www.dof.gob.mx/nota_detalle.php?codigo=5647999&fecha=05/04/2022#gsc.tab=0

González-Félix ML, Minjarez-Osorio C, Perez-Velazquez M, Urquidez-Bejarano P. Influence of dietary lipid on growth performance and body composition of the Gulf corvina, Cynoscion othonopterus. Aquaculture. 2015;448:401-9. https://doi.org/10.1016/j.aquaculture.2015.06.031

Minjarez-Osorio C, Castillo-Alvarado S, Gatlin DM III, González-Félix ML, Perez-Velazquez M, Rossi W. Plant protein sources in the diets of the sciaenids red drum (Sciaenops ocellatus) and shortfin corvina (Cynoscion parvipinnis): A comparative study. Aquaculture. 2016;453:122-9. https://doi.org/10.1016/j.aquaculture.2015.11.042

Fischer W, Krupp F, Schneider W, Sommer C, Carpenter KE, Niem VH. FAO identification guide for fishery purposes. Western-Central Pacific. Vol. 3, Vertebrates. Rome, Italy;1995. 1813 p.

Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227:680-5. https://doi.org/10.1038/227680a0

Díaz-López M, Moyano-López FJ, Alarcón-López FJ, García-Carreño FL, Navarrete del Toro MA. Characterization of fish acid proteases by substrate-gel electrophoresis. Comp Biochem Physiol B. 1998;121:369-77. https://doi.org/10.1016/S0305-0491(98)10123-2

Anson ML. The estimation of pepsin, trypsin, papain, and cathepsin with hemoglobin. J Gen Physiol. 1938;22:79-89. https://doi.org/10.1085/jgp.22.1.79

Bougatef A, Balti R, Zaied SB, Souissi N, Nasri M. Pepsinogen and pepsin from the stomach of smooth hound (Mustelus mustelus): Purification, characterization and amino acid terminal sequences. Food Chem. 2008;107:777-84. https://doi.org/10.1016/j.foodchem.2007.08.077

Martinez A, Olsen RL. Characterization of pepsins from cod. US Biochem Corp. 1989;16:22-23.

Castillo-Yañez FJ, Pacheco-Aguilar R, García-Carreño FL, Navarrete-Del Toro MA. Characterization of acidic proteolytic enzymes from Monterey sardine (Sardinops sagax caeruleus) viscera. Food Chem. 2004;85:343-50. https://doi.org/10.1016/j.foodchem.2003.07.008

Wu T, Sun LC, Du CH, Cai QF, Zhang QB, Su WJ, Cao MJ. Identification of pepsinogens and pepsins from the stomach of European eel (Anguilla anguilla). Food Chem. 2009;115:137-42. https://doi.org/10.1016/j.foodchem.2008.11.077

Punekar NS. Enzymes: catalysis, kinetics and mechanisms. Singapore: Springer Nature Singapore Pte Ltd; 2018. 562 p. https://doi.org/10.1007/978-981-13-0785-0

Schlüter H, Apweiler R, Holzhütter HG, Jungblut PR. Finding one's way in proteomics: a protein species nomenclature. Chem Cent J. 2009;3:1-10. https://doi.org/10.1186/1752-153X-3-11

Andreadis A, Gallego ME, Nadal-Ginard B. Generation of protein isoform diversity by alternative splicing: mechanistic and biological implications. Annu Rev Cell Biol. 1987;3:207-42. https://doi.org/10.1146/annurev.cb.03.110187.001231

Xia X. Bioinformatics and the cell: Modern computational approaches in genomics, proteomics and transcriptomics. 2nd ed. Boston, USA: Springer; 2007. Chapter 10, Protein isoelectric point; p. 207-9. https://doi.org/10.1007/978-0-387-71337-3

Arunchalam K, Haard NF. Isolation and characterization of pepsin from polar cod (Boreogadus saida). Comp Biochem Physiol B Comp Biochem. 1985;80:467-73. https://doi.org/10.1016/0305-0491(85)90274-3

Nalinanon S, Benjakul S, Visessanguan W, Kishimura H. Tuna pepsin: characteristics and its use for collagen extraction from the skin of threadfin bream (Nemipterus spp.). J Food Sci. 2008;73:C413-C419. https://doi.org/10.1111/j.1750-3841.2008.00777.x

Scopes RK. Enzyme activity and assays. In: Encyclopedia of Life Sciences. London: John Wiley & Sons Ltd; 2002. https://doi.org/10.1038/npg.els.0000712

Nurhayati T, Ambarsari L, Nurilmala M, Abdullah A, Rakhmawati IAI, Yuniasih. Pepsin activity from gastric of milkfish and catfish in Indonesian waters. IOP Conf Ser Earth Environ Sci. 2020;404:012060. https://doi.org/10.1088/1755-1315/404/1/012060

Downloads

Published

2024-04-24

How to Cite

1.
Perez-Velazquez M, Maldonado-Othón CA, González-Félix ML. Molecular weights and optimum temperature and pH for pepsin activity of three sciaenid finfish species from the Gulf of California. Arch Biol Sci [Internet]. 2024Apr.24 [cited 2024Nov.22];76(1):83-90. Available from: https://serbiosoc.org.rs/arch/index.php/abs/article/view/9376

Issue

Section

Articles

Most read articles by the same author(s)