Evaluation of the Biochemical and Functional Characteristic of Stinging catfish, Heteropneustes fossilis Muscle Tissue with Emphasize on Myofibrillar Protein and Collagen

Treesa Varghese; Saleena Mathew

doi:10.17485/IJST/v16i1.1630

Article

Evaluation of the Biochemical and Functional Characteristic of Stinging catfish, Heteropneustes fossilis Muscle Tissue with Emphasize on Myofibrillar Protein and Collagen

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Indian Journal of Science and Technology

DOI: 10.17485/IJST/v16i1.1630

Year: 2023, Volume: 16, Issue: 1, Pages: 66-76

Original Article

Evaluation of the Biochemical and Functional Characteristic of Stinging catfish, Heteropneustes fossilis Muscle Tissue with Emphasize on Myofibrillar Protein and Collagen

Treesa Varghese^1,2*, Saleena Mathew²

¹School of Biosciences, Mar Athanasios College for Advanced Studies, Tiruvalla, Kerala, India
²School of Industrial Fisheries, Cochin University of Science and Technology, Kochi (Retd), Kerala, India

*Corresponding Author
Email: [email protected]

Received Date:09 August 2022, Accepted Date:28 November 2022, Published Date:06 January 2023

This work is licensed under a Creative Commons Attribution 4.0 International License.

Abstract

Objectives: To evaluate the physico-chemical and functional characteristics of the stinging catfish muscle tissue during the storage time of 18 hours following the death of the fish. Methods: In the present study, stinging catfish were collected from the paddy fields and streams near Tiruvalla Kerala. Fish were slaughtered immediately and analyzed for changes in pH value, cook loss, expressible water content, water holding capacity, sensory demerit score values, and textural profile and were compared with progress of rigor mortis. Study also evaluated the changes in protein fractions present in the muscle tissue and correlated them with autolytic enzyme activities. Findings: In stinging catfish, the rigor mortis occurred within four hours of storage (78.37 %) at ambient temperature. The post rigor stage was attained after the 6th hour and the K value reached above 60% within the 8th hour which indicates the unacceptable range for consumption. The present study also proved that the stinging catfish is an inosine producer. The initial concentration of sarcoplasmic protein in fish muscle (13.71%) decreased to 7.62% at the end of 18 hours of storage. The muscle tissue myofibrillar protein also showed a decrease from an initial concentration of 44.87% to a final concentration of 18.02%. Protein denaturation was evident with an increase from 39.65% to 73.20% at the end of the storage period. Collagen concentration was found to be reduced (31.85% reduction) after the 18th hour of storage. Pepsin soluble collagen was less susceptible to the activity of collagenase enzyme in the pre-rigor stage, confirming its role in post-rigor muscle softening when compared to acid soluble and insoluble collagen. Novelty: The present work authenticated that post-rigor softening of stinging catfish muscle is typically due to the degradation of pepsin soluble collagen and not reported elsewhere. Additionally, myofibrillar proteins have more influence on total hardness and stiffness than collagen, while cohesiveness is a better function of collagen than myofibrillar protein. These findings make it useful to perceive the process thatinduces softening in catfish and to create effective strategies to prevent it.

Keywords: Collagen; Myofibrillar Protein; Adenosine Nucleotides; Autolytic Enzymes; Textural Profile

References

Shahadat H, M, Sarker S, Sharifuzzaman SM, Chowdhury SR. New species of stinging catfish Heteropneustes nani (Siluriformes: Heteropneustidae) from Noakhali. Vertebrate Zoology. 2013;63(3):259–267. Available from: https://www.senckenberg.de/wp-content/uploads/2019/08/03_vertebrate_zoology_63-3_hossain_259-267.pdf
Ghaly AE, Budge DD, Brooks S, MS. Fish Spoilage Mechanisms and Preservation Techniques: Review. American Journal of Applied Sciences. 2010;7(7):859–877. Available from: https://doi.org/10.3844/ajassp.2010.859.877
Prabhakar SPK, Vatsa, Sant S, Pathak. A Comprehensive Review on Freshness of Fish and Assessment: Analytical Methods and Recent Innovations. Food Research International. 2020;133:109157. Available from: https://doi.org/10.1016/j.foodres.2020.109157
Suárez MD, Abad M, Ruiz-Cara T, Estrada JD, García-Gallego M. Changes in muscle collagen content during post mortem storage of farmed sea bream (Sparus aurata): influence on textural properties. Aquaculture International. 2005;13(4):315–325. Available from: https://doi.org/10.1007/s10499-004-3405-6
Sato K, Ando M, Kubota S, Origasa K, Kawase H, Toyohara H, et al. Involvement of Type V Collagen in Softening of Fish Muscle during Short-Term Chilled Storage. Journal of Agricultural and Food Chemistry. 1997;45(2):343–348. Available from: https://doi.org/10.1021/jf9606619
Koohmaraie M, Geesink GH. Contribution of postmortem muscle biochemistry to the delivery of consistent meat quality with particular focus on the calpain system. Meat Science. 2006;74(1):34–43. Available from: https://doi.org/10.1016/j.meatsci.2006.04.025
Ahmed Z, Donkor O, Street WA, Vasiljevic T. Calpains- and cathepsins-induced myofibrillar changes in post-mortem fish: Impact on structural softening and release of bioactive peptides. Trends in Food Science & Technology. 2015;45(1):130–146. Available from: https://doi.org/10.1016/j.tifs.2015.04.002
Bito M, Yamada K, Mikumo Y, Amano K. Studies on rigor mortis of fish: Differences in the mode of rigor-mortis among some varieties of fish by modified cuttings method. Bulletin of Tokai Regional Fisheries Research Laboratory. 1983;109:89–96. Available from: https://agris.fao.org/agris-search/search.do?recordID=JP19840076545
Ryder JM. Determination of adenosine triphosphate and its breakdown products in fish muscle by high-performance liquid chromatography. Journal of Agricultural and Food Chemistry. 1985;33(4):678–680. Available from: https://doi.org/10.1021/jf00064a027
Saito T, Arai KI, Matsuyoshi M. A New Method for Estimating the Freshness of Fish. Nippon Suisan Gakkaish. 1959;24(9):749–750. Available from: https://doi.org/10.2331/suisan.24.749
Bremner HA, Hallett IC. Muscle Fiber?Connective Tissue Junctions in the Fish Blue Grenadier (Macruronus novaezelandiae). A Scanning Electron Microscope Study. Journal of Food Science. 1985;50(4):975–980. Available from: https://doi.org/10.1111/j.1365-2621.1985.tb12993.x
Borresen T. New methods for determination of liquid holding capacity, salt water holding capacity and cook loss in fish muscle. (pp. 1-7) Tromso, Norway. FTFI. 1980.
Benjakul S, Visessanguan W, Tueksuban J. Changes in physico-chemical properties and gel-forming ability of lizardfish (Saurida tumbil) during post-mortem storage in ice. Food Chemistry. 2003;80(4):535–544. Available from: https://doi.org/10.1016/S0308-8146(02)00339-4
Devadasan K, Nair MR. Observations on changes in the major protein nitrogen fraction of prawns and sardines during ice storage. Fishery Technology. 1970;7(2):195–197. Available from: https://core.ac.uk/download/pdf/33720228.pdf
Nishimoto M, Sakamoto R, Mizuta S, Yoshinaka R. Identification and characterization of molecular species of collagen in ordinary muscle and skin of the Japanese flounder Paralichthys olivaceus. Food Chemistry. 2005;90(1-2):151–156. Available from: https://doi.org/10.1016/j.foodchem.2004.03.034
Warrier S, Ninjoor V, Sawant PL, Kumta US. Lysosomal enzymes in drip & muscle of Harpodon nehereus. Indian Journal of Biochemistry and Biophysics. 1972;9(2):207–209. Available from: https://www.osti.gov/biblio/4384276
Moore S, Stein W. A modified ninhydrin reagent for the photometric determination of amino acids and related compounds. Journal of Biological Chemistry. 1954;211(18):71178. Available from: https://www.osti.gov/biblio/4384276
Daskalova A. Farmed fish welfare: stress, post-mortem muscle metabolism, and stress-related meat quality changes. International Aquatic Research. 2019;11(2):113–124. Available from: https://doi.org/10.1016/S0021-9258(18)71178-2
Li T, Li J, Hu W. Changes in microbiological, physicochemical and muscle proteins of post mortem large yellow croaker (Pseudosciaena crocea) Food Control. 2013;34(2):514–520. Available from: https://doi.org/10.1007/s40071-019-0230-0
Li J, Zhou G, Xue P, Dong X, Xia Y, Regenstein J, et al. Spoilage microbes’ effect on freshness and IMP degradation in sturgeon fillets during chilled storage. Food Bioscience. 2021;41:101008. Available from: https://doi.org/10.1016/j.fbio.2021.101008
Adoga IJ, Egila J, OFS. Storage life of tilapia (Oreochromis niloticus) in ice and ambient temperature. Researcher. 2010;2(5):39–44. Available from: http://www.sciencepub.net/researcher/research0205/06_2727_research0205_39_44.pdf
Ali H, Nawaz K, Amoa, Qi Y, Leng, Jia H, et al. Poultry Response to Heat Stress: Its Physiological, Metabolic, and Genetic Implications on Meat Production and Quality Including Strategies to Improve Broiler Production in a Warming World. Frontiers in Veterinary Science. 2021;8:1–16. Available from: https://doi.org/10.3389/fvets.2021.699081
Lin SB, Chen LC, Chen HH. The change of thermal gelation properties of horse mackerel mince led by protein denaturation occurring in frozen storage and consequential air floatation wash. Food Research International. 2005;38(1):19–27. Available from: https://doi.org/10.1016/j.foodres.2004.08.001
Ochiai Y, Ozawa H. Biochemical and physicochemical characteristics of the major muscle proteins from fish and shellfish. Fisheries Science. 2020;86(5):729–740. Available from: https://doi.org/10.1007/s12562-020-01444-y
Guan F, Chen Y, Zhao S, Chen Z, Yu C, Yuan Y. Effect of slurry ice during storage on myofibrillar protein of Pseudosciaena crocea. Food Scicience & Nutrition. 2021. Available from: https://doi.org/10.1002/fsn3.2355
Modzelewska-Kapituła M, Kwiatkowska A, Jankowska B, Dąbrowska E. Water holding capacity and collagen profile of bovine m. infraspinatus during postmortem ageing. Meat Science. 2015;100:209–216. Available from: https://doi.org/10.1016/j.meatsci.2014.10.023
Moreno HM, Montero MP, Gómez-Guillén MC, Fernández-Martín F, Mørkøre T, Borderías J. Collagen characteristics of farmed Atlantic salmon with firm and soft fillet texture. Food Chemistry. 2012;134(2):678–685. Available from: https://doi.org/10.1016/j.foodchem.2012.02.160
Liliana G, Fidalgo JA, Saraiva SP, Aubourg M, Vázquez JA, Torres. Enzymatic activity during frozen storage of atlantic horse mackerel (Trachurus trachurus) pre-treated by high-pressure processing. Food and Bioprocess Technology. 2015;8(3):493–502. Available from: https://doi.org/10.1007/s11947-014-1420-9
Hernández-Herrero MM, Duflos G, Malle P, Bouquelet S. Collagenase activity and protein hydrolysis as related to spoilage of iced cod (Gadus morhua) Food Research International. 2003;36(2):141–147. Available from: https://doi.org/10.1016/S0963-9969(02)00129-1
Shigemura Y, Ando M, Tsukamasa Y, Makinodan Y, Kawai T. Correlation of type V collagen content with post-mortem softening of fish meat during chilled storage. Fisheries Science. 2003;69(4):842–848. Available from: https://doi.org/10.1046/j.1444-2906.2003.00696.x
Alderton AL, Means WJ, Kalchayanand N, Mccormick RJ, Miller KW. Bovine metalloprotease characterization and in vitro connective tissue degradation1. Journal of Animal Science. 2004;82(5):1475–1481. Available from: https://doi.org/10.2527/2004.8251475x.
Ali AMM, Benjakul S, Kishimura H. Molecular characteristics of acid and pepsin soluble collagens from the scales of golden carp (Probarbus jullieni) Emirates Journal of Food and Agriculture. 2017;29(6):450. Available from: https://doi.org/10.9755/ejfa.2016-09-1316
Nalinanon S, Benjakul S, Visessanguan W, Kishimura H. Use of pepsin for collagen extraction from the skin of bigeye snapper (Priacanthus tayenus) Food Chemistry. 2007;104(2):593–601. Available from: https://doi.org/10.1016/j.foodchem.2006.12.035

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© 2023 Varghese & Mathew. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Published By Indian Society for Education and Environment (iSee)