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      Biochemical features and modulation of digestive enzymes by environmental temperature in the greater amberjack, Seriola dumerili

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      Frontiers in Marine Science
      Frontiers Media SA

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          Abstract

          The study of fish digestive biochemistry is essential to understand factors that affect the net efficiency of food transformation and growth, and therefore aquaculture profitability. The aim of the present study was to assess the activity and functional characteristics of key digestive enzymes in juveniles of greater amberjack ( Seriola dumerili), as well as the possible modulation of their relative importance by water temperature. For that, a combination of biochemical assays and substrate-SDS-PAGE were used. Under physiological conditions pepsin activity was negligible. Chymotrypsin was the most active enzyme in the digestive tract of the greater amberjack, while lipase was the enzyme with lower activity, though both enzymes in addition to trypsin were responsive to water temperature as revealed by discriminant analysis. Seriola dumerili showed to have pH-sensitive and, except for chymotrypsin, thermally robust proteases. Inhibition assays showed the major importance of serine proteases and revealed inverse trypsin and chymotrypsin responses to environmental temperature, with higher trypsin contribution in 26°C-fish while higher chymotrypsin contribution in 18°C-fish. Zymograms revealed three isotrypsin and three isochymotrypsin enzymes, with no variation in the presence of particular isoforms among rearing temperatures. However, they confirmed the role of chymotrypsin activity in providing digestive plasticity, with one of the isoforms being more active at lower temperatures. Thus, results indicate that variation in the relative contribution of chymotrypsin isoenzymes to a particular environmental temperature occurs due to different physic-chemical features of isoforms as a source of functional flexibility. This study assessed for the first time the effects of rearing temperature on greater amberjack digestive enzymes, increasing the knowledge on its digestive biochemistry, and aiding in the improvement of management practices for this species industrialization.

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          Most cited references51

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          THE ESTIMATION OF PEPSIN, TRYPSIN, PAPAIN, AND CATHEPSIN WITH HEMOGLOBIN

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            Comparative study of digestive enzymes in fish with different nutritional habits. Proteolytic and amylase activities

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              Effects of temperature on feeding and digestive processes in fish.

              As most fish are ectotherms, their physiology is strongly affected by temperature. Temperature affects their metabolic rate and thus their energy balance and behavior, including locomotor and feeding behavior. Temperature influences the ability/desire of the fish to obtain food, and how they process food through digestion, absorb nutrients within the gastrointestinal tract, and store excess energy. As fish display a large variability in habitats, feeding habits, and anatomical and physiological features, the effects of temperature are complex and species-specific. The effects of temperature depend on the timing, intensity, and duration of exposure as well as the speed at which temperature changes occur. Whereas acute short-term variations of temperature might have drastic, often detrimental, effects on fish physiology, long-term gradual variations might lead to acclimation, e.g. variations in metabolic and digestive enzyme profiles. The goal of this review is to summarize our current knowledge on the effects of temperature on energy homeostasis, with specific focus on metabolism, feeding, digestion, and how fish are often able to "adapt" to changing environments through phenotypic and physiological changes.
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                Author and article information

                Journal
                Frontiers in Marine Science
                Front. Mar. Sci.
                Frontiers Media SA
                2296-7745
                July 28 2022
                July 28 2022
                : 9
                Article
                10.3389/fmars.2022.960746
                d5fd759e-3621-4b26-9748-1fc9c7c32aa4
                © 2022

                Free to read

                https://creativecommons.org/licenses/by/4.0/

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