Variations in the activity of digestive enzymes along the intestine of the burbot Lota lota expressed by different methods

Извекова, Г. И.; Solovyev, Mikhail; Kashinskaya, E. N.; Извеков, Е. И.

doi:10.1007/s10695-013-9773-y

Cited by 19 publications

(17 citation statements)

References 24 publications

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“…The key role in food utilization depends on the activity of digestive enzymes present in various regions of the digestive tract. The analysis of the efficiency of fish digestion under natural and aquaculture conditions requires of detailed studies on various aspects of food hydrolysis in the gut, including the influence of temperature and pH on the activity of digestive enzymes among others, since enzyme activity mainly depends on these two factors (Izvekova et al, 2013). The majority of research dealing with analysis of activity of digestive enzymes starts with determining the optimal pH values for their functioning.…”

Section: Introductionmentioning

confidence: 99%

Dependence of pH values in the digestive tract of freshwater fishes on some abiotic and biotic factors

et al. 2017

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The values of pH in the digestive tracts of 20 freshwater fish species inhabiting various Russian Federation waterbodies were studied. Only in six species (Coregonus lavaretus, Coregonus migratorius, Catostomus catostomus, Carassius gibelio, Rutilus rutilus, Leuciscus leuciscus) out of 20 species, the differences in pH values between different regions of the intestine were significant. Feeding habits, feeding frequency and gut fullness in fish affected pH values. Temperature was one of the most important factors affecting pH values. During cold seasons (spring and fall; average water temperature: 8-10 ○ С and 5-6 ○ С, respectively), pH values in fish guts were higher than in summer (water temperature 22-25 °C) for C. gibelio, Perca fluviatilis, Cyprinus carpio, L. leuciscus, and R. rutilus from the Chany Lake. Similar results (lower pH values in intestine at higher water temperatures) were also obtained for C. gibelio in warmer years in comparison to colder years in the same waterbody and in L. leuciscus and P. fluviatilis in the different waterbodies with different water temperatures. It is hypothesized that dependence of pH in fish gut on temperature may serve as a regulatory mechanism for maintaining the activities of hydrolytic enzymes at the required level for their successful functioning. (Barrington, 1957; Fange & Grove, 1979; Sorvachev, 1982), but also by their feeding habits (Pegel', 1959) and the stage of the digestion process (Maier, 1984; Deguara et al., 2003). Regarding the intestine, the values of pH of this section of the digestive tract in different species like goldfish Carassius gibelio, ide Leuciscus idus, wild carp Cyprinus carpio, perch Perca fluviatilis, and zander Sander lucioperca are close to neutral or weakly alkaline, but seldom approach to the acidic range, regardless of the fact of having a stomach or being agastric species (Solovyev et al., 2015). Thus, the different level of pH values could effect on the activity of digestive enzymes as it was shown in numerous in vitro studies (Solovyev et al., 2015; Concha-Frias et al., 2016; Pujante et al., 2016 among others). Alkaline proteases may actively function in a broad range of pH values (Alarcon et al., 1998; Solovyev et al., 2015). The optimal pH values for intestinal alkaline proteases range from 8 to 10 and they could be species-specific, as it was demonstrated for Asian bony tongue Scleropages formosus, S. sagax caerulea, Mayan cichlid Cichlasoma urophthalmus and three-spot cichlid Cichlasoma trimaculatum (Natalia et al., 2004; Castillo-Yaneza et al., 2004; Cuenca-Soria et al., 2013; Toledo-Solís et al., 2015). In particular, the optimal pH values for trypsin range from 8 to 9 in different fish species such as Atlantic halibut Hippoglossus hippoglossus, Dover sole Solea solea, turbot S. maximus and red drum Sciaenops ocellatus (Glass et al., 1989; Lazo et al., 2007); whereas for chymotrypsin, the optimal pH value is close to 8 in red drum S. ocellatus (Applebaum et al., 2001). However, it was shown that both trypsin and chymotrypsin...

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Section: Introductionmentioning

confidence: 99%

Dependence of pH values in the digestive tract of freshwater fishes on some abiotic and biotic factors

et al. 2017

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“…In this sense, the studies on protease characterization allow us to understand the capacity of fish to hydrolyze and metabolize proteins, which are necessary for adequate growth and development (Ma et al 2005). For several years many studies have been conducted to characterize digestive proteases such as in common dentex (Dentex dentex), blue discus (Symphysodon aequifasciata), burbot (Lota lota) and common carp (Cyprinus carpio) (Alarcón, Díaz, Moyano, & Abellan, 1998;Chong, Natalia, & Hashim, 2002a;Izvekova, Solovyev, Kashinskaya, & Izvekov, 2013;Farhoudi, Abedian, Nazari, & Makhdoomi, 2013). In Mexico, the culture of marine fish is based on a few species such as spotted rose snapper (Lutjanus guttatus) (Ibarra-Castro, & Alvarez-Lajonchère, 2011), totoaba (Totoaba macdonaldi) (Galaviz, et al 2015) and red drum (Sciaenops ocellatus) (Gatlin III, 2002).…”

Section: Introductionmentioning

confidence: 99%

Partial Characterization of Digestive Proteases in the Common Snook Centropomus undecimalis

Concha‐Frías¹,

Álvarez‐González²,

Gaxiola³

et al. 2016

IJB

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Common snook (Centropomus undecimalis) is a marine species with high aquaculture potential; although its digestive physiology is still unknown and knowledge of that could allow the development of a balanced feed for commercial culture of this fish. The objective of this study was to partially characterize the digestive proteases in C. undecimalis using electrophoretic and biochemical techniques. A total of 50 wild snook juveniles were used to determine the optimal values of pH stability and temperature as well as the effect of inhibitors on digestive, gastric and intestinal proteases. The optimal pH for gastric proteases was obtained to be 2 with stability obtained between 2 and 8; the optimal temperature was detected at 75ºC for in vitro test, and the thermal stability was between 25 and 45ºC. Intestinal proteases showed two peaks of activity at a pH of 7 and 11; meanwhile, the greatest stability was found between a pH of 4 and 10; the optimal temperature was at 65ºC, and the greatest stability was detected between 35 and 45ºC. Up to 86% of the gastric protease activity was inhibited by pepstatin A; meanwhile, the intestinal proteases TPCK, TLCK, 1-10 Phenanthroline, SBT1, EDTA, PMSF and ovalbumin reduced the activity by 17%, 68%, 85%, 41%, 40.5%, 60% and 59%, respectively.

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“…An additional factor exacerbating these negative effects could be infection with the large cestode Eubothrium rugosum (Batsch, 1786). This species exclusively parasitises the burbots and in some years the prevalence of infection reaches 100% (Izvekova et al 2013). Therefore, understanding the adaptation of E. rugosum to the enzymatically hostile intestinal environment is of particular interest.…”

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confidence: 99%

Inactivation of proteolytic enzymes by Eubothrium rugosum (Cestoda) from the gut of burbot Lota lota

2017

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Parasitic organisms inhabiting the alimentary canal should permanently resist the destructive action of host digestive enzymes. The intestinal parasites were shown to produce specific protease inhibitors protecting them from proteolysis. However, little is known about this adaptive mechanism in cestodes so far, especially for the tapeworms dwelling inside the fish intestines. Here, we explored the ability to inactivate proteolytic enzymes in the fish tapeworm Eubothrium rugosum (Batsch, 1786) (Bothriocephalidea) parasitising the intestine of wild burbot, Lota lota (Linnaeus). The assays were conducted with different concentrations of commercial trypsin and homogenate of intestinal mucosa both being the sources of proteinases. The incubation of live E. rugosum in trypsin solutions of two different concentrations caused a significant decrease in the enzyme activity. The extent of activity reduction was dependent on trypsin concentration. At the same time, the inhibitory effect of the worm incubation medium turned out to be statistically insignificant. These findings suggest partial adsorption of the enzyme to the tegument surface, with its further inactivation. In contrast to the incubation medium, the worm extract suppressed over 80% of trypsin activity and nearly half of the proteolytic activity in the mucosa homogenate. Notably, the inhibitory activity of the tapeworms hardly depended on their size characteristics. Finally, the research has demonstrated secretion of proteinase inhibitor in E. rugosum, which appears to be essential for its survival in enzymatically hostile environment.

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Variations in the activity of digestive enzymes along the intestine of the burbot Lota lota expressed by different methods

Cited by 19 publications

References 24 publications

Dependence of pH values in the digestive tract of freshwater fishes on some abiotic and biotic factors

Dependence of pH values in the digestive tract of freshwater fishes on some abiotic and biotic factors

Partial Characterization of Digestive Proteases in the Common Snook Centropomus undecimalis

Inactivation of proteolytic enzymes by Eubothrium rugosum (Cestoda) from the gut of burbot Lota lota

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