Biochemical Characterization and Comparison of Pancreatic Lipases from the Pacific Bluefin Tuna, Thunnus orientalis; Totoaba, Totoaba macdonaldi; and Striped Bass, Morone saxatilis

Abstract

Lipolytic activity from pancreatic crude extracts from the Pacific bluefin tuna (PBT), Thunnus orientalis; totoaba, Totoaba macdonaldi; and striped bass, Morone saxatilis, were biochemically characterized to detect possible differences in the digestive capacity of each fish. The maximum activity was at temperatures ranging from 35 to 45 C and at pH 8.0; the activity decreased significantly at a pH lower than 7.0. Lipases from PBT and totoaba showed an increase in activity with the presence of sodium taurocholate (NaTC; 6 mM). However, no increase in activity could be observed when a mixture of bile salts or natural bile extracts was used in the reaction mixture, which was observed in the presence of NaTC. In contrast, the lipase activity from striped bass increased accordingly when NaCl was added at different levels (0–1.5 M). Calcium was not required in the reaction mixture for any of the fish species tested. We concluded that all three lipases have different physicochemical properties and ionic strength and emulsifier requirements to obtain their maximum activity. Striped bass was far too sensitive to NaCl, while totoaba and PBT were sensitive to NaTC. The differences in activity shown here suggest the possibility of studying the use of different additives on feed formulations to maximize lipase efficiency.

Partial characterization, quantification and optimum activity of trypsin and lipase from the sciaenids Cynoscion othonopterus, Cynoscion parvipinnis and Cynoscion xanthulus

“…The optimum temperature for lipase activity of C. parvipinnis was 45°C; at 40 and 45°C C. xanthulus showed no differences in activity, and for C. othonopterus, 45°C was the temperature where the highest activity was recorded, quite similar to the observation for T. macdonaldi with optimum lipase activity at 45°C [18,19]. Optimum lipase activities between 35 to 45°C in T. orientalis and Morone saxatilis [18] have been reported, and 35°C for O. tshawytscha and M. novaezelandiae [15]. Differences in optimum temperatures for pancreatic enzymes could be explained by the differences in environmental temperatures observed in the habitats of the species, which clearly lead to adaptations [46].…”

“…The optimum temperature for enzyme activity in finfish and higher vertebrates is usually higher than their optimum physiological temperature; this is explained by the increment observed in the molecular kinetic energy at higher temperatures, up until the point where denaturation of the protein occurs [48]. Optimum pH for lipase activity on the other hand was 8.0 for all three sciaenids, coinciding with the value reported for T. macdonaldi, M. saxatilis and T. orientalis [18,19]. For O. tshawytscha and M. novaezelandiae, the optimum pH was reported to be 8.0-8.5 [15].…”

“…Because it requires the presence of bile salts to hydrolyze triacylglycerols or phospholipids with medium or long-chain fatty acids, this enzyme is also known as bile salt-dependent lipase [9,10]. Both lipases have been described in marine finfish [11][12][13][14][15][16][17][18][19][20].…”

Partial characterization, quantification and activity of pancreatic lipase in the gastrointestinal tract of Totoaba Macdonaldi

“…It was established that the BSDL of S. ocellatus had the highest activity at a pH close to 8.0 and 50°C [47], the same temperature value reported for optimal lipolytic activity in S. aurata [41]. The maximum lipolytic activity from pancreatic crude extracts of T. orientalis, T. macdonaldi and Morone saxatilis was reported at pH 8.0 and temperatures ranging from 35 to 45°C [39]. Optimal lipolytic activity was observed at 40°C for Sardinops sagax caerulea [48], while the highest lipolytic activity was observed at 35°C and at a pH of 8-8.5 for O. tshawytscha and Macruronus novaezelandiae [38].…”

“…In this study, the molecular weight determined for pancreatic lipase of T. macdonaldi was 70.4 kDa, which is within the range of values previously mentioned for other fish species. For this sciaenid, there is a strong possibility that the pancreatic lipase described in the current study is not a BSDL because the activity of the enzyme was detected without supplementation of bile salts, and its activity did not increase in the presence of bile salts or natural bile extracts [39], although this inference requires further confirmation.…”