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

Abstract

Trypsin and pancreatic lipase promote the digestion of proteins and lipids, respectively, when they are secreted into the anterior intestine; however, since the pancreas is a diffuse tissue in fish, the characterization and quantification of pancreatic enzymes is uncommon. The objective of this study was to partially characterize and compare the enzymatic activities of lipase and trypsin within the gastrointestinal tract of Cynoscion parvipinnis, Cynoscion othonopterus and Cynoscion xanthulus, to contribute to the knowledge of the digestive physiology of these important commercial sciaenids and to reveal whether they have potential for biotechnological applications. The presence of lipase and trypsin was confirmed by zymography and the molecular weights of both enzymes were determined by electrophoresis. For lipase, molecular weights of 65.8 and 69.5 kDa were determined for C. othonopterus and C. xanthulus, respectively. For C. parvipinnis, two lipases of 61.5 and 36.0 kDa were determined. In all three species the largest lipase activity was observed in the anterior intestine, followed by pyloric caeca, with optimum activity observed at pH 8.0 and at temperatures ranging between 40 and 45°C. Molecular weights of trypsin were 24.4, 23.6 and 23.7 kDa in C. othonopterus, C. parvipinnis, and C. xanthulus, respectively. The optimum pH of activity ranged between 7.0 and 9.0 and optimum temperature between 55 and 65°C for all species. These enzymes meet certain criteria that make them potential candidates for some industrial applications, such as the food industry and the production of detergents.

Physicochemical and Biochemical Properties of Trypsin-like Enzyme from Two Sturgeon Species

“…In general, trypsins have molecular weights in the range of 20-30 kDa [47]. In particular, different molecular weights for trypsins have been reported in various fish species such as 21.7 kDa for mrigal carp [48], 23.2 kDa for common kilka [40], 23.5 kDa for pirarucu [49], 24 kDa for small red scorpion fish [50], 21 and 24 kDa for liver of albacore tuna [51], 24 kDa for catfish [52], 24.4 kDa for gulf corvina [53], 25 kDa for Monterey sardine [54], 26 kDa for common dolphinfish [55], 27 kDa for zebra blenny [56], 28.8 kDa for sardinelle [57], 29 kDa for Atlantic bonito [58], 38.5 kDa for tambaqui [59], and 42 kDa for skipjack tuna [60]. However, several reasons such as different habitat and climate, autolytic degradation, and genetic variation among fish species may explain why trypsins from various sources have different molecular weights [60,61].…”

Efek Perbedaan Temperatur terhadap Aktivitas Tripsin-Like dan Amilase Digesti Ikan Lunjar (Rasbora lateristriata Blkr.)

“…Adanya aktivitas tripsin-like yang tidak berbeda secara signifikan di antara temperatur 20-50ºC pada penelitian ini yang menunjukkan bahwa temperatur optimal tripsin-like berada pada temperatur tersebut. Fenomena ini tidak berbeda dengan hasil penelitian sebelumnya pada Cynoscion xanthulus dan Cynoscion othonopterus yang memperlihatkan aktivitas tripsin-like tidak berbeda secara signifikan di antara temperatur 20-50ºC (Félix et al, 2020). Hasil yang tidak berbeda juga dijumpai pada ikan Totoaba macdonaldi yang menunjukkan aktivitas tripsin-like sama pada temperatur 20-40ºC (Gutiérrez et al, 2020).…”

Trypsin from Pyloric Caeca of Asian Seabass: Purification, Characterization, and Its Use in the Hydrolysis of Acid-Soluble Collagen

“…Trypsin is a very important enzyme, with several commercial uses in food companies. Trypsin has been isolated, purified, and characterized from various species of fish, including the mrigal carp (Cirrhinus mrigala) [12], common kilka (Clupeonella cultriventris caspia) [13], pirarucu (Arapaima gigas) [14], small red scorpion fish (Scorpaena notata) [15], albacore tuna (Thunnus alalunga) [16], catfish (Luphiosilurus alexandri) [17], gulf corvina (Cynoscion parvipinnis) [18], Monterey sardine (Sardinops sagax caerulea) [19], common dolphinfish (Coryphaena hippurus) [20], skipjack tuna (Katsuwonus pelamis) [21], zebra blenny (Salaria basilisca) [22], sardinelle (Sardinella aurita) [23], Atlantic bonito (Sarda sarda) [24], tambaqui (Colossoma macropomum) [25], yellowfin tuna (Thunnus albacores) [26], beluga (Huso huso), and sevruga (Acipenser stellatus) [27]. Trypsin was used to hydrolyze gelatin from the skin of giant catfish, in which antioxidative peptides were generated [28].…”