Trypsin purified from Coryphaena hippurus (common dolphinfish): Purification, characterization, and application in commercial detergents

Santos, Dávida Maria Ribeiro Cardoso dos; Santos, Claudio Wilian Victor dos; Souza, Cledson Barros de; Albuquerque, Fabiana Sarmento de; Oliveira, José Marcos dos Santos; Pereira, Hugo Juarez Vieira

doi:10.1016/j.bcab.2020.101584

Cited by 11 publications

(14 citation statements)

References 35 publications

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“…PT showed a higher K cat for BAPNA than the trypsin extracted from P. disjunctivus [56] and Sardinella aurita [23]. Nonetheless, PT had a K cat lower than that of trypsin from Cirruhinus mrigala [12] and Coryphaena hippurus [20] (Table 3). PT had a relatively lower K cat for TAME.…”

Section: Enzyme Kineticsmentioning

confidence: 94%

“…PT had a lower K m value for hydrolyzing BAPNA than those of trypsin from P. disjunctivus [56], Sardinella aurita [23], and Cirruhinus mrigala [12]. Conversely, PT had a higher K m than trypsin from Coryphaena hippurus [20] when BAPNA was used as a substrate (Table 3). Similarly, PT had a lower K m value for TAME hydrolysis than those of trypsin from Macruronus novaezealandiae [46], Engraulis japonica [57], and Lutjanus vitta [34], but showed a higher K m than trypsin from Thunnus tonggol [58].…”

Section: Enzyme Kineticsmentioning

confidence: 99%

“…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].…”

Section: Introductionmentioning

confidence: 99%

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

Patil

Baloch

Nile

et al. 2023

Foods

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The study aimed to purify trypsin from the pyloric caeca of Asian seabass (Lates calcarifer), and investigate its proteolytic capability toward acid-soluble collagen (ASC) in comparison with commercial porcine trypsin (CPT). Trypsin was purified from pyloric caeca, a leftover from the evisceration process, via ammonium sulphate (40–60% saturation) precipitation, and a soybean trypsin inhibitor (SBTI)–Sepharose 4B column. A 18.5-fold purification and a yield of 15.2% were obtained. SDS-PAGE analysis confirmed a single band of trypsin with a molecular weight of 23.5 kDa. Purified trypsin also showed the single band in native-PAGE. The optimal pH and temperature of trypsin for BAPNA (the specific substrate for amidase) hydrolysis were 8.5 and 60 °C, respectively. The trypsin was stable within the pH range of 7.0–9.5 and temperature range of 25–55 °C. Protease inhibition study confirmed that the purified enzyme was trypsin. The purified trypsin had a Michaelis–Menten constant (Km) and catalytic constant (kcat) of 0.078 mM and 5.4 s−1, respectively, when BAPNA was used. For the hydrolysis of TAME (the specific substrate for esterase), the Km and Kcat were 0.09 mM and 4.8 s−1, respectively. Partially purified seabass trypsin (PPST) had a slightly lower hydrolysis capacity toward ASC than CPT, as evidenced by the lower degree of hydrolysis and protein degradation when the former was used. Both the α-chain and β-chain became more degraded as the hydrolysis time increased. Based on MALDI-TOP, peptides with MW of 2992-2970 Da were dominant in the hydrolysates. Therefore, seabass trypsin could be used in the production of hydrolyzed collagen. It could have economic importance to the market, by replacing some commercial proteases, which have religious constraints.

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Section: Enzyme Kineticsmentioning

confidence: 94%

Section: Enzyme Kineticsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

Patil

Baloch

Nile

et al. 2023

Foods

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“…47,59 However, this temperature is higher than that of common sea bream trypsin 58 (50 °C) and common dolphinfish (Coryphaena hippurus) trypsin (40°C). 63 Thermostability was also explored through the incubation of the enzyme at various temperatures for 1 h, as depicted in Figure 4b. The trypsin exhibited high stability between 20 to 40 °C, retaining 100% and 77% of its residual activity, respectively.…”

Section: Optimal Ph and Stabilitymentioning

confidence: 99%

Purification of Trypsin from Sardine (Sardina pilchardus) Viscera and Its Application in Preparation of Antioxidative Fish Protein Hydrolysates

2024

TJNPR

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Among the alkaline proteases in fish viscera, trypsin is one the key members, belonging to the serine-protease family (EC. 3.4.21). 20 Recently, special focus has been on the isolation of trypsins from fish viscera as a value-added product with versatile applications in several sectors. 21,22 Trypsins are utilized as essential components in detergents. 18,23,24 Additionally, they play a crucial role in extracting carotenoproteins from shrimp waste, 25,26,27 contributing to the production of protein hydrolysates that serve as valuable source of biopeptides. 28,29,30 Moreover, promoting the sustainable use of fish byproducts for human consumption stands as a top priority. Nowadays, the formation of fish protein hydrolysates (FPH) stands as one of the promising industrial applications of fish by-products. 31,32,33 The outstanding functional (emulsifier, foaming compounds) bioactive activities (antioxidant, antihypertensive, antibacterial), and nutritional properties of FPH broaden its range of applications. In fact, multiple reviews have uncovered the diverse bioactivities of hydrolysates and peptides derived from marine by-products, as well as their current and potential applications. 6,[34][35][36][37][38][39][40] The most efficient methods for obtaining protein hydrolysates from fish waste are considered to be bioconversion through enzymatic hydrolysis and fermentation. In fact, natural antioxidants are favored over chemically synthesized ones due to their GRAS statue (Generally Recognized As Safe). 41,42 Proteases from animals, plants, bacteria, and fungi have been applied in addition to the bacterial commercial protease Alcalase®. 28,[43][44][45][46] The primary species captured along the Moroccan coast is the sardine (S. pilchardus), with the majority of this harvest being employed in the production of canned sardines. The processing of raw materials results in the production of by-products such as heads, viscera, and muscle.

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“…The effect of trypsin [11], keratinase [12,13], and alkaline protease [14] on cleaning is obvious. The compound washing effect is better after the protease is proportioned.…”

Section: Introductionmentioning

confidence: 99%

Compatibility and Washing Performance of Compound Protease Detergent

Zhang

Xiao

et al. 2021

Applied Sciences

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Protease is the main enzyme of detergent. Through the combination of different proteases and the combination of protease and detergent additives, it can adapt to different washing conditions to improve the washing effect. In this experiment, whiteness determination, microscope scanning, Fourier transform infrared spectroscopy, and X-ray photoelectron spectroscopy were used to detect the whiteness values of the cloth pieces before and after washing, as well as the stain residue between the fibers on the surface of the cloth pieces. The protease detergent formula with better decontamination and anti-deposition effects was selected. The combination of alkaline protease, keratinase, and trypsin was cost-effective in removing stains. Polyacrylamide gel electrophoresis showed that the molecular weight of the protein significantly changed after adding the enzyme preparation during washing, and the molecular weight of the protein was directly proportional to protein redeposition. The composite protease had a better comprehensive decontamination effect, and when compatible with suitable surfactants, anti-redeposition agents, and water-softening agents, the compound protease detergent exhibited a stronger decontamination ability than commercial detergents.

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Trypsin purified from Coryphaena hippurus (common dolphinfish): Purification, characterization, and application in commercial detergents

Cited by 11 publications

References 35 publications

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

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

Purification of Trypsin from Sardine (Sardina pilchardus) Viscera and Its Application in Preparation of Antioxidative Fish Protein Hydrolysates

Compatibility and Washing Performance of Compound Protease Detergent

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