Biochemical characterization of trypsins from the hepatopancreas of Japanese sea bass (Lateolabrax japonicus)

Cai, Qiu-Feng; Jiang, Yu-Kun; Zhou, Li-Gen; Sun, Le-Chang; Osatomi, Kyoshi; Cao, Min‐Jie

doi:10.1016/j.cbpb.2011.04.002

Cited by 20 publications

(7 citation statements)

References 36 publications

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“…These results are consistent with those reported for trypsin from fish species in literature [6]. Trypsin stability to pH variation was similar to the findings reported by Silva et al [7] for silver mojarra D. rhombeus remaining stable in a range of alkaline pH (8.5-11.0) and being unstable in pH below 8.5 and showing negligible activity at pH 4.5, while Cai et al [20] reported recovery of activity for Japanese sea bass L. japonicus in the pH range from 7.0 to 11.0.…”

Section: Discussionsupporting

confidence: 91%

“…In this study, peak activity of trypsin was found in the pH 9.0. Similar reports have showed the optimum activity of enzymatic crude extracts from Brownstripe red snapper Lutjanus vitta [26], Japanese sea bass L. japonicus [20] and pirarucu A. gigas [8] in the range from 8.5 to 10.0. These results are consistent with those reported for trypsin from fish species in literature [6].…”

Section: Discussionsupporting

confidence: 79%

“…The activity of the trypsin from crude extract tested in the present study was higher than that from crude extract of Japanese sea bass Lateolabrax japonicus (0.30 IU/mg) [20], zebra blenny Salaria basilisca (0.12 IU/mg) [11], pirarucu A. gigas (0.37 IU/mg [8], tropical gar A. tropicus (0.000 006 IU/mg) [13] and hybrid catfish (Clarias microcephalus x Clarias gariepinus) (0.18 IU/mg) [21].…”

Section: Discussioncontrasting

confidence: 67%

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Study on enzymes of industrial interest in digestive viscera: Greater amberjack (Seriola dumerili)

Oliveira¹,

Nascimento²,

Assis³

et al. 2017

JCLM

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Section: Discussionsupporting

confidence: 91%

Section: Discussionsupporting

confidence: 79%

Section: Discussioncontrasting

confidence: 67%

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Study on enzymes of industrial interest in digestive viscera: Greater amberjack (Seriola dumerili)

Oliveira¹,

Nascimento²,

Assis³

et al. 2017

JCLM

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“…Trypsins are mainly known to be more active at pH 7.5-10.5 (Simpson 2000). The optimum pH (8.5) recorded for trypsin in both ICEs was similar with results reported for trypsins from the brownstripe red snapper viscera and the albacore tuna liver (Khantaphant and Benjakul 2010; Klomkalo and Benjakul 2018), whereas both trypsins indicated the lower optimum temperature than those recorded for the Japanese sea bass, the albacore tuna spleen and the pirarucu (Cai et al 2011;Poonsin et al 2019; De Freitas-Junior et al 2021). However, optimum pH may differ depending upon the experimental conditions such as concentration and type of substrate, temperature and type of metal ions (Klomkalo et al 2006).…”

Section: Effect Of Ph On Activity and Stabilitysupporting

confidence: 82%

Physicochemical and biochemical properties of intestinal trypsin from sturgeon fish

Zamani

Khajavi

Kenari

et al. 2022

Preprint

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This work aimed to determine the physicochemical and biochemical characterization of the intestinal trypsin from beluga (Huso huso) and sevruga (Acipenser stellatus), two highly valuable sturgeon species, by a series of assays. According to the results obtained from casein-zymogram and inhibitory activity staining method, indicating the existence of trypsin in the intestinal crude extract of both species, molecular weight of the enzyme was estimated to be 27.5 and 29.5 kDa in sevruga and beluga, respectively. Optimum pH and temperature of both trypsins were recorded at 8.5 and 55°C by BAPNA (a specific substrate), respectively. The stability of both trypsins was well preserved at pH from 6.0 to11.0 and temperatures of up to 50°C. TLCK and SBTI, two specific trypsin inhibitors, showed a significant inhibitory effect on the enzymatic activity of both trypsins (P < 0.05). The enzyme activity was significantly increased in the presence of Ca+ 2 and surfactants and decreased by oxidizing agents, Cu+ 2, Zn+ 2 and Co+ 2 (P < 0.05). However, univalent ions Na+and K+ did not show any significant effect on the activity of both trypsins (P > 0.05). Therefore, the results of our study can contribute to the clear understanding of the intestinal trypsin activity in beluga and sevruga under evaluated experimental conditions.

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“…In the last 12 years, some other native fish trypsins have been characterized and are summarized in Table 1. BAPNA and TAME remain the preferred substrates for the enzymatic characterization; however, alternative synthetic substrates, such as t-butyloxy-carbonyl-Phe-Ser-Arg-4-methyl-coumaryl-7-amide (Boc-Phe-Ser-Arg-MCA), N-benzoyl-l-arginine ethyl ester HCl (BAEE), and benzyloxycarbonyl-l-Phe-l-Arg-p-nitroanilide (CBZ-FR-pNA) and benzyloxycarbonyl-Gly-Pro-Arg p-nitroanilide acetate salt (CBZ-GPR-pNA), have been recently assayed (Liu et al 2007;Lu et al 2008;Cai et al 2011;Stefansson et al 2017). These fluorogenic substrates facilitate the quantification of enzymatic activity; however, it is unknown whether the features observed using these synthetic substrates resemble those that would be obtained using natural substrates.…”

Section: Sources and Enzymatic Properties Of Native Fish Trypsinsmentioning

confidence: 99%

Fish trypsins: potential applications in biomedicine and prospects for production

Cruz¹,

Álvarez‐González²,

Peña³

et al. 2018

3 Biotech

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In fishes, trypsins are adapted to different environmental conditions, and the biochemical and kinetic properties of a broad variety of native isoforms have been studied. Proteolytic enzymes remain in high demand in the detergent, food, and feed industries; however, our analysis of the literature showed that, in the last decade, some fish trypsins have been studied for the synthesis of industrial peptides and for specific biomedical uses as antipathogenic agents against viruses and bacteria, which have been recently patented. In addition, innovative strategies of trypsin administration have been studied to ensure that trypsins retain their properties until they exert their action. Biomedical uses require the production of high-quality enzymes. In this context, the production of recombinant trypsins is an alternative. For this purpose, -based systems have been tested for the production of fish trypsins; however,-based systems also seem to show great potential in the production of fish trypsins with higher production quality. On the other hand, there is a lack of information regarding the specific structures, biochemical and kinetic properties, and characteristics of trypsins produced using heterologous systems. This review describes the potential uses of fish trypsins in biomedicine and the enzymatic and structural properties of native and recombinant fish trypsins obtained to date, outlining some prospects for their study.

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Biochemical characterization of trypsins from the hepatopancreas of Japanese sea bass (Lateolabrax japonicus)

Cited by 20 publications

References 36 publications

Study on enzymes of industrial interest in digestive viscera: Greater amberjack (Seriola dumerili)

Study on enzymes of industrial interest in digestive viscera: Greater amberjack (Seriola dumerili)

Physicochemical and biochemical properties of intestinal trypsin from sturgeon fish

Fish trypsins: potential applications in biomedicine and prospects for production

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