Digestive proteinases of red shrimp Pleoticus muelleri (Decapoda, Penaeoidea): partial characterization and relationship with molting

Fernández-Gimenez, Analía Verónica; García‐Carreño, Fernando; Toro, M. A. Navarrete del; Fenucci, Jorge L.

doi:10.1016/s1096-4959(01)00437-7

Cited by 74 publications

(49 citation statements)

References 19 publications

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“…According to Dall et al (1990), activities of digestive enzymes are least affected by moulting processes during the intermoult stage. In P. muelleri, enzyme activities were lowest during the intermoult stage while they were highest in the postmoult stage (Fernández Gimenez et al, 2001). In P. vannamei, trypsin activity was significantly influenced by starvation as well as by moulting (Muhlia-Almazán and García-Carreño, 2002).…”

Section: Variation Of Trypsinmentioning

confidence: 93%

“…Generally, maximum activities of most crustacean proteinases range between pH 5.0 and 9.0 (Garcia-Carreñ o, 1992;Garcia-Carreño et al, 1994;Ceccaldi, 1997). Trypsin-like serine proteinases typically show pH-optima at neutral or slightly alkaline conditions between pH 7.5 and 9.0; for example, total proteinase of the shrimp P. muelleri which has a high amount of trypsin-like serine proteinases has a pH-optimum between pH 7.5 and 8.0 (Fernández Gimenez et al, 2001). In P. vannamei, where the major proteinases were the serine proteinases trypsin and chymotrypsin, total proteolytic activity was highest at slightly alkaline conditions (Le Moullac et al, 1997).…”

Section: The Presence Of Cysteine Proteinasesmentioning

confidence: 99%

“…On the contrary, Crangon extracts with high trypsin activities did show distinct peaks of trypsin and chymotrypsin. In many crustaceans, the number of trypsin isoforms varies between species but mostly at least two or three isoforms are present (e.g., Honjo et al, 1990, Fernández Gimenez et al, 2001, Muhlia-Almazán and García-Carreño, 2002. Both Crangon species, however, expressed only a single trypsin isoform.…”

Section: The Presence Of Cysteine Proteinasesmentioning

confidence: 99%

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Cysteine proteinases substitute for serine proteinases in the midgut glands of Crangon crangon and Crangon allmani (Decapoda: Caridea)

Teschke

Saborowski

2005

Journal of Experimental Marine Biology and Ecology

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The utilization of dietary proteins in crustaceans is facilitated by a set of peptide hydrolases which are often dominated by btrypsin-likeQ serine proteinases. As expected, the North Sea shrimps Crangon crangon and Crangon allmani showed in their midgut glands high proteolytic activities. However, the majority of animals lacked trypsin and chymotrypsin. Conversely, a minority of about 10% of the animals had elevated trypsin activities. The appearance of trypsin was neither related to the mode of feeding nor to the nutritive state of the animals. When present, trypsin was expressed in both species as a single isoform of apparently 20 kDa. The lack of serine proteinases was also confirmed by inhibitor assays. AEBSF, a serine proteinase inhibitor, slightly reduced total proteinase activity by less than 10%. In contrast E 64, a cysteine proteinase inhibitor, caused a reduction of more than 70% of total proteinase activity, indicating that a substantial share of proteolytic activity is caused by cysteine proteinases. Cathepsin L-like proteinases were identified as major cysteine proteinases.A comparison with the eucarid crustaceans Pandalus montagui, Pagurus bernhardus, Cancer pagurus and Euphausia superba showed a similar high level of total proteinase activity in all species. Trypsin, however, varied significantly between species showing lowest activities in Caridea and the highest activity in E. superba. E 64 suppressed total proteinase activity by more than 70% in Crangon species but not in C. pagurus and E. superba. In contrast, the serine proteinase inhibitor AEBSF had only little effect in Caridea but was most effective in P. bernhardus, C. pagurus and E. superba. The results may indicate different traits of food utilization strategies in some eucarid crustaceans. Caridea may express predominantly cysteine proteinase, while in Anomura, Brachyura and Euphausiacea, serine proteinases may prevail. D

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Section: Variation Of Trypsinmentioning

confidence: 93%

Section: The Presence Of Cysteine Proteinasesmentioning

confidence: 99%

Section: The Presence Of Cysteine Proteinasesmentioning

confidence: 99%

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Cysteine proteinases substitute for serine proteinases in the midgut glands of Crangon crangon and Crangon allmani (Decapoda: Caridea)

Teschke

Saborowski

2005

Journal of Experimental Marine Biology and Ecology

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“…However, literature data support our results. The gastric pH for some crustacean species were reported to range between pH 5.3 and 6.2 [5,22], the maximum activity of total proteinase appeared in a broad range between pH 5 and 8 [21,[23][24][25] and the maximum of trypsin activity was found at pH 7-8.2 [21,24]. However, also the maximum activity of chymotrypsin ranged between pH 5 and 8 [26].…”

Section: Ph-profilesmentioning

confidence: 99%

Stability and effects of organic solvents on endopeptidases from the gastric fluid of the marine crab Cancer pagurus

Saborowski

Sahling

Toro³

et al. 2004

Journal of Molecular Catalysis B: Enzymatic

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Activities of proteolytic enzymes, represented by azocasein digestion (total protease), trypsin, and chymotrypsin from the gastric fluid of the marine crab, Cancer pagurus, were evaluated for operational parameters like pH-optimum, thermal stability, and effectors such as metal ions and organic solvents. Total protease activity was 98.5 ± 4.3 E 366 min −1 ml −1 . Trypsin and chymotrypsin activities amounted to 14.7 ± 1.5 U ml −1 and 197 ± 59 U ml −1 , respectively. The maximum activity of total protease appeared at pH 5-7, that of trypsin at pH 7-9, and that of chymotrypsin at pH 6.5-7. Trypsin and chymotrypsin activities were slightly activated by Ca 2+ , but were drastically reduced by Zn 2+ . In the presence of 2-propanol, trypsin activity was enhanced 8-fold at 30• C. Highest amplification of activity of up to 30-fold, however, appeared below 12• C. The effects of ethanol and acetone were less distinct. These caused a 2.5-fold increase of activity. Methanol was the least activating solvent.Activities of all enzymes remained stable for up to 127 days at 5• C, keeping up to 70% of the initial activity. When stored at 25• C for 120 days, total protease decreased to about 40% and trypsin and chymotrypsin activities kept more than 60% of initial activity. Zymograms showed five major and several minor proteolytic bands with apparent molecular weight of 20-45 kDa. After long-term storage at room temperature, the major bands remained active, while some bands with minor activity disappeared. This proteolytic enzyme preparation from the gastric fluid of crab seems suitable for biotechnological application at neutral pH and in the presence of organic solvents.

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“…However, informations about chymotrypsins are less available [2]. Chymotrypsins cleave the peptides on the carboxyl side of phenylalanine, tyrosine and tryptophan residues and have been purified and characterized from mammals [3,4]; fishes [5-7] and crustaceans such as scallop ( Pecten maximus ) [8] and shrimp ( Penaus vannamei ) [9]. Chymotrypsins act primarily as an aid of digestion and as anti-inflammatory agent by preventing tissue damage and fibrin clots.…”

Section: Introductionmentioning

confidence: 99%

A new chymotrypsin-like serine protease involved in dietary protein digestion in a primitive animal, Scorpio maurus: purification and biochemical characterization

et al. 2011

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BackgroundMost recent works on chymotrypsins have been focused on marine animals and insects. However, no study was reported in chelicerate.ResultsScorpion chymotrypsin-like protease (SCP) was purified to homogeneity from delipidated hepatopancreases. The protease NH2-terminal sequence exhibited more than 60% monoacids identity with those of insect putative peptidases. The protease displayed no sequence homology with classical proteases. From this point of view, the protease recalls the case of the scorpion lipase which displayed no sequence homology with known lipases. The scorpion amylase purified and characterized by our time, has an amino-acids sequence similar to those of mammalian amylases. The enzyme was characterized with respect its biochemical properties: it was active on a chymotrypsin substrate and had an apparent molecular mass of 25 kDa, like the classically known chymotrypsins. The dependence of the SCP activity and stability on pH and temperature was similar to that of mammalian chymotrypsin proteases. However, the SCP displayed a lower specific activity and a boarder pH activity range (from 6 to 9).Conclusionlower animal have a less evaluated digestive organ: a hepatopancreas, whereas, higher ones possess individualized pancreas and liver. A new chymotrypsin-like protease was purified for the first time from the scorpion hepatopancreas. Its biochemical characterization showed new features as compared to classical chymotrypsin-higher-animals proteases.

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Digestive proteinases of red shrimp Pleoticus muelleri (Decapoda, Penaeoidea): partial characterization and relationship with molting

Cited by 74 publications

References 19 publications

Cysteine proteinases substitute for serine proteinases in the midgut glands of Crangon crangon and Crangon allmani (Decapoda: Caridea)

Cysteine proteinases substitute for serine proteinases in the midgut glands of Crangon crangon and Crangon allmani (Decapoda: Caridea)

Stability and effects of organic solvents on endopeptidases from the gastric fluid of the marine crab Cancer pagurus

A new chymotrypsin-like serine protease involved in dietary protein digestion in a primitive animal, Scorpio maurus: purification and biochemical characterization

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