On the purification and characterization of three anionic, serine-type peptide hydrolases from antarctic krill, Euphausia Superba

Osnes, Knut Kr.; Mohr, Viggo

doi:10.1016/0305-0491(85)90497-3

Cited by 51 publications

(34 citation statements)

References 16 publications

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“…E 64 is a highly selective and irreversible inhibitor for cysteine proteinases (Barrett et al, 1982;Katunuma and Kominami, 1995) while AEBSF specifically inhibits serine proteinases (Markwardt et al, 1974). Accordingly, the inhibitor assays confirm the predominance of cysteine proteinases in the midgut gland extracts of both Crangon species while serine proteinases represented the dominant endopeptidases in E. superba, E. bernhardus and C. pagurus, respectively (Osnes and Mohr, 1985;Tsai et al, 1986).…”

Section: The Presence Of Cysteine Proteinasesmentioning

confidence: 68%

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: The Presence Of Cysteine Proteinasesmentioning

confidence: 68%

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 presence of calcium is also found to stabilize the enzymc against thermal inactivation (scc e.g. Osnes et al, 1985). For the new crystal structurc presented here, only one of the four independent molecules is refined with a structurally bound calcium ion.…”

Section: The Four Ncs-related Moleculesmentioning

confidence: 99%

“…In particular many marine species are known to have a rather complex isoenzyme pattern. Capelin (Hjelmeland & Raa, 1982), Antarctic krill (Osnes & Mohr, 1985), cod (Gudmundsd6ttir et aL, 1993), anchovy (Martfnes et aL, 1988) and crayfish (Kim et aL, 1994) have all been identified with multiple forms of trypsin. While the predominant isoforms in mammals are cationic, only anionic variants have been reported for the above-mentioned marine species.…”

Section: Introductionmentioning

confidence: 99%

Structure of a Non-psychrophilic Trypsin from a Cold-Adapted Fish Species

1998

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The crystal structure of cationic trypsin (CST) from the Atlantic salmon (Salmo salar) has been refined at 1.70 ,A, resolution. The crystals are orthorhombic, belong to space group P212121, with lattice parameters a = 65.91, b = 83.11 and c = 154.79 ,~,, and comprise four molecules per asymmetric unit. The structure was solved by molecular replacement with AMoRe and refined with X-PLOR to an R value of 17.4% and Rfree of 21.5% for reflections IFI > 30"F between 8.0 and 1.7 A resolution. The four non-crystallographic symmetry (NCS) related molecules in the asymmetric unit display r.m.s, deviations in the range 0.31-0.74,~ for main-chain atoms, with the largest differences confined to two loops. One of these is the calcium-binding loop where the electrondensity indicates a calcium ion for only one of the four molecules. In order to find structural rationalizations for the observed difference in thermostability and catalytic efficiency of CST, anionic salmon trypsin (AST) and bovine trypsin (BT), the three structures have been extensively compared. The largest deviations for the superimposed structures occur in the surface loops and particularly in the so-called 'autolysis loop'. Both the salmon enzymes possess a high methionine content, lower overall hydrophobicity and enhanced surface hydrophilicity, compared with BT. These properties have so far been correlated to cold-adaptation features, while in this work it is shown that the non-psychrophilic cationic salmon trypsin shares these features with the psychrophilic anionic salmon trypsin.

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“…For both shrimp species, autolysis was most likely mediated by heat-activated proteases that were active at neutral or slightly alkaline pHs. Optimal temperature and pH for autolysis of both species tested were similar to those of proteases from Antarctic krill (Euphausia superba) (pH 8.2, 60°C) (Osnes & Mohr, 1985), North Pacific krill (Euphausia pacifica) (pH 8-9, 50°C) (Sun et al, 2014), hepatopancreas of fresh water prawn (Macrobrachium rosenbergii) (pH 7, 60°C) (Sriket et al, 2011) or Pacific brown shrimp (Penaeus californiensis) (pH 8, 50°C) (Vega-Villasante et al, 1995), etc.…”

Section: Effect Of Temperature and Phmentioning

confidence: 69%

Untitled

Pongsetkul¹,

Benjakul²,

Sumpavapol³

et al. 2017

Turk. J. Fish. Aquat. Sci.

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Autolysis of Acetes vulgaris and Macrobrachium lanchesteri was comparatively studied. Maximal autolytic activities were found at pH 7, 55°C for A. vulgaris and pH 8, 60°C for M. lanchesteri. Both shrimps dominantly contained serine proteases as indicated by the marked inhibition by PMSF and SBTI. When both shrimps were used for Kapi production and characterized, differences in characteristics as well as antioxidant activities were obtained. Kapi produced from A. vulgaris (KA) showed the higher degree of hydrolysis (15.93±0.51%), peroxide values (0.20±0.23 mg cumene peroxide/ kg sample) and TBARS value (0.55±0.16 mg MDA/ kg sample), compared with Kapi produced from M. lanchesteri (KM), indicating the higher protein degradation and lipid oxidation in this sample. Moreover, KA also possessed the higher antioxidative activities including ferric reducing antioxidant power (FRAP) (14.12±1.34 µmol TE/ g sample), chelating activity (3.21±0.05 µmol EE/ g sample), hydrogen peroxide (30.05±0.49 µmol TE/ g sample) and singlet oxygen scavenging activities (48.46±0.32 µmol EE/ g sample) than KM, except for DPPH and ABTS radical scavenging activities, which showed lower activity (P<0.05) and had no difference (P>0.05), respectively. Therefore, different levels and types of endogenous proteases in both shrimps determined the autolysis, characteristics and antioxidative properties of resulting Kapi.

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On the purification and characterization of three anionic, serine-type peptide hydrolases from antarctic krill, Euphausia Superba

Cited by 51 publications

References 16 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)

Structure of a Non-psychrophilic Trypsin from a Cold-Adapted Fish Species

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