Remaining activity (%)
100 80 60 40 20 0
Crangon
crangon Pagurus
bernhardus Cancer pagurus
Euphausia superba Pandalus
montagui
Remaining activity (%)
100 90 80 70 60 50
Crangon crangon
Cysteine
Cysteine Proteinases Proteinases vs. vs. Serine Proteinases: Serine Proteinases:
Traits of Protein Utilization in Crustaceans Traits of Protein Utilization in Crustaceans
Mathias
Mathias Teschke Teschke • • Reinhard Saborowski Reinhard Saborowski
University of Hamburg
University of Hamburg • • AWI – AWI – Marine Station - Marine Station - Helgoland Helgoland
The utilization of dietary proteins is facilitated by a set of digestive peptide hydrolases. In crustaceans these are often dominated by „trypsin- like“ serine proteinases. In addition, highly active cysteine- and metallo proteinases were identified. However, the distribution of proteinases
classes is diverse between species. In order to reveal possible traits in the preferences of digestive proteinases between crustaceans we investigated the distribution of serine- and cysteine proteinases in the midgut glands of a set of ecologically important species by activity
measurements and inhibitor assays.
E 64, a specific inhibitor of cysteine proteinases supressed total proteinase activity by more than 70 % in Crangon spec.. In P. bernhardus, C. pagurus and E.superba, however, E 64 caused almost no
loss of activity.
All investigated crustaceans showed high total proteinase activities which did not differ between species.
In contrast, the serine proteinase inhibitor AEBSF had only little effect in Crangon spec.
but was most effective in P.bernhardus, C.
pagurus and E. superba.
CONCLUSIONS
The investigated set of crustaceans showed different preferences of digestive proteinase classes The expression of proteinase classes could be related to the different life style and feeding habits of these species
Proteinase classes may reflect phylogenetic patterns: Caridea express predominantly cysteine proteinases, while Anomura, Brachyura and Euphausiacea prefer serine proteinases.
In FPLC-fractions of C. crangon- extracts we detected a broad activity-peak of the cysteine proteinase cathepsin L while simultaneously no
trypsin activity was found. In contrast four distinct peaks of trypsin activity were detected in FPLC-fractions of E. superba which are matched
closely with the elution profile of total proteinase activity.
Pagurus Pagurus bernhardusbernhardus A
Anomuranomura
Cancer Cancer paguruspagurus Brachyura Brachyura
Euphausia superba Euphausia superba Euphausiacea Euphausiacea
Crangon crangon, C.
Crangon crangon, C. allmani allmani CarideaCaridea Pandalus montaguiPandalus montagui, , CarideaCaridea
Trypsin activities, in contrast, differed significantly between species. Lowest activities appeared in Crangon
spec. while highest trypsin activity was present in Antarctic krill.
Spec. aktivity (dE366 min-1g-1 fw)
0,0 0,1 0,2 0,3 0,4 0,5 0,6
Crangon crangon
Crangon allmani
Pandalus montagui
Pagurus bernhardus
Cancer pagurus
Euphausia superba
Spec. Trypsin aktivity (Ug-1 fw)
0 1 2 3 4 5 6 7 8 9 10
a a a b
Crangon crangon
Crangon allmani
Pandalus montagui
Pagurus bernhardus
Cancer pagurus
Euphausia superba
b c
Fraction
0 10 20 30 40 50 60 70
Protein, Aktivität, Gradient (%)
0 20 40 60 80
100 Protein Gesamtproteinase
Cathepsin L Gradient
E64
AEBSF
Trypsin Total proteinase
Fraction
0 10 20 30 40 50 60 70
Gradient, Protein, Activity (%)
0 20 40 60 80 100 Gradient
Protein total Protease Trypsin
