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Literature summary extracted from

  • Zhang, Y.; He, S.; Simpson, B.K.
    A cold active transglutaminase from Antarctic krill (Euphausia superba) purification, characterization and application in the modification of cold-set gelatin gel (2017), Food Chem., 232, 155-162 .
    View publication on PubMed

Application

EC Number Application Comment Organism
2.3.2.13 food industry gelatin is a soluble protein prepared by partial hydrolysis of collagen with widespread utility in food industry, and TGase has been used to enzymatically modify gelatin by forming cross-links to enhance its rheological properties. Gelatin can set to elastic gel on cooling below 35°C from disordered molecules to ordered network predominantly by hydrogen bonds, where TGase introduces additional covalent cross-linkages to improve gelation. Addition of TGase from Euphausia superba at 0.1 U/mg increases the gel strength, setting temperature, setting time, and melting temperature of cold-set gelatin gel. Properties of gelatin with addition of TGase purified from Antarctic krill, overview Euphausia superba

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.2.13 (NH4)2SO4 65.58% activity remaining at 10 mM Euphausia superba
2.3.2.13 Ba2+ 22.55% activity remaining at 10 mM Euphausia superba
2.3.2.13 Cu2+ 19.78% activity remaining at 10 mM Euphausia superba
2.3.2.13 EGTA 42.93% activity remaining at 10 mM Euphausia superba
2.3.2.13 iodoacetic acid 28.75% activity remaining at 10 mM Euphausia superba
2.3.2.13 Mg2+ 53.52% activity remaining at 10 mM Euphausia superba
2.3.2.13 Mn2+ 30.65% activity remaining at 10 mM Euphausia superba
2.3.2.13 NEM 34.38% activity remaining at 10 mM Euphausia superba
2.3.2.13 PCMB 1.62% activity remaining at 10 mM Euphausia superba
2.3.2.13 PMSF 40.79% activity remaining at 10 mM Euphausia superba
2.3.2.13 Zn2+ 20.12% activity remaining at 10 mM Euphausia superba

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.3.2.13 Ca2+ required, best at 10 mM Euphausia superba
2.3.2.13 Na+ activates, best at 1.8 mM Euphausia superba

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.2.13 protein glutamine + alkylamine Euphausia superba
-
 protein N5-alkylglutamine + NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.13 Euphausia superba
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.2.13 native enzyme about 10.3fold from Antarctic krill by ammonium sulfate fractionation, dialysis, ultrafiltration, and cation exchange chromatography, followed by a second ultrafiltration, precipitation with 80-90% ethanol, and freeze drying Euphausia superba

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3.2.13 53.518
-
 purified native enzyme, pH 7.5, 25°C Euphausia superba

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.13 gelatin glutamine + alkylamine
-
 Euphausia superba gelatin N5-alkylglutamine + NH3
-
 ?
2.3.2.13 N,N'-dimethyl casein glutamine + monodansylcadaverine the enzymatic activity is determined by measuring the fluorescence of monodansylcadaverine (MDC) crosslinking to N,N'-dimethyl casein (DMC) exposure. Fluorescence intensity of MDC incorporated into DMC is measured at excitation and emission wavelengths of 350 and 480 nm, respectively Euphausia superba ?
-
 ?
2.3.2.13 protein glutamine + alkylamine
-
 Euphausia superba protein N5-alkylglutamine + NH3
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.2.13 ? x * 78000, SDS-PAGE Euphausia superba

Synonyms

EC Number Synonyms Comment Organism
2.3.2.13 cold active transglutaminase
-
 Euphausia superba
2.3.2.13 TGase
-
 Euphausia superba
2.3.2.13 transglutaminase
-
 Euphausia superba

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.2.13
-
 10
-
 Euphausia superba

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.3.2.13 additional information
-
 cold-active enzymes have more flexible structures compared with their mesophilic and thermophilic counterparts. This flexibility contributes to the high catalytic activity as well as the high temperature instability of cold active enzymes Euphausia superba
2.3.2.13
-
 65 most active at 0-10°C, the relative activity at 45°C, 55°C and 65°C declined to 50%, 47% and 44%, respectively Euphausia superba

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.2.13 8 9
-
 Euphausia superba

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.3.2.13 6 9 80-100% of maximal activity within this range Euphausia superba

General Information

EC Number General Information Comment Organism
2.3.2.13 additional information addition of TGase at 0.1 U/mg increases the gel strength, setting temperature, setting time, and melting temperature of cold-set gelatin gel Euphausia superba