Application | Comment | Organism |
---|---|---|
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 | Comment | Organism | Structure |
---|---|---|---|
(NH4)2SO4 | 65.58% activity remaining at 10 mM | Euphausia superba | |
Ba2+ | 22.55% activity remaining at 10 mM | Euphausia superba | |
Cu2+ | 19.78% activity remaining at 10 mM | Euphausia superba | |
EGTA | 42.93% activity remaining at 10 mM | Euphausia superba | |
iodoacetic acid | 28.75% activity remaining at 10 mM | Euphausia superba | |
Mg2+ | 53.52% activity remaining at 10 mM | Euphausia superba | |
Mn2+ | 30.65% activity remaining at 10 mM | Euphausia superba | |
NEM | 34.38% activity remaining at 10 mM | Euphausia superba | |
PCMB | 1.62% activity remaining at 10 mM | Euphausia superba | |
PMSF | 40.79% activity remaining at 10 mM | Euphausia superba | |
Zn2+ | 20.12% activity remaining at 10 mM | Euphausia superba |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | required, best at 10 mM | Euphausia superba | |
Na+ | activates, best at 1.8 mM | Euphausia superba |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
protein glutamine + alkylamine | Euphausia superba | - |
protein N5-alkylglutamine + NH3 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Euphausia superba | - |
- |
- |
Purification (Comment) | Organism |
---|---|
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 Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
53.518 | - |
purified native enzyme, pH 7.5, 25°C | Euphausia superba |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
gelatin glutamine + alkylamine | - |
Euphausia superba | gelatin N5-alkylglutamine + NH3 | - |
? | |
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 | ? | - |
? | |
protein glutamine + alkylamine | - |
Euphausia superba | protein N5-alkylglutamine + NH3 | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 78000, SDS-PAGE | Euphausia superba |
Synonyms | Comment | Organism |
---|---|---|
cold active transglutaminase | - |
Euphausia superba |
TGase | - |
Euphausia superba |
transglutaminase | - |
Euphausia superba |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
- |
10 | - |
Euphausia superba |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
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 |
- |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | 9 | - |
Euphausia superba |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6 | 9 | 80-100% of maximal activity within this range | Euphausia superba |
General Information | Comment | Organism |
---|---|---|
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 |