Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.3.2.13 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
Search for more literature for 2.3.2.13

Application

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

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

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Euphausia superba
-
-
-

Purification (Commentary)

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 [micromol/min/mg]

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 and Products (Substrate)

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

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

Synonyms

Synonyms Comment Organism
cold active transglutaminase
-
 Euphausia superba
TGase
-
 Euphausia superba
transglutaminase
-
 Euphausia superba

Temperature Optimum [°C]

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

Temperature Range [°C]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
8 9
-
 Euphausia superba

pH Range

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

General Information

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