EC Number | Application | Comment | Organism |
---|---|---|---|
2.3.2.13 | biotechnology | enzyme TGZ treatment effectively improves the textural properties of milk protein concentrate (MPC) gel at strength level and water-holding capacity. Optimal texture of MPC gel is achieved after TGZ treatment using 2 U/g TGZ for 2 h at 35°C and pH 7.0, method evaluation and optimization, overview | Zea mays |
EC Number | Cloned (Comment) | Organism |
---|---|---|
2.3.2.13 | gene tgz, recombinant expression of wild-type and codon-optimized enzyme in Pichia pastoris strain GS115 under control of two different promoter types, PFLD1 and PTEF1. Higher expression of TGZ is obtained under the induction of PFLD1 | Zea mays |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.3.2.13 | Ca2+ | required | Zea mays |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.2.13 | protein glutamine + alkylamine | Zea mays | - |
protein N5-alkylglutamine + NH3 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.2.13 | Zea mays | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.3.2.13 | recombinant expression of wild-type and codon-optimized, engineered enzymes from Pichia pastoris strain GS115 by ultrafiltration, gel filtration, anion exchange chromatography, and a second step of gel filtration | Zea mays |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
2.3.2.13 | 0.32 | - |
recombinant wild-type enzyme, about, pH 7.0, 30°C | Zea mays |
2.3.2.13 | 0.889 | - |
recombinant engineered and optimized enzyme, pH 7.0, 30°C | Zea mays |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.2.13 | casein glutamine + hydroxylamine | - |
Zea mays | casein N5-hydroxyglutamine + NH3 | - |
? | |
2.3.2.13 | N-CBZ-Glu-Gly + hydroxylamine | - |
Zea mays | CBZ-Glu-(gamma-monohydroxamate)-Gly + NH3 | - |
? | |
2.3.2.13 | protein glutamine + alkylamine | - |
Zea mays | protein N5-alkylglutamine + NH3 | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.3.2.13 | TGase | - |
Zea mays |
2.3.2.13 | TGZ | - |
Zea mays |
2.3.2.13 | transglutaminase | - |
Zea mays |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.3.2.13 | 30 | - |
assay at | Zea mays |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.3.2.13 | 7 | - |
assay at | Zea mays |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.3.2.13 | physiological function | transglutaminase (TGase) catalyzes post-translational modification of proteins by gamma-glutamyl-epsilon-lysine chain links, covalent conjugation of polyamines, and deamidation. Analysis of cross-linking effect of recombinant TGZ on the properties of acid-induced milk protein concentrate (MPC) gel | Zea mays |