Cold active transglutaminase from antarctic Penicillium chrysogenum: Partial purification, characterization and potential application in food technology

GLODOWSKY, ALEJANDRO P.; MAC CORMACK, WALTER P.; RUBERTO, LUCAS A.; LEVIN, GUSTAVO J.; RUBERTO, LUCAS A.; LEVIN, GUSTAVO J.; MARTORELL, MARÍA MARTHA; MARTORELL, MARÍA MARTHA; GLODOWSKY, ALEJANDRO P.; MAC CORMACK, WALTER P.

Biocatalysis and Agricultural Biotechnology

Elsevier

Lugar: Amsterdam; Año: 2020 vol. 29 p. 1 - 7

1878-8181

A novel transglutaminase (TGase, EC 2.3.2.13) from antarctic Penicillium chrysogenum was partially purified using ammonium sulfate precipitation and anionic exchange chromatography. The final extract had a specific activity of 7.81 mU/mg, purification fold of 7.16, and a yield of 5.02%. The molecular weight was estimated to be 67 kDa by bioinformatic analysis and SDS - PAGE. Maximum TGase activity was observed at pH 8.0 and 30 °C, mesophilic conditions (near 40 °C) resulted in total inactivation. A slight improvement in TGase activity was observed in the presence of Ca 2+ , it increased to 127.78 ± 9.62% at 35 mM but return to normal values at higher concentrations. Additionally, the enzyme activity decreased progressively in the presence of EDTA and STPP suggesting that the enzyme is Ca 2+ dependent but this cofactor is being supplied by the fermented substrate. The partially purified TGase was used as an additive to modify the rheology of a cold - set gelatin gel achieving an in crease in the gel strength and gumminess of 32.25% and 30.50% respectively.