Characterization of a cold-active transglutaminase from a crayfish, Pacifastacus leniusculus.

Sirikharin R, Söderhäll I, Söderhäll K

Fish Shellfish Immunol. 80 (-) 546-549 [2018-09-00; online 2018-06-27]

Transglutaminase (TGase) from signal crayfish (Pacifastacus leniusculus) and its activity at low temperatures was studied. TGase is an abundant protein in the hematopoietic (HPT) cells and this tissue was used for TGase enzyme preparation. The optimal temperature and pH for the activity of crayfish TGase were determined. We found that TGase activity at 4 °C showed nearly the same activity as at a temperature of 22 °C. TGase activity from crayfish was compared with guinea pig liver TGase activity at 4 °C and the crayfish TGase displayed a higher activity while guinea pig liver TGase had a very low activity at this low temperature. By comparing kinetic parameters to guinea pig liver TGase, the results showed that a high activity of crayfish TGase was due to a decreasing K m value for pentylamine as a substrate, while it did not affect the kcat value (at 22 °C). The amino acid sequences of a krill and a crayfish TGase, which both are cold adapted, do not give any clue to why these two enzymes are cold-adapted. These results demonstrate that crayfish TGase is adapted to have significant activity at low temperatures and since crayfish are living in quite cold waters this is an interesting adaptation of this enzyme.

Affiliated researcher

QC bibliography QC xrefs

PubMed 29960064

DOI 10.1016/j.fsi.2018.06.042

Crossref 10.1016/j.fsi.2018.06.042

S1050-4648(18)30383-8