Isolation and characterization of a salt-tolerant γ-glutamyl transpeptidase from xerophilic Aspergillus sydowii.

Xerophilic Aspergillus molds isolated from halo-alkaliphilic and dry environments are attractive genetic resources for obtaining salt- and osmo-adaptive enzymes. A. sydowii MA0196 secreted the largest amount of γ-glutamyl transpeptidase (GGT) during solid-state fermentation at a low initial water activity (a w = 0.85). Gel filtration analysis revealed that the molecular mass of the purified native enzyme (MA0196 GGT) was 120 kDa. SDS-PAGE analysis showed that MA0196 GGT consists of two subunits with molecular masses of 56.4 and 33 kDa, indicating production from a proenzyme via autoproteolysis. Deglycosylation of the subunits by N-glycosidase F yielded 40.9 and 19.6 kDa species. MA0196 GGT retained transpeptidase and hydrolysis activities and their catalytic efficiency (k cat/K m) under high salt and low water activity. The enzyme displayed broad substrate specificity toward γ-glutamyl acceptors such as amino acids and the imidazole dipeptides, carnosine and anserine. Carnosine and L-glutamine were converted into γ-glutamyl-β-alanyl-L-histidine by MA0196 GGT with a 32.9% yield in the presence of 2% (v/v) dimethyl sulfoxide. Phylogenetic analysis indicated that MA0196 GGT forms a distinct lineage from A. oryzae and A. sojae GGTs. These excellent properties indicate that MA0196 GGT can be used in salted fermentation and for producing bioactive peptides. Supplementary Information: The online version contains supplementary material available at 10.1007/s13205-022-03259-3. © King Abdulaziz City for Science and Technology 2022, Springer Nature or its licensor holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.