Effects of using high solid concentrations on the synthesis of γ-[Glu](n≥1)-Gln catalyzed by glutaminase from Bacillus amyloliquefaciens were examined in this study. An increment in solid concentration from 10% to 50% (w/w) increased the extent of synthesis of γ-[Glu](n≥1)-Gln, based on the analyses of amino acid composition and amino nitrogen content. Size-exclusion high-performance liquid chromatography analysis revealed an increase in molecular mass of γ-[Glu](n≥1)-Gln resulting from the increase of solid concentration from 10% to 50% (w/w). UPLC-Q-TOF-MS/MS analysis showed that the enzymatic reaction mixtures post γ-glutamyl transpeptidation contained γ-Glu-Gln, γ-Glu-Glu-Gln, γ-Glu-Glu-Glu-Gln, γ-Glu-Glu-Glu-Glu-Gln and γ-Glu-Glu-Glu-Glu-Glu-Gln. The intensity of each γ-[Glu](n=1,2,3,4,5)-Gln produced at a solid concentration of 50% (w/w) was higher than that at 10% (w/w). These findings indicated the potential of such an energy- and water-efficient approach for synthesizing γ-[Glu](n≥1)-Gln at high solid concentrations.
Keywords: Enzymatic synthesis; Glutaminase; High solid concentration; γ-[Glu]((n)(≥)(1))-Gln.
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