gamma-Glutamyl-peptides are frequently endowed with biological activities. In this work, "kokumi peptides " such as gamma- glutamyl-methionine (1) and gamma-glutamyl-(S)-allyl-cysteine (2), as well as the neuroprotective gamma-glutamyl-taurine (3) and the antioxidant ophthalmic acid (4), were synthesized through an enzymatic transpeptidation reaction catalyzed by the gamma-glutamyl transferase from Bacillus subtilis (BsGGT) using glutamine as the gamma-glutamyl donor. BsGGT was covalently immobilized on glyoxylagarose resulting in high protein immobilization yield and activity recovery (> 95%). Compounds 1-4 were obtained in moderate yields (19-40%, 5-10 g/L) with a variable purity depending on the presence of the main byproduct (gamma-glutamyl-glutamine, 0-16%). To achieve process intensification and better control of side reactions, the synthesis of 2 was moved from batch to continuous flow. The specific productivity was 1.5 times higher than that in batch synthesis (13.7 mu mol/min*g), but it was not accompanied by a paralleled improvement of the impurity profile.

From Batch to Continuous Flow Bioprocessing: Use of an Immobilized γ-Glutamyl Transferase from B. subtilis for the Synthesis of Biologically Active Peptide Derivatives / M.S. Robescu, F. Annunziata, V. Somma, C. Calvio, C.F. Morelli, G. Speranza, L. Tamborini, D. Ubiali, A. Pinto, T. Bavaro. - In: JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY. - ISSN 0021-8561. - 70:42(2022 Oct 26), pp. 13692-13699. [10.1021/acs.jafc.2c03702]

From Batch to Continuous Flow Bioprocessing: Use of an Immobilized γ-Glutamyl Transferase from B. subtilis for the Synthesis of Biologically Active Peptide Derivatives

F. Annunziata;V. Somma;C.F. Morelli;G. Speranza;L. Tamborini;A. Pinto
;
2022

Abstract

gamma-Glutamyl-peptides are frequently endowed with biological activities. In this work, "kokumi peptides " such as gamma- glutamyl-methionine (1) and gamma-glutamyl-(S)-allyl-cysteine (2), as well as the neuroprotective gamma-glutamyl-taurine (3) and the antioxidant ophthalmic acid (4), were synthesized through an enzymatic transpeptidation reaction catalyzed by the gamma-glutamyl transferase from Bacillus subtilis (BsGGT) using glutamine as the gamma-glutamyl donor. BsGGT was covalently immobilized on glyoxylagarose resulting in high protein immobilization yield and activity recovery (> 95%). Compounds 1-4 were obtained in moderate yields (19-40%, 5-10 g/L) with a variable purity depending on the presence of the main byproduct (gamma-glutamyl-glutamine, 0-16%). To achieve process intensification and better control of side reactions, the synthesis of 2 was moved from batch to continuous flow. The specific productivity was 1.5 times higher than that in batch synthesis (13.7 mu mol/min*g), but it was not accompanied by a paralleled improvement of the impurity profile.
Bacillus subtilis; enzyme immobilization; flow chemistry; kokumi peptides; γ-glutamyl transferase
Settore CHIM/06 - Chimica Organica
CAR_RIC17CMORE_01 - Value-added products through biocatalysis: TAILored GLUtamyl TRANsferases - MORELLI, CARLO - CAR_RIC - Bandi Fondazione Cariplo - 2017
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/943849
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