|Publisher DOI:||10.1002/biot.201600625||Title:||Bioreaction engineering leading to efficient synthesis of L-glyceraldehyd-3-phosphate||Language:||English||Authors:||Molla, Getachew Shibabaw
Kinfu, Birhanu M.
Streit, Wolfgang R.
|Keywords:||Glycerol kinase;L-Glyceraldehyde-3-phosphate instability;Mg to ATP ratio 2+;Reaction kinetics;Reactor simulation||Issue Date:||19-Dec-2016||Publisher:||Wiley-VCH||Source:||Biotechnology Journal 3 (12): 1600625 (2017-03-01)||Journal or Series Name:||Biotechnology journal||Abstract (english):||Enantiopure L-glyceraldehyde-3-phosphate (L-GAP) is a useful building block in natural biological and synthetic processes. A biocatalytic process using glycerol kinase from Cellulomonas sp. (EC 18.104.22.168) catalyzed phosphorylation of L-glyceraldehyde (L-GA) by ATP is used for the synthesis of L-GAP. L-GAP has a half-life of 6.86 h under reaction conditions. The activity of this enzyme depends on the Mg2+ to ATP molar ratio showing maximum activity at the optimum molar ratio of 0.7. A kinetic model is developed and validated showing a 2D correlation of 99.9% between experimental and numerical data matrices. The enzyme exhibits inhibition by ADP, AMP, methylglyoxal and Ca2+, but not by L-GAP and inorganic orthophosphate. Moreover, equal amount of Ca2+ exerts a different degree of inhibition relative to the activity without the addition of Ca2+ depending on the Mg2+ to ATP molar ratio. If the Mg2+ to ATP molar ratio is set to be at the optimum value or less, inorganic hexametaphosphate (PPi6) suppresses the enzyme activity; otherwise PPi6 enhances the enzyme activity. Based on reaction engineering parameters such as conversion, selectivity and specific productivity, evaluation of different reactor types reveals that batchwise operation via stirred-tank reactor is the most efficient process for the synthesis of L-GAP.||URI:||http://hdl.handle.net/11420/3159||ISSN:||1860-7314||Institute:||Technische Biokatalyse V-6||Type:||(wissenschaftlicher) Artikel|
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