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. 
Chow, Jennifer 
Streit, Wolfgang R. 
Wohlgemuth, Roland 
Liese, Andreas  
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 2.7.1.30) 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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