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Enhanced succinic acid production by Mannheimia employing optimal malate dehydrogenase
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Journal Article
Enhanced succinic acid production by Mannheimia employing optimal malate dehydrogenase
2020
Overview
Succinic acid (SA), a dicarboxylic acid of industrial importance, can be efficiently produced by metabolically engineered
Mannheimia succiniciproducens
. Malate dehydrogenase (MDH) is one of the key enzymes for SA production, but has not been well characterized. Here we report biochemical and structural analyses of various MDHs and development of hyper-SA producing
M. succiniciproducens
by introducing the best MDH.
Corynebacterium glutamicum
MDH (
Cg
MDH) shows the highest specific activity and least substrate inhibition, whereas
M. succiniciproducens
MDH (
Ms
MDH) shows low specific activity at physiological pH and strong uncompetitive inhibition toward oxaloacetate (
ki
of 67.4 and 588.9 μM for
Ms
MDH and
Cg
MDH, respectively). Structural comparison of the two MDHs reveals a key residue influencing the specific activity and susceptibility to substrate inhibition. A high-inoculum fed-batch fermentation of the final strain expressing
cgmdh
produces 134.25 g L
−1
of SA with the maximum productivity of 21.3 g L
−1
h
−1
, demonstrating the importance of enzyme optimization in strain development.
Malate dehydrogenase (MDH) is one of the key enzymes for succinic acid (SA) bioproduction. Here, the authors report biochemical and structural analyses of various MDHs to reveal amino acids influencing the specific activity and susceptibility to substrate inhibition, and achieve industrial-level SA production.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 82/80
/ 82/83
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Corynebacterium glutamicum - enzymology
/ Corynebacterium glutamicum - genetics
/ Enzymes
/ Humanities and Social Sciences
/ Inoculum
/ Kinetics
/ Malate Dehydrogenase - chemistry
/ Malate Dehydrogenase - genetics
/ Malate Dehydrogenase - metabolism
/ Oxaloacetic Acid - metabolism
/ Pasteurellaceae - enzymology
/ Pasteurellaceae - metabolism
/ Recombinant Proteins - chemistry
/ Recombinant Proteins - genetics
/ Recombinant Proteins - metabolism
/ Science
