Expression of Lactate Dehydrogenase in Aspergillus niger for L-Lactic Acid Production.

PLoS One

Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Mumbai, Maharashtra, India.

Published: June 2016

AI Article Synopsis

  • Different engineered organisms have faced challenges in producing L-lactate, with low yields at low pH and costly downstream processing being significant issues.
  • Aspergillus niger, known for its ability to produce citrate and tolerate acidic conditions, was found to lack reports on lactate production or functional lactate dehydrogenase (LDH), prompting a genetic investigation.
  • By utilizing the A. niger citrate synthase promoter to express mouse lactate dehydrogenase, the engineered C12 strain achieved 7.7 g/l of L-lactate from glucose in acidic conditions, marking A. niger as a promising platform for lactate production.

Article Abstract

Different engineered organisms have been used to produce L-lactate. Poor yields of lactate at low pH and expensive downstream processing remain as bottlenecks. Aspergillus niger is a prolific citrate producer and a remarkably acid tolerant fungus. Neither a functional lactate dehydrogenase (LDH) from nor lactate production by A. niger is reported. Its genome was also investigated for the presence of a functional ldh. The endogenous A. niger citrate synthase promoter relevant to A. niger acidogenic metabolism was employed to drive constitutive expression of mouse lactate dehydrogenase (mldhA). An appraisal of different branches of the A. niger pyruvate node guided the choice of mldhA for heterologous expression. A high copy number transformant C12 strain, displaying highest LDH specific activity, was analyzed under different growth conditions. The C12 strain produced 7.7 g/l of extracellular L-lactate from 60 g/l of glucose, in non-neutralizing minimal media. Significantly, lactate and citrate accumulated under two different growth conditions. Already an established acidogenic platform, A. niger now promises to be a valuable host for lactate production.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4684279PMC
http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0145459PLOS

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