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Water reuse in the L ‐lysine fermentation process
Author(s) -
Hsiao TzuYin,
Glatz Charles E.
Publication year - 2000
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/(sici)1097-0290(19960205)49:3<341::aid-bit13>3.0.co;2-h
Subject(s) - effluent , fermentation , chemistry , corynebacterium glutamicum , ammonium , chromatography , pulp and paper industry , lysine , ion exchange resin , wastewater , ion exchange , food science , waste management , biochemistry , organic chemistry , ion , amino acid , engineering , gene
L ‐Lysine is produced commercially by fermentation. As is typical for fermentation processes, a large amount of liquid waste is generated. To minimize the waste, which is mostly the broth effluent from the cation exchange column used for l ‐lysine recovery, we investigated a strategy of recycling a large fraction of this broth effluent to the subsequent fermentation. This was done on a labscale process with Corynebacterium glutamicum ATCC 21253 as the l ‐lysine‐producing organism. Broth effluent from a fermentation in a defined medium was able to replace 75% of the water for the subsequent batch; this recycle ratio was maintained for three sequential batches without affecting cell mass and l ‐lysine production. Broth effluent was recycled at 50% recycle ratio in a fermentation in a complex medium containing beet molasses. The first recycle batch had an 8% lower final l ‐lysine level, but 8% higher maximum cell mass. In addition to reducing the volume of liquid waste, this recycle strategy has the additional advantage of utilizing the ammonium desorbed from the ion‐exchange column as a nitrogen source in the recycle fermentation. The major problem of recycling the effluent from the complex medium was in the cation‐exchange operation, where column capacity was 17% lower for the recycle batch. The loss of column capacity probably results from the buildup of cations competing with l ‐lysine for binding. © 1996 John Wiley & Sons, Inc.