History of glutamate production1–3
Chiaki Sano
ABSTRACT
In 1907 Kikunae Ikeda, a professor at the Tokyo Imperial Univer-
sity, began his research to identify the umami component in kelp.
Within a year, he had succeeded in isolating, purifying, and iden-
tifying the principal component of umami and quickly obtained
a production patent. In 1909 Saburosuke Suzuki, an entrepre-
neur, and Ikeda began the industrial production of monosodium
L-glutamate (MSG). The first industrial production process was
an extraction method in which vegetable proteins were treated
with hydrochloric acid to disrupt peptide bonds. L-Glutamic acid
hydrochloride was then isolated from this material and purified as
MSG. Initial production of MSG was limited because of the
technical drawbacks of this method. Better methods did not
emerge until the 1950s. One of these was direct chemical syn-
thesis, which was used from 1962 to 1973. In this procedure,
acrylonitrile was the starting material, and optical resolution of
DL-glutamic acid was achieved by preferential crystallization. In
1956 a direct fermentation method to produce glutamate was in-
troduced. The advantages of the fermentation method (eg, reduc-
tion of production costs and environmental load) were large
enough to cause all glutamate manufacturers to shift to fermen-
tation. Today, total world production of MSG by fermentation is
estimated to be 2 million tons/y (2 billion kg/y). However, future
production growth will likely require further innovation. Am
J Clin Nutr 2009;90(suppl):728S–32S.
INTRODUCTION
In 1907 Kikunae Ikeda began a research project to identify the
substance in kelp (Laminariaceae) that produced a unique taste
favored in soup stocks in Japan. His research was based on the
hypothesis that one or more taste substances may exist in kelp
that could not be categorized as bitter, sour, salty, or sweet (the
known basic tastes at the time). He named this putative fifth
basic taste umami. More generally, Ikeda hoped that, if suc-
cessful, the results of his research might have a commercial
application, such as in a seasoning that would contribute to the
improvement of human nutrition in Japan. In 1908 he identified
the umami taste component of kelp as L-glutamate. He filed
a patent claim for a process to produce a new seasoning con-
sisting mainly of a salt of L-glutamic acid (1). Saburousuke
Suzuki, a well-known entrepreneur in the chemical and phar-
maceutical industry, then began a collaboration with Ikeda to
produce and commercialize the new seasoning. In 1909 this
seasoning was named AJI-NO-MOTO and was registered as
a trademark.
728S Am J Clin Nutr 2009;90(suppl):728S–32S. Printed in USA. Ó 2009 American Society for Nutrition
THE EXTRACTION METHOD: THE FIRST INDUSTRIAL
PRODUCTION METHOD
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The development of an industrial production method began in
December 1908. Because this was the first attempt to produce
amino acids on an industrial scale, the absence of experience
made the development process very challenging. The early
production process consisted of 3 parts: extraction, isolation, and
purification (2).
Extraction
Ikeda proposed using wheat gluten as the source of glutamate
because it has the highest content of L-glutamine among industrially
available raw materials. L-Glutamine becomes L-glutamic acid
after protein hydrolysis; the total glutamate content (glutamate +
glutamine) of hydrolyzed wheat gluten is .30 g/100 g protein
(3). Gluten was first separated from wheat flour by washing the
starch from dough. The resulting crude gluten was transferred to
pottery vessels (termed Domyoji-game), combined with hydro-
chloric acid, and heated for 20 h. A variety of vessels were
tested, and old-fashioned Domyoji-game (Figure 1) proved to
be the most resistant to hydrochloric acid and heat. The protein
hydrolysate was filtered to eliminate a black residue (termed
humus) that resulted from the reaction of amino acids with
carbohydrates and was then returned to the Domyoji-game to be
concentrated for 24 h. This concentrate was transferred to an-
other Domyoji-game and stored for 1 mo to allow the L-glutamic
acid hydrochloride salt to crystallize.
The crystallization of L-glutamic acid hydrochloride proved
very effective for extracting L-glutamate from the hydrolysate
because it is the only amino acid salt in the hydrolysate with a
very low solubility in concentrated hydrochloric acid (Figure 2).
In addition, the salt crystal itself has very high selectivity against
other amino acids: L-glutamic acid molecules stack along the
crystal’s a-axis, linking a-amino N-H-Cl and c-carboxyl
O-H-Cl hydrogen bonds (6). Structurally, it is difficult for other
amino acids to insert themselves into these growing crystals,
which makes the crystallization process also a process of
1
From the Technology and Engineering Center, Ajinomoto Co, Tokyo,
Japan.
2
Presented at the “100th Anniversary Symposium of Umami Discovery:
The Roles of Glutamate in Taste, Gastrointestinal Function, Metabolism, and
Physiology,” held in Tokyo, Japan, 10–13 September 2008.
3
Address correspondence and reprint requests to C Sano, Technology
and Engineering Center Ajinomoto Co, 1-1 Suzuki-cho, Kawasaki-ku,
Kawasaki-shi 210-8681, Japan. E-mail: chiaki_sano@ajinomoto.com.
First published online July 29, 2009; doi: 10.3945/ajcn.2009.27462F.
 HISTORY OF GLUTAMATE PRODUCTION
FIGURE 1. Hydrolysis using Domyoji-game vessels in the Zushi factory
(Kanagawa Prefecture, Japan). Wheat gluten was placed into Domyoji-game
pots by shovel, and concentrated hydrochloric acid was added. The slurry
was stirred with a pole and heated for 20 h to promote hydrolysis. The
Domyoji-game pots were made in Tokoyame (Aichi prefecture), Japan.
Tokoyame was famous for the manufacture of ceramic wares from very
fine, local clay. This clay produced ceramic pots that were highly resistant
to acid and high temperature. Reproduced with permission from reference 4.
(partial) purification. The unusual crystal structure also limits
the extent to which other compounds in the gluten hydrolysate
(coloring agents, other organic acids) become incorporated into
growing crystals or otherwise inhibit crystallization. By this
simple crystallization process, L-glutamate could thus be re-
covered from the hydrolysate at a high yield and with improved
purity. Nevertheless, it should be noted that this early process
was very hazardous because it exposed workers and facilities to
corrosive conditions (hydrogen chloride gas was released into
the local atmosphere).
Isolation
The crystals of L-glutamic acid hydrochloride were separated
from the liquid by filtration and redissolved in water. This so-
lution was again filtered to eliminate humus. The pH was then
adjusted to the isoelectric point of L-glutamic acid (pH 3.2) with
sodium or potassium hydroxide, and this solution was stored for
1 wk to allow L-glutamic acid to crystallize out. This step no-
tably increased the purity of the crystals for the following rea-
son. There are 2 polymorphs in L-glutamic acid crystals:
a metastable, granular a-form (7) and a stable, thin, platelike
b-form (8). The a-form grows better than the b-form in solutions
containing other amino acids. And, growing by its specific hy-
drogen bonding network, the dominant (001) face of the a-form
selectively incorporates L-glutamic acid molecules at both the
L-a-amino acid and the c-carboxyl residues (9). Because the
solution of the crude L-glutamic acid hydrochloride salt created
in the early production method (described above) still contained
other amino acids, the a-form of glutamic acid was the dominant
crystal formed at pH 3.2. Purity was improved because the
grown a-form crystals did not contain other amino acids.
Purification
The separated L-glutamic acid, a-form crystals were redis-
solved in water and placed into an enamel-jacketed ironware
729S
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FIGURE 2. Solubility of crystalline forms of glutamate at different
hydrogen ion concentrations in aqueous solution (35°C). The abscissa
indicates the pH of the solution. The ordinate indicates the solubility of
each crystal form of glutamate noted in the graph [glutamic acid
hydrochloride (L-GluHCl), glutamic acid (L-Glu), and monosodium
glutamate (L-GluNa)]. Lowering the pH of the solution (by the addition of
hydrochloric acid, +HCl in the graph) below 3.2 causes glutamic acid to
become more soluble until the pH reaches 0.45. As the pH continues to
decrease, the dominant component, now the hydrochloride salt of glutamic
acid, becomes increasingly insoluble and crystallizes out of the solution.
Reproduced with permission from reference 5.
vessel. Sodium bicarbonate was added to adjust the solution to
a neutral pH (litmus paper was used). This monosodium gluta-
mate solution was then decolorized by adding activated carbon
and filtering. The filtered, clear solution was then concentrated
by heating and cooled in the enameled vessel, causing mono-
sodium L-glutamate (MSG) crystals to form and precipitate.
When separated from the solution, the lump of MSG crystals
was cracked by hammer into a powder and separated from any
adhered mother liquor by centrifugation. The final MSG powder
was dried, sieved, and packed as the final product.
In March 1909 the first commercial MSG was successfully
produced. This early commercial material was a light-brown
powder of ’85% purity. When grown from a pure solution, the
shape of MSG crystals is a rhombic prism. Like the b-form, the
growth of MSG crystals is highly affected by the presence of
other amino acids. In the presence of increasing concentrations
of other amino acids (eg, L-alanine), the MSG crystal becomes
short and eventually a powder (10, 11). As the purification
technology improved over succeeding years, the form of the
product changed from a powder to rhombic prism crystals.
PROGRESS IN THE EXTRACTION METHOD
Production process
The problems with the initial hydrolysis process were largely
environmental, deriving from the corrosion of the materials in the
facility by the evolution of vapors containing hydrogen chloride
gas. To overcome such problems, a sulfuric acid hydrolysis
process was attempted. However, this approach failed, due to
amino acid racemization produced by the heat generated in the
neutralization process. Consequently, the method returned to the
use of hydrochloric acid. To scale up hydrolysis, the Domyoji-
game vessel was replaced by a granite stone chamber with
enameled steam pipes. Finally, in the 1930s, the corrosion
problem was completely solved through the development of
a rubber-lined iron vessel. This technology allowed hydrolysis to
730S
be performed in a completely sealed vessel with no leakage of
hydrogen chloride gas into the environment. This rubber-lining
technology was originally developed by Ajinomoto (Tokyo,
Japan), on the basis of Ikeda’s ideas, but was also introduced in
part by a German company. Although the sulfuric acid process
proved unsuccessful, lessons learned during its development and
testing nonetheless contributed to progress in process control,
including the use of pH meters during the crystallization and
neutralization processes. Optical rotation was also adopted to
measure the concentration of L-glutamate in the process liquor.
A new raw material and the effective use of co-products
From a business viewpoint, it was inevitable that a large
amount of co-product could be sold (the wheat starch separated
from wheat gluten was sold to the textile industry). In 1935, to
avoid a bottleneck in MSG production due to variable sales of
wheat starch, another protein source was developed for use in
MSG production, de-oiled soybean flakes. De-oiled soybean
flakes allowed diversification of co-products, which included
edible oil, alcohol, liquid seasoning, and fertilizer. The technical
optimization of the extraction process was achieved in 1937.
However, as production of MSG increased to meet demand, new
efforts were needed to ensure adequate supplies of raw materials,
successful movement of co-products, and proper management of
environmental issues. In the United States and Europe from the
1920s through the 1950s, the raw material need was met by
a waste product of the beet sugar industry: pyroglutamic acid
(5-oxo-L-proline), which was hydrolyzed to produce L-glutamic
acid (12). Nonetheless, after the World War II, it became in-
creasingly clear that new production processes would be re-
quired to meet the ever-increasing demand for MSG.
THE CHEMICAL SYNTHESIS METHOD
The development of a new production process in the 1950s
moved in 2 directions: chemical synthesis and fermentation.
Regarding chemical synthesis, 3 methods were developed. Two
were joint industry-university projects. One used acrylonitrile as
the starting material and was ultimately adopted (13) because the
polyacrylic fiber industry was launched in Japan in the mid-
1950s and acrylonitrile could be supplied at a cost lower than
that of other potential starting materials. In this process, the
synthesis gas (H2:CO; 2:1) was introduced to acrylonitrile to
yield 4-oxobutylo-nitrile (the “oxo-process”). Ammonium cya-
nide (obtained from ammonia, methane, and air) was then added
to synthesize 2-amino-pentane-di-nitrile (the Strecker process).
The di-nitrile was then hydrolyzed with caustic soda (sodium
hydroxide) to produce DL-disodium glutamate. The pH of the
reaction solution was then adjusted with sulfuric acid to prepare
for the optical resolution of glutamic acid.
As part of the development of the chemical synthesis process,
the optical resolution method was also developed to permit
separate crystallization of each optical isomer. In the improved
process, a solution of the racemic mixture of glutamic acid was
fed to L-and D-glutamic acid seed crystals that were separated by
a screen in an oval-shaped crystallization tank (14). Because
each seed crystal enables the crystallization of only its optical
isomer, each isomer could be grown and centrifuged separately.
This optical resolution method was established by finding the
SANO
conditions at which each optical isomer has a higher crystal
growth rate than DL-glutamic acid anhydride crystals and a lower
solubility than DL-glutamic acid monohydrate crystals. The re-
sulting L-glutamic acid crystals were then neutralized and pro-
cessed to MSG by using existing methods. The D-form crystals
were then reheated to create racemic compounds and subjected
again to the optical isomer separation procedure. The chemical
synthesis method started commercial production in 1961 and
ended in 1973, with maximum production reaching 1200 tons/mo
(1.2 million kg/mo).
FERMENTATION METHOD
The fermentation method is a production process in which
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a specific amino acid is synthesized in large amounts by a spe-
cially selected microorganism in culture. The selected microor-
ganism is cultured with carbohydrates and ammonia and releases
the L-form of the amino acid into the culture medium. The cell
produces glutamate from 2-oxo-glutarate (2-oxo-pentanedioic
acid) by reductive ammonia fixation that uses the enzyme glu-
tamate dehydrogenase, a normal cellular constituent. In 1956
Kyowa Hakko Kogyo Co Ltd succeeded in developing the
first industrial fermentation technology for L-glutamate. The
L-glutamate-producing bacterium was reported in 1957 by Ki-
noshita et al (15). Since that report, many bacteria useful in
glutamate production have been isolated, including Co-
rynebacterium glutamicum, Brevibacterium lactofermentum,
and Brevibacterium flavum. These glutamate-producing bacteria
are all coryneform bacteria, which are gram positive, non-
spore-forming, and nonmotile and require biotin for growth.
Glutamate accumulation in the medium occurs only under bi-
otin-limiting conditions. The requirement for biotin limitation
prevented the use of standard raw materials such as sugar mo-
lasses because they contained biotin. Significant efforts were
thus expended to overcome this difficulty. Ultimately, methods
were discovered, such as the addition of a surfactant or of
penicillin or the use of microorganisms auxotrophic for glycerol
or oleate, that allowed the bacteria to produce large amounts of
glutamate without biotin limitation.
Currently, despite such positive developments in fermentation
methods, it is curious that the mechanism of excessive glutamate
production by such microorganisms is not understood. The first
model, proposed in the 1960s, invoked a “leaky” cell membrane
hypothesis, which allowed glutamate to leak into the medium as it
was produced by the cell. The intracellular reaction was thus
pulled toward glutamate synthesis as product was lost from the
cell. But this hypothesis was discarded because investigators
noted that leakage was specific to glutamate and occurred against
a concentration gradient (16). A subsequent hypothesis suggested
the existence of an active transport mechanism in glutamate-
producing cells that exports the amino acid into the medium.
Recent support for this idea has emerged with the identification of
a glutamate export protein and its gene, yggB (NCgl1221) (16).
YggB is a homolog of a mechanosensitive channel, which
senses alterations in membrane tension and modulates the re-
lease of osmoprotectants into the medium in response. YggB
in coryneform bacteria is considered to have a similar function.
A recent model involving glutamate export is presented in
Figure 3, which shows that under conditions in which glutamate
accumulates in the medium, membrane tension has been altered
in a manner that triggers the opening of the YggB gate.
 HISTORY OF GLUTAMATE PRODUCTION
The industrial production of MSG using fermentation tech-
nology continues to improve in terms of conversion yield from
sugar to glutamate and in production speed of the fermentation.
Fermentation allows the isolation of L-glutamate to be a simple
process because the cells produce the L-isomer. To improve
MSG purity, a new method for purifying L-glutamic acid crystals
was developed, which uses recrystallization of the b-form (17)
and subsequent conversion to MSG. The mother liquor of the
crystallization process is then concentrated and used as a liquid
fertilizer (after pH adjustment with ammonia). The invention of
the fermentation method has dramatically improved glutamate
production methods and allowed production to keep up with
demand for the product.
FUTURE PROSPECTS FOR MSG PRODUCTION
In 2007 the world production of MSG was estimated to be
’2 million tons (2 billion kg), with demand continuing to in-
crease ’3%/y, notably in developing countries. Clearly, Ikeda
correctly foresaw the usefulness to humans of identifying and
then producing the umami taste component of kelp. A century
after his discovery, it is now appropriate to reflect on the overall
environmental effect of this industrial activity (ie, the use of raw
materials and the production of co-products) and attempt to see
it in light of today’s environmental concerns. It is my hope that
the glutamate industry will pursue environmental sustainability
in its production processes. An attempt to integrate the gluta-
mate industry into the biocycle with agriculture may be one
answer. (Other articles in this supplement to the Journal include
references 18–46.)
I thank the following individuals for their help in the preparation of this
article: Ken-ichi Baba (for history of extraction and purification technology),
Kunisuke Izawa (for the chemical synthesis method), Hisao Ito (for the fer-
mentation method), Kazuhiro Hasegawa, and Tatsuki Kashiwagi (for crystal-
FIGURE 3. Glutamate export by YggB (NCgl1221) in bacterial cells.
The dashed line indicates the bacterial cell membrane. Glucose, taken up by
the cell, is metabolized through the Krebs cycle to 2-oxoglutaric
(a-ketoglutaric in the diagram) acid, from which glutamate is produced
with ammonia by glutamate dehydrogenase. Conditions for glutamate
accumulation in the medium, such as biotin limitation, change the
bacterial cell membrane tension, which triggers the expression of the
yggB gene and the production of its membrane protein, leading to
the active transport of glutamate from the cell into the medium. L-Glu,
glutamic acid; PEP, phosphoenolpyruvate; Pyr, pyruvate; AcCo, acetyl-
coenzyme A; OAA, oxaloacetate; Cit, citrate; Icit, isocitrate; Ma, malate;
Fu, fumalate; SucCo, succinyl-coenzyme A.
731S
lization data). I also thank Isao Uenoyama, Jun Ikeda, Bradley Bigger, and
Ryuji Yamaguchi for offering information, advice, and assistance.
The author is employed by Ajinomoto Co, Inc, a manufacturer of food,
pharmaceuticals, fine chemicals, and amino acids, including glutamate.
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