glutathione review

Topics: Glutathione, Amino acid, Escherichia coli Pages: 33 (4172 words) Published: October 10, 2013

Yin Li . Gongyuan Wei . Jian Chen

Glutathione: a review on biotechnological production

Received: 1 June 2004 / Revised: 16 August 2004 / Accepted: 31 August 2004 / Published online: 12 October 2004 # Springer-Verlag 2004

Abstract This Mini-Review summarizes the historic
developments and technological achievements in the
biotechnological production of glutathione in the past 30
years. Glutathione is the most abundant non-protein thiol
compound present in living organisms. It is used as a
pharmaceutical compound and can be used in food
additives and the cosmetic industries. Glutathione can be
produced using enzymatic methods in the presence of ATP
and its three precursor amino acids (L-glutamic acid, Lcysteine, glycine). Alternatively, glutathione can be produced by direct fermentative methods using sugar as
a starting material. In the latter method, Saccharomyces
cerevisiae and Candida utilis are currently used to produce
glutathione on an industrial scale. At the molecular level,
the genes gshA and gshB, which encode the enzymes γglutamylcysteine synthetase and glutathione synthetase, respectively, have been cloned from Escherichia coli and
over-expressed in E. coli, S. cerevisiae, and Lactococcus
lactis. It is anticipated that, with the design and/or
discovery of novel producers, the biotechnological
production of glutathione will be further improved to
expand the application range of this physiologically and
medically important tripeptide.

Glutathione (γ-glutamyl-L-cysteinylglycine, GSH) is the
most abundant non-protein thiol compound widely
Y. Li (*) . G. Wei . J. Chen
The Key Laboratory of Industrial Biotechnology, Ministry of
Education; School of Biotechnology, Southern Yangtze
170 Huihe Road,
Wuxi, 214036, People’s Republic of China
Tel.: +86-510-5885727
Fax: +86-510-5888301
G. Wei
School of Life Science, Soochow University,
Suzhou, 215007, People’s Republic of China

distributed in living organisms and, predominantly, in
eukaryotic cells (Meister and Anderson 1983). While over
90% of the glutathione is normally present in the reduced
form GSH, several additional forms of glutathione are
present in (microbial) cells, tissues, and plasmas. Glutathione disulfide GSSG (oxidized glutathione), formed upon oxidation of GSH, can be in turn be reduced to GSH
by glutathione reductase at the expense of NADPH
(Carmel-Harel and Storz 2000). Besides GSSG, GSH
may occur in other forms of mixed disulfides, for example,
GS-S-CoA, GS-S-Cys (Penninckx 2002), and GS-S-protein which is formed via glutathionylation. Although GSH has been found to be involved in many
physiological processes and to play various important
roles, the major and general functions of GSH can be
summarized into three major ways, i.e. serving as
antioxidant, immunity booster, and detoxifier in higher
eukaryotic organisms (Pastore et al. 2003). First, the
strong electron-donating capability of GSH and the
relatively high intracellular concentration (up to millimolar levels) enable the maintenance of a reducing cellular
environment. This makes GSH an important antioxidant
for protecting DNA, proteins, and other biomolecules
against oxidative damage generated by, for example,
reactive oxygen species. Second, GSH plays an important
role in immune function via white blood cell production
and is one of the most potent anti-viral agents known.
Finally, GSH can be conjugated to exogenous electrophiles and diverse xenobiotics by glutathione-S-transferase to accomplish detoxification. GSH is thus considered to be one of the most powerful, versatile, and important

self-generated defense molecules. In humans, GSH deficiency has been linked to a number of disease states: HIV infection, liver cirrhosis, pulmonary diseases, gastrointestinal and pancreatic inflammations, diabetes, neurodegenerative diseases, and aging (Wu...
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