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.com
Volume 7, Issue 1 (Suppl)
J Biotechnol Biomater
ISSN: 2155-952X JBTBM, an open access journal
March 20-21, 2017 Rome, Italy
&
15
th
World Congress on
2
nd
International Conference on
Biotechnology And Biotech Industries Meet
Enzymology and Molecular Biology
Enzymology & Mol. Biology 2017
Biotechnology Congress 2017
March 20-21, 2017
Tejaswani Saragadam et al., J Biotechnol Biomater 2017, 7:1(Suppl)
http://dx.doi.org/10.4172/2155-952X.C1.071Catabolic route for 3-guanidinopropionic acid utilization by
Aspergillus niger
: Involvement of
4-guanidinobutyrase
Tejaswani Saragadam, Sunil Kumar
and
Narayan S Punekar
IIT Bombay, India
A
spergillus niger
is a metabolically versatile filamentous fungus that utilizes various guanidinium compounds as nitrogen source.
The fungus utilizes 4-guanidinobutyric acid (GB), whereas its lower structural homologue 3-guanidinopropionic acid (GP) is
very poorly metabolized. The enzyme 4-guanidinobutyrase (GBase) facilitates GB catabolism in this fungus. There is no specific
3-guanidinopropionase (GPase) in
A. niger
but the purified GBase itself exhibits low GPase activity. Based on these observations
we hypothesized that the inability of the fungus to mobilize GP as a nitrogen source is because GP is a poor GBase substrate. Two
strategies were employed to test this; one was to increase the mycelial GBase levels and tailoring the GBase specificity towards GP was
the second approach. A constitutive expression of GBase in
A. niger
resulted in normal growth on GP indicating that intracellular
GBase levels essentially limit GP utilization in this fungus. There was a direct correlation between growth on GP and cellular GBase
levels. In the second approach, altering GBase substrate specificity was attempted.
A. niger
spores were exposed to ethyl methane
sulfonate (EMS) and the mutants were selected through differential growth on GP versus GB. One mutant that better utilized GP
than the parent strain was selected and analyzed. Neither an increased GBase activity nor a specific GPase activity was observed in
this mutant. Furthermore, no mycelial GPase activity was detected when the mutant was grown on GP. The presence of urea in the
spent media when the mutant was grown on GP however implicates a GPase. The possibility of an alternate route for GP catabolism,
not involving a GBase needs further study.
Biography
Tejaswani Saragadam is an Integrated MSc-PhD student working under Professor N S Punekar at IIT Bombay. She is working on the aspects of enzymology and
metabolism in
Aspergillus niger
, an industrially well-known fungus for citric acid production and various enzymes. Understanding the nitrogen metabolism in this
fungus and studying new pathways and enzymes involved in nitrogen metabolism forms her major work. Further characterizing these enzymes and understanding
their role in the novel metabolic pathways forms the basis of her study.
tejaswini.iitb@gmail.com