Abstract
The proportion of glucoamylases, GAI and GAII, in the culture supernatant of Aspergillus awamori fermentations depends on the medium C/N ratio in such a way that the transformation of GAI into GAII is favored by the existence of a surplus of the carbon source in the growth medium. This condition also favors the appearance of the proteolytic activity. The authors report the observation that the shift in the isoenzyme proportion was concomitant to the peak of proteolytic activity. A peptide that may have resulted from the continuous degradation of the GAI C-terminal peptide, Gp-1, was isolated by gel filtration and purified by reverse-phase chromatography. This peptide matched with the region G14-A34 of the substrate-binding domain of GAI, thus reinforcing the hypothesis of the extracellular proteolytic processing of GAI.
Author to whom all correspondence and reprint requests should be addressed. Email: enzitec@iq.ufrj.br
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Nascimento, H.J., Soares, V.F., Bon, E.P.S., Silva, J.G. (1998). Extracellular Proteolytic Processing of Aspergillus awamori GAI into GAII is Supported by Physico-Chemical Evidence. In: Finkelstein, M., Davison, B.H. (eds) Biotechnology for Fuels and Chemicals. Applied Biochemistry and Biotechnology. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-4612-1814-2_58
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DOI: https://doi.org/10.1007/978-1-4612-1814-2_58
Publisher Name: Humana Press, Totowa, NJ
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