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Chemistry of Natural Compounds

, Volume 46, Issue 6, pp 1008–1009 | Cite as

Identification of the amino-acid composition of cellulolytic enzymes by a phenylthiocarbamoyl method

  • Sh. Ya. Mirzaakhmedov
  • D. T. Ruzmetova
  • N. Sh. Berdiev
  • Sh. I. Salikhov
Article
  • 52 Downloads

The fungus Aspergillus terreus is known to produce highly active cellulolytic and xylanolytic enzymes depending on the cultivation conditions [1, 2, 3]. The enzymes can be used for biodegradation of ligno-cellulose wastes [4] and to destroy plant cell walls [5]. Knowledge of the physicochemical properties of the enzymes is needed in order to apply them successfully in various economic sectors.

Our goal was to study the physicochemical properties of cellulase-II, xylanase-I, xylanase-II, and pectinase isolated from A. terreus by determining the amino-acid composition, the N-terminus amino acids, and the isoelectric points (pI).

The aforementioned enzymes were isolated and purified by the literature methods [1, 6]. The classical method for determining the amino-acid composition of proteins and peptides consist of separating their acid hydrolysates using ionexchange chromatography with subsequent identification as ninhydrin derivatives [7]. We used a highly sensitive phenylthiocarbamoyl...

Keywords

Isoelectric Point CH3CN Literature Method CH3COONa Methanesulfonic Acid 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media, Inc. 2011

Authors and Affiliations

  • Sh. Ya. Mirzaakhmedov
    • 1
  • D. T. Ruzmetova
    • 1
  • N. Sh. Berdiev
    • 1
  • Sh. I. Salikhov
    • 1
  1. 1.A. S. Sadykov Institute of Bioorganic Chemistry, Academy of Sciences of the Republic of UzbekistanTashkentUzbekistan

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