Article

Inhibitory action of toxic compounds present in lignocellulosic hydrolysates on xylose to xylitol bioconversion by Candida guilliermondii.

Department of Biotechnology, Engineering College of Lorena, University of São Paulo, Estrada Municipal do Campinho s/n, 12602-810, Lorena, SP, Brazil.
Journal of Industrial Microbiology (impact factor: 1.8). 01/2011; 38(1):71-8. DOI:10.1007/s10295-010-0830-6 pp.71-8
Source: PubMed

ABSTRACT The inhibitory action of acetic acid, ferulic acid, and syringaldehyde on metabolism of Candida guilliermondii yeast during xylose to xylitol bioconversion was evaluated. Assays were performed in buffered and nonbuffered semidefined medium containing xylose as main sugar (80.0 g/l), supplemented or not with acetic acid (0.8-2.6 g/l), ferulic acid (0.2-0.6 g/l), and/or syringaldehyde (0.3-0.8 g/l), according to a 2(3) full factorial design. Since only individual effects of the variables were observed, assays were performed in a next step in semidefined medium containing different concentrations of each toxic compound individually, for better understanding of their maximum concentration that can be present in the fermentation medium without affecting yeast metabolism. It was concluded that acetic acid, ferulic acid, and syringaldehyde are compounds that may affect Candida guilliermondii metabolism (mainly cell growth) during bioconversion of xylose to xylitol. Such results are of interest and reveal that complete removal of toxic compounds from the fermentation medium is not necessary to obtain efficient conversion of xylose to xylitol by Candida guilliermondii. Fermentation in buffered medium was also considered as an alternative to overcome the inhibition caused by these toxic compounds, mainly by acetic acid.

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    Article: Purification and properties of phenolic acid decarboxylase from Candida guilliermondii
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    ABSTRACT: A heat-labile phenolic acid decarboxylase from Candida guilliermondii (an anamorph of Pichia guilliermondii) was purified to homogeneity by simple successive column chromatography within 3 days. The molecular mass was 20 kDa by sodium dodecyl sulfate–polyacrylamide gel electrophoresis and 36 kDa by gel-filtration chromatography, suggesting that the purified enzyme is a homodimer. The optimal pH and temperature were approximately 6.0 and 25�C. Characteristically, more than 50% of the optimal activity was observed at 0�C, suggesting that this enzyme is cold-adapted. The enzyme converted p-coumaric acid, ferulic acid, and caffeic acid to corresponding products with high specific activities of approximately 600, 530, and 46 U/mg, respectively. The activity was stimulated by Mg2? ions, whereas it was completely inhibited by Fe2?, Ni2 ?, Cu2?, Hg2?, 4-chloromericuribenzoate, N-bromosuccinimide, and diethyl pyrocarbonate. The enzyme was inducible and expressed inside the cells moderately by ferulic acid and p-coumaric acid and significantly by non-metabolizable 6-hydroxy-2- naphthoic acid.
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Keywords

acetic acid
 
Assays
 
buffered medium
 
Candida guilliermondii
 
Candida guilliermondii metabolism
 
Candida guilliermondii yeast
 
cell growth
 
complete removal
 
different concentrations
 
efficient conversion
 
fermentation medium
 
ferulic acid
 
maximum concentration
 
next step
 
nonbuffered semidefined medium
 
semidefined medium
 
toxic compound
 
toxic compounds
 
xylitol bioconversion
 
yeast metabolism