This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Dobozi, M. S. Articles by Bruschi, C. V. Search for Related Content PubMed PubMed Citation Articles by Dobozi, M. S. Articles by Bruschi, C. V. Agricola Articles by Dobozi, M. S. Articles by Bruschi, C. V.

 Previous Article  |  Next Article 

Appl Environ Microbiol. 1992 November; 58(11): 3466-3471
Copyright © 1992, American Society for Microbiology. All Rights Reserved.

Xylanase Activity of Phanerochaete chrysosporium

Mária Szakács Dobozi^,*, György Szakács and Carlo V. Bruschi

¹ Microbiology Group, UNIDO ICGEB, Padriciano 99, I-34012, Trieste, Italy, and Department of Agricultural Chemical Technology, Technical University of Budapest, Gellért tér 4, H-1111 Budapest, Hungary²

ABSTRACT

Xylan-degrading enzymes were induced when Phanerochaete chrysosporium was grown at 30°C in shake flask media containing xylan, Avicel PH 102, or ground corn stalks. The highest xylanase activity was produced in the corn stalk medium, while the xylan-based fermentation resulted in the lowest induction. Analytical and preparative isoelectric focusing were used to characterize xylanase multienzyme components. Preparative focusing was performed only with the cultures grown on Avicel and corn stalk. Of over 30 protein bands separated by analytical focusing from the Avicel and corn stalk media, three main groups (I, II, and III) of about five isoenzymes each showed xylanase activity when a zymogram technique with a xylan overlay was used. Enzyme assays revealed the presence of 1,4-ß-endoxylanase and arabinofuranosidase activities in all three isoenzyme groups separated by preparative isoelectric focusing. ß-Xylosidase activity appeared in the first peak and also as an independent peak between peaks II and III. Denatured molecular masses for the three isoenzyme groups were found to be between 18 and 90 kDa, and pI values were in the range of 4.2 to 6.0. ß-Xylosidase has an apparent molecular mass of 20, 30, and 90 kDa (peak I) and 18 and 45 kDa (independent peak), indicating a trimer and dimer structure, respectively, with pI values of 4.2 and 5.78, respectively. Three more minor xylanase groups were produced on corn stalk medium: a double peak in the acidic range (pI 6.25 to 6.65 and 6.65 to 7.12) and two minor peaks in the alkaline range (pI 8.09 to 8.29 and 9.28 to 9.48, respectively). The profile of xylanases separated by isoelectric focusing (zymogram) of culture filtrate from cells grown on corn stalk media was more complex than that of culture supernatants from cells grown on cellulose. The pH optima of the three major xylanase groups are in the range of pH 4 to 5.5.

^* Corresponding author.

Present address: Department of Biochemistry, Central Food Research Institute, Herman Ottó út 15, H-1022 Budapest, Hungary.

This article has been cited by other articles:

• Sato, S., Liu, F., Koc, H., Tien, M. (2007). Expression analysis of extracellular proteins from Phanerochaete chrysosporium grown on different liquid and solid substrates. Microbiology 153: 3023-3033 [Abstract] [Full Text]