A new group of exo-acting family 28 glycoside hydrolases of Aspergillus niger that are involved in pectin degradation

Elena S. Martens-Uzunova; Joris S. Zandleven; Jaques A. E. Benen; Hanem Awad; Harrie J. Kools; Gerrit Beldman; Alphons G. J. Voragen; Johan A. Van den Berg; Peter J. Schaap

doi:10.1042/BJ20060703

A new group of exo-acting family 28 glycoside hydrolases of Aspergillus niger that are involved in pectin degradation

Elena S. Martens-Uzunova
, Joris S. Zandleven
, Jaques A. E. Benen
, Hanem Awad
, Harrie J. Kools
, Gerrit Beldman
, Alphons G. J. Voragen
, Johan A. Van den Berg
, Peter J. Schaap

Wageningen University & Research

Research output: Contribution to journal › Article › Academic › peer-review

51 Citations (Scopus)

Abstract

The fungus Aspergillus niger is an industrial producer of pectin-degrading enzymes. The recent solving of the genomic sequence of A. niger allowed an inventory of the entire genome of the fungus for potential carbohydrate-degrading enzymes. By applying bioinformatics tools, 12 new genes, putatively encoding family 28 glycoside hydrolases, were identified. Seven of the newly discovered genes form a new gene group, which we show to encode exoacting pectinolytic glycoside hydrolases. This group includes four exo-polyaalacturonan hydrolases, (PGAX, PGXA, PGXB and PGXC) and three putative exo-rhamnogalacturonan hydrolases (RGXA. RGXB and RGXC). Biochemical identification using polygalacturonic acid and xylogalacturonan as substrates demonstrated that indeed PGXB and PGXC act as exo-polygalacturonases, whereas PGXA acts as an exo-xylogalacturonan hydrolase. The expression levels of all 21 genes were assessed by microarray analysis. The results from the present study demonstrate that exo-acting glycoside hydrolases play a prominent role in pectin degradation.

Original language	English
Pages (from-to)	43-52
Number of pages	10
Journal	Biochemical Journal
Volume	400
DOIs	https://doi.org/10.1042/BJ20060703
Publication status	Published - 15 Nov 2006
Externally published	Yes

Access to Document

10.1042/BJ20060703

Cite this

@article{de3c11462bae424d9374b83011f34c47,

title = "A new group of exo-acting family 28 glycoside hydrolases of Aspergillus niger that are involved in pectin degradation",

abstract = "The fungus Aspergillus niger is an industrial producer of pectin-degrading enzymes. The recent solving of the genomic sequence of A. niger allowed an inventory of the entire genome of the fungus for potential carbohydrate-degrading enzymes. By applying bioinformatics tools, 12 new genes, putatively encoding family 28 glycoside hydrolases, were identified. Seven of the newly discovered genes form a new gene group, which we show to encode exoacting pectinolytic glycoside hydrolases. This group includes four exo-polyaalacturonan hydrolases, (PGAX, PGXA, PGXB and PGXC) and three putative exo-rhamnogalacturonan hydrolases (RGXA. RGXB and RGXC). Biochemical identification using polygalacturonic acid and xylogalacturonan as substrates demonstrated that indeed PGXB and PGXC act as exo-polygalacturonases, whereas PGXA acts as an exo-xylogalacturonan hydrolase. The expression levels of all 21 genes were assessed by microarray analysis. The results from the present study demonstrate that exo-acting glycoside hydrolases play a prominent role in pectin degradation.",

author = "Martens-Uzunova, \{Elena S.\} and Zandleven, \{Joris S.\} and Benen, \{Jaques A. E.\} and Hanem Awad and Kools, \{Harrie J.\} and Gerrit Beldman and Voragen, \{Alphons G. J.\} and \{Van den Berg\}, \{Johan A.\} and Schaap, \{Peter J.\}",

year = "2006",

month = nov,

day = "15",

doi = "10.1042/BJ20060703",

language = "English",

volume = "400",

pages = "43--52",

journal = "Biochemical Journal",

issn = "0264-6021",

publisher = "Portland Press Ltd",

}

TY - JOUR

T1 - A new group of exo-acting family 28 glycoside hydrolases of Aspergillus niger that are involved in pectin degradation

AU - Martens-Uzunova, Elena S.

AU - Zandleven, Joris S.

AU - Benen, Jaques A. E.

AU - Awad, Hanem

AU - Kools, Harrie J.

AU - Beldman, Gerrit

AU - Voragen, Alphons G. J.

AU - Van den Berg, Johan A.

AU - Schaap, Peter J.

PY - 2006/11/15

Y1 - 2006/11/15

N2 - The fungus Aspergillus niger is an industrial producer of pectin-degrading enzymes. The recent solving of the genomic sequence of A. niger allowed an inventory of the entire genome of the fungus for potential carbohydrate-degrading enzymes. By applying bioinformatics tools, 12 new genes, putatively encoding family 28 glycoside hydrolases, were identified. Seven of the newly discovered genes form a new gene group, which we show to encode exoacting pectinolytic glycoside hydrolases. This group includes four exo-polyaalacturonan hydrolases, (PGAX, PGXA, PGXB and PGXC) and three putative exo-rhamnogalacturonan hydrolases (RGXA. RGXB and RGXC). Biochemical identification using polygalacturonic acid and xylogalacturonan as substrates demonstrated that indeed PGXB and PGXC act as exo-polygalacturonases, whereas PGXA acts as an exo-xylogalacturonan hydrolase. The expression levels of all 21 genes were assessed by microarray analysis. The results from the present study demonstrate that exo-acting glycoside hydrolases play a prominent role in pectin degradation.

AB - The fungus Aspergillus niger is an industrial producer of pectin-degrading enzymes. The recent solving of the genomic sequence of A. niger allowed an inventory of the entire genome of the fungus for potential carbohydrate-degrading enzymes. By applying bioinformatics tools, 12 new genes, putatively encoding family 28 glycoside hydrolases, were identified. Seven of the newly discovered genes form a new gene group, which we show to encode exoacting pectinolytic glycoside hydrolases. This group includes four exo-polyaalacturonan hydrolases, (PGAX, PGXA, PGXB and PGXC) and three putative exo-rhamnogalacturonan hydrolases (RGXA. RGXB and RGXC). Biochemical identification using polygalacturonic acid and xylogalacturonan as substrates demonstrated that indeed PGXB and PGXC act as exo-polygalacturonases, whereas PGXA acts as an exo-xylogalacturonan hydrolase. The expression levels of all 21 genes were assessed by microarray analysis. The results from the present study demonstrate that exo-acting glycoside hydrolases play a prominent role in pectin degradation.

UR - https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=eur_pure&SrcAuth=WosAPI&KeyUT=WOS:000242226600005&DestLinkType=FullRecord&DestApp=WOS

U2 - 10.1042/BJ20060703

DO - 10.1042/BJ20060703

M3 - Article

C2 - 16822232

SN - 0264-6021

VL - 400

SP - 43

EP - 52

JO - Biochemical Journal

JF - Biochemical Journal

ER -

A new group of exo-acting family 28 glycoside hydrolases of Aspergillus niger that are involved in pectin degradation

Abstract

Access to Document

Other files and links

Fingerprint

Cite this