Plant and Cell Physiology Supplement
Supplement to Plant and Cell Physiology Vol. 48
Conference information

α-L-Arabinofuranosidases from tomato fruit
*Fumika MiyohashiJyunko MatsunoYusuke KamiyoshiharaAkira TateishiHiroaki Inoue
Author information
CONFERENCE PROCEEDINGS FREE ACCESS

Pages 371

Details
Abstract
α-L-Arabinofuranosidase is an enzyme that is able to hydrolyze arabinosyl residues from pectin or hemicellulose. The loss of arabinosyl residues from cell wall polysaccharides was observed in many kinds of fruit and it seems to be related for fruit softening or textual changes. It is also reported that the existence of arabinosyl residues in cell wall polysaccharides affected the adhesion of each cell.
In tomato fruit, α-L-arabinofuranosidase activity was detected both ripened and developing fruit. α-L-Arabinofuranosidases purified from higher plants were classified in glycoside hydrolase family 3 or 51. Family 3 α-L-arabinofuranosidases seem to be bi-functional enzyme with β-xylosidase activity. Therefore, this enzyme may act against the release of xylosyl residues in vivo in addition to arabinofuranosidase activity. However, the role of the enzyme is unclear. We cloned α-L-arabinofuranosidase cDNAs exhibiting different expression pattern. Substrate specificities of each clone will be discussed.
Content from these authors
© 2007 by The Japanese Society of Plant Physiologists
Previous article Next article
feedback
Top