Publication

Rhamnogalacturonan alpha-D-galactopyranosyluronohydrolase - An enzyme that specifically removes the terminal nonreducing galacturonosyl residue in rhamnogalacturonan regions of pectin

Related publications (4)

How General Is Anomeric Retention during Collision-Induced Dissociation of Glycans?

Thomas Rizzo, Robert Paul Pellegrinelli, Ahmed Ben Faleh, Stephan Warnke, Eduardo Carrascosa Casado, Lei Yue

: Despite the essential role that glycans play in many biological processes, their isomeric com-plexity makes their structural determination partic-ularly challenging. Tandem mass spectrometry has played a central role in glycan analysis, and recent work h ...

2020

Stereochemical course of hydrolysis catalysed by alpha-L-rhamnosyl and alpha-D-galacturonosyl hydrolases from Aspergillus aculeatus

The stereochemical course of hydrolysis catalysed by four Aspergillus aculeatus enzymes acting on alpha-L-rhamnosyl and alpha-D-galacturonosyl linkages in the hairy regions of pectins has been determined using H-1-NMR. Exogalacturonase acts with inversion ...

1998

Characterization of recombinant rhamnogalacturonan alpha-L-rhamnopyranosyl-(1,4)-alpha-D-galactopyranosyluronide lyase from Aspergillus aculeatus - An enzyme that fragments rhamnogalacturonan I regions of pectin

The four major oligomeric reaction products from saponified modified hairy regions (MHR-S) from apple, produced by recombinant rhamnogalacturonan (RC) alpha-L-rhamnopyranosyl-(1,4)-alpha-D-galactopyranosyluronide lyase (rRG-lyase) from Aspergillus aculeatu ...

1998

RHAMNOGALACTURONAN ALPHA-L-RHAMNOPYRANOHYDROLASE - A NOVEL ENZYME SPECIFIC FOR THE TERMINAL NONREDUCING RHAMNOSYL UNIT IN RHAMNOGALACTURONAN REGIONS OF PECTIN

Two alpha-L-rhamnohydrolases with different substrate specificities were isolated from a commercial preparation produced by Aspergillus aculeatus. The first rhamnohydrolase was active toward p-nitrophenyl-alpha-L-rhamnopyranoside, naringin, and hesperidin ...

1994

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