Polygalacturonic acid; Pectic oligosaccharides; Pectolytic enzymes; Degree of polymerization; HPAEC-PAD
Abstract :
[en] The present study investigates the individual efficiency of six commercial pectinase preparations (Endopolygalacturonase M2, Pectinase, Viscozyme L, Pectinex Ultra SP-L, Pectinase 62L and Macer8 FJ) in catalyzing the liberation of pectic oligosaccharides (POS) from polygalacturonic acid. On the basis of high-performance anion-exchange chromatography with pulsed amperometric detection (HPAEC-PAD) analysis of the enzymatic hydrolysates, products release kinetics revealed a random cleavage pattern and an exo mode of cleavage for all the enzymes except for Endopolygalacturonase M2.
All six enzymes generated oligoGalA with different degree of polymerization (DP); the quantitative composition of oligoGalA depended on the enzyme specificity and the time of enzymatic reaction. Endopolygalacturonase M2 was the best enzyme preparation for production of oligoGalA, with 18% (wt) of digalacturonic acid and 58% (wt) of trigalacturonic acid after 2h of reaction. Concerning galacturonic acid production, Pectinase 62L was superior to the other enzyme preparations with 47% (wt) after 1h of reaction.
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