Enzymatic production of pectic oligosaccharides from polygalacturonic acid with commercial pectinase preparations

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 2 h of reaction. Concerning galacturonic acid production, Pectinase 62L was superior to the other enzyme preparations with 47% (wt) after 1 h of reaction.

► Efficiency of six commercial pectinases in catalyzing liberation of POS. ► Pattern of random and exo cleavage were found for all except for EPG-M2. ► All six enzymes generated oligoGalA with different degree of polymerization. ► Yields of oligoGalA depended on the enzyme specificity and reaction time. ► Among them, EPG-M2 was the best enzyme for production of oligoGalA.