초록
<P><B>Highlights</B></P><P>► 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.</P> <P><B>Abstract</B></P><P>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.</P><P>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.</P>