As an advanced biotechnology company, Creative Enzymes always has the prospective insight toward the development of enzyme industries. While the need of measuring enzyme activity grows as one of the most important markets, Creative Enzymes provides a panel of approaches to achieve accurate activity quantification. Combining the advantages of cutting-edge instrument and skilled operations, our specialized enzymologists offer perfect assay services for virtually any enzyme. Creative Enzymes is adept at hydrolase assays, including the beta-porphyranase.

Beta-porphyranases belong to the glycoside hydrolase family and degrade the sulfated polymers. The main substrate of the enzyme is porphyran, which is a sulfated carbohydrate derived from red algae of the genus Porphyra. These enzymes, PorA and PorB, specifically cleave the beta-1,4 linkage between beta-D-galactopyranose and alpha-L-galactopyranose-6-sulfate, forming mostly the disaccharide alpha-L-galactopyranose-6-sulfate-(1→3)-beta-D-galactose, but some longer oligosaccharides are also observed. PorA and PorB slightly differ in substrate specificity: PorA displays a strict requirement for C6- sulfate in both binding subsites, and PorB tolerates the presence of 3-6-anhydro-L-galactose. Both enzymes do not accept methylation of the galactose unit.

Unlike agarose and carrageenan, porphyran is not utilized as food ingredients for its gelling or texturizing properties. However, it is one of the most consumed algal polysaccharides because it is the main component of edible P. yezoensis and P. tenera, which are extensively used in the preparation of sushi. As other sulfated galactans, porphyran also showed some potential in pharmacological applications, based on its hypolipidemic and anti-allergic properties. As one of the few enzymes that degrade porphyran, more and more studies have been focused on optimization of the catalytical activity of beta-porphyranases. Creative Enzymes supports such research with reliable activity measurement of beta-porphyranases, by detecting the released reducing sugar using spectrophotometric assays.

Figure: The crystal structure of beta-porphyranase A from Zobellia galactanivorans.
Reference: Hehemann, J.H. et al. J.Biol.Chem. 2012 287: 30571-30584.

Creative Enzymes is one of the few companies that provide activity assays for beta-porphyranase. With comprehensive expertise and known-how, the scientists of Creative Enzymes can offer more targeted and proper testing methods. We are engaged in solving any tough challenges in your enzymatic research. Our strong technology is visible among the global market. In the future, Creative Enzymes will continue the assay service as your reliable partner.