Characterization of Hyaluronan-Degrading Enzymes from Yeasts

Hyaluronidases (HAases) from yeasts were characterized for the first time. The study elucidated that hyaluronate 4-glycanohydrolase and hyaluronan (HA) lyase can be produced by yeasts. Six yeasts producing HAases were found through express screening of activities. The extracellular HAases from two of the yeast isolates, Pseudozyma aphidis and Cryptococcus laurentii, were characterized among them. P. aphidis HAase hydrolyzed beta-1,4 glycosidic bonds of HA, yielding even-numbered oligosaccharides with N-acetyl-d-glucosamine at the reducing end. C. laurentii produced hyaluronan lyase, which cleaved beta-1,4 glycosidic bonds of HA in beta-elimination reaction, and the products of HA degradation were different-sized even-numbered oligosaccharides. The shortest detected HA oligomer was dimer. The enzymes' pH and temperature optima were pH 3.0 and 37-45 A degrees C (P. aphidis) and pH 6.0 and 37 A degrees C (C. laurentii), respectively. Both HAases showed good thermostability.