Abstract

A number of Sphingomonas strains capable of synthesizing the bacterial exopolysaccharide gellan and related polymers were shown to possess constitutive gellanase activity. In each case, the degradation of deacylated gellan was due to extracellular, eliminase-type enzymes (lyases) which cleave the sequence ... beta-D-glucosyl 1,4-beta-D-glucuronosyl ... in the tetrasaccharide repeat unit of the substrate polysaccharides. Deacetylated rhamsan was an alternative substrate but there was little or no action against most other polysaccharides with similar structures. Slight differences were found between the specificities of the lyases from different strains. Activities of gellan lyase preparations were generally low. As well as the extracellular 'gellanase' activity, all the bacteria possessed varying amounts of beta-D-glucosidase and beta-D-glucuronidase activities apparently located in the periplasm. The products from deacylated gellan and the chemically deacylated form of polysaccharide S194 (rhamsan gum), which is effectively a gentiobiosylated form of gellan, closely resembled those recently obtained by the authors from other, gellan-degrading, non-gellan-producing bacteria. The enzymes had negligible activity against the natural, acylated gellan and rhamsan polysaccharides from bacteria now designated as strains of Sphingomonas.

Full Text
Paper version not known

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.