Unknown

Dataset Information

0

Engineering broad-spectrum digestion of polyuronides from an exolytic polysaccharide lyase.


ABSTRACT: BACKGROUND:Macroalgae represents a promising source of fermentable carbohydrates for use in the production of energy efficient biofuel. The primary carbohydrate in brown algae is the uronic acid-containing alginate, whereas green algae contains a significant amount of glucuronan. A necessary step in the conversion of these polyuronides to bioethanol is saccharification, which can be achieved by enzymatic or chemical degradation. RESULTS:Polysaccharide lyases are a class of enzymes which cleave uronic acid-containing glycans via a ?-elimination mechanism, acting both endo- and exolytically on their substrates. In the present work, we characterize a putative alginate lyase from Stenotrophomonas maltophilia K279a (Smlt2602) and describe a H208F mutant that, in addition to cleaving alginate-based substrates, displays significant, exolytic glucuronan activity. CONCLUSIONS:To our knowledge this is the first polysaccharide lyase to act exolytically on glucuronan and is an attractive candidate for the broad-spectrum digestion of polyuronides into fermentable monomers.

SUBMITTER: MacDonald LC 

PROVIDER: S-EPMC4765187 | biostudies-literature | 2016

REPOSITORIES: biostudies-literature

altmetric image

Publications

Engineering broad-spectrum digestion of polyuronides from an exolytic polysaccharide lyase.

MacDonald Logan C LC   Weiler Elizabeth B EB   Berger Bryan W BW  

Biotechnology for biofuels 20160224


<h4>Background</h4>Macroalgae represents a promising source of fermentable carbohydrates for use in the production of energy efficient biofuel. The primary carbohydrate in brown algae is the uronic acid-containing alginate, whereas green algae contains a significant amount of glucuronan. A necessary step in the conversion of these polyuronides to bioethanol is saccharification, which can be achieved by enzymatic or chemical degradation.<h4>Results</h4>Polysaccharide lyases are a class of enzymes  ...[more]

Similar Datasets

| S-EPMC1567917 | biostudies-literature
| S-EPMC8105002 | biostudies-literature
| S-EPMC8558848 | biostudies-literature
| S-EPMC5711954 | biostudies-literature
| S-EPMC4576204 | biostudies-literature
| S-EPMC4954714 | biostudies-literature