Unknown

Dataset Information

0

Cloning, Expression, and Characterization of a New PL25 Family Ulvan Lyase from Marine Bacterium Alteromonas sp. A321.


ABSTRACT: Ulvan lyases can degrade ulvan to oligosaccharides with potent biological activity. A new ulvan lyase gene, ALT3695, was identified in Alteromonas sp. A321. Soluble expression of ALT3695 was achieved in Escherichia coli BL21 (DE3). The 1314-bp gene encoded a protein with 437 amino acid residues. The amino acid sequence of ALT3695 exhibited low sequence identity with polysaccharide lyase family 25 (PL25) ulvan lyases from Pseudoalteromonas sp. PLSV (64.14% identity), Alteromonas sp. LOR (62.68% identity), and Nonlabens ulvanivorans PLR (57.37% identity). Recombinant ALT3695 was purified and the apparent molecular weight was about 53 kDa, which is different from that of other polysaccharide-degrading enzymes identified in Alteromonas sp. A321. ALT3695 exhibited maximal activity in 50 mM Tris-HCl buffer at pH 8.0 and 50 °C. ALT3695 was relatively thermostable, as 90% activity was observed after incubation at 40 °C for 3 h. The Km and Vmax values of ALT3695 towards ulvan were 0.43 mg·mL-1 and 0.11 ?mol·min-1·mL-1, respectively. ESI-MS analysis showed that enzymatic products were mainly disaccharides and tetrasaccharides. This study reports a new PL25 family ulvan lyase, ALT3695, with properties that suggest its great potential for the preparation of ulvan oligosaccharides.

SUBMITTER: Gao J 

PROVIDER: S-EPMC6836179 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications

Cloning, Expression, and Characterization of a New PL25 Family Ulvan Lyase from Marine Bacterium <i>Alteromonas</i> sp. A321.

Gao Jian J   Du Chunying C   Chi Yongzhou Y   Zuo Siqi S   Ye Han H   Wang Peng P  

Marine drugs 20191008 10


Ulvan lyases can degrade ulvan to oligosaccharides with potent biological activity. A new ulvan lyase gene, <i>ALT3695</i>, was identified in <i>Alteromonas</i> sp. A321. Soluble expression of <i>ALT3695</i> was achieved in <i>Escherichia coli</i> BL21 (DE3). The 1314-bp gene encoded a protein with 437 amino acid residues. The amino acid sequence of ALT3695 exhibited low sequence identity with polysaccharide lyase family 25 (PL25) ulvan lyases from <i>Pseudoalteromonas</i> sp. PLSV (64.14% ident  ...[more]

Similar Datasets

| S-EPMC4882643 | biostudies-literature
| S-EPMC5295221 | biostudies-literature
| S-EPMC6281962 | biostudies-literature
| S-EPMC6357633 | biostudies-literature
| S-EPMC6627919 | biostudies-literature
| S-EPMC9728341 | biostudies-literature
| S-EPMC9781882 | biostudies-literature
| S-EPMC6315854 | biostudies-literature
| S-EPMC167341 | biostudies-other
| S-EPMC5867630 | biostudies-literature