Abstract
Alginate lyases have been widely used to prepare alginate oligosaccharides in food, agricultural, and medical industries. Therefore, discovering and characterizing novel alginate lyases with excellent properties has drawn increasing attention. Herein, a novel alginate lyase FsAlyPL6 of Polysaccharide Lyase (PL) 6 family is identified and biochemically characterized from Flammeovirga sp. NJ-04. It shows highest activity at 45 °C and could retain 50% of activity after being incubated at 45 °C for 1 h. The Thin-Layer Chromatography (TLC) and Electrospray Ionization Mass Spectrometry (ESI-MS) analysis indicates that FsAlyPL6 endolytically degrades alginate polysaccharide into oligosaccharides ranging from monosaccharides to pentasaccharides. In addition, the action pattern of the enzyme is also elucidated and the result suggests that FsAlyPL6 could recognize tetrasaccharide as the minimal substrate and cleave the glycosidic bonds between the subsites of −1 and +3. The research provides extended insights into the substrate recognition and degradation pattern of PL6 alginate lyases, which may further expand the application of alginate lyases.
Highlights
Alginate is a linear acidic polysaccharide that constitutes the cell wall of brown algae [1]
The open reading frame (ORF) consisted of 2238 bps and encoded a putative alginate lyase of 745 amino acid residues with a theoretical molecular mass of 83.09 kDa
The gene of FsAlyPL6 was ligated into pET-21a(+) and the recombinant plasmid was transformed into E. coli BL21 (DE3) for heterologously expression
Summary
Alginate is a linear acidic polysaccharide that constitutes the cell wall of brown algae [1]. The alginate molecule could not get into the circulation system due to its huge molecular structure It could not exhibit its physiological activities. As the degrading products of alginate, are smaller with excellent solubility and bioavailability than the polysaccharides. The physiological effects, such as anticoagulant, antioxidant, and antineoplastic activities, can be retained after degradation. They have been widely used as anticoagulants, plant growth accelerators and tumor inhibitors in food, agricultural, and medical fields [3,4,5]. The biochemical properties and degrading pattern of the enzyme have been investigated and this research would further expand the applications of alginate lyases in related fields
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