Characterization and Application of an Alginate Lyase, Aly1281 from Marine Bacterium Pseudoalteromonas carrageenovora ASY5

Abstract

Alginate extracted from widely cultured brown seaweed can be hydrolyzed by alginate lyase to produce alginate oligosaccharides (AOS) with intriguing biological activities. Herein, a novel alginate lyase Aly1281 was cloned from marine bacterium Pseudoalteromonas carrageenovora ASY5 isolated from mangrove soil and found to belong to polysaccharide lyase family 7. Aly1281 exhibited maximum activity at pH 8.0 and 50 °C and have broad substrate specificity for polyguluronate and polymannuronate. Compared with other alginate lyases, Aly1281 exhibited high degradation specificity and mainly produced di-alginate oligosaccharides which displayed good antioxidant function to reduce ferric and scavenge radicals such as hydroxyl, ABTS+ and DPPH. Moreover, the catalytic activity and kinetic performance of Aly1281 were highly improved with the addition of salt, demonstrating a salt-activation property. A putative conformational structural feature of Aly1281 was found by MD simulation analysis for understanding the salt-activation effect.

Characterization of a New Bifunctional and Cold-Adapted Polysaccharide Lyase (PL) Family 7 Alginate Lyase from Flavobacterium sp.

“…S20 ( Figure 3 ), and the latter prefers polyM [ 65 ], implying that AlyS02 may be polyG-preferred. Moreover, catalytic sites (Q169, H171, and Y285) were predicted in AlyS02 based on previous research on alginate lyase AlyA5 from Zobellia galactanivorans DsijT and Aly1281 from Pseudoalteromonas carrageenovora ASY5 [ 64 , 66 ]. The results of sequence alignment further confirmed that AlyS02 belongs to the PL7 family.…”

“…S20 appears to take penta-, hexa- and hepta-alginate oligosaccharides as the major depolymerization products [ 32 ]. Some alginate lyases can cleave the substrate mainly releasing the products with single DP distribution [ 63 , 64 ]. During the enzymatic preparation of oligosaccharides, high degradation specificity will be conducive for the oligosaccharide purification and application.…”

“…However, few of these reported enzymes have been commercially used owing to their poor properties [ 56 ]. Several alginate lyases with certain specific characteristics have been found and studied, such as pH stability [ 51 , 57 ], thermo-tolerance [ 58 ], cold adaption [ 59 , 60 ], acidic or alkaline adaption [ 61 , 62 ], single product distribution [ 63 , 64 ], which are quite significant for both research and commercial purposes, but the enzymes with optimal characteristics are rare. It is worth noting that cold-adapted alginate lyases make running biocatalysis at low temperature possible, which is crucial to reduce the danger of contamination and improve the sustainability of enzyme utilization, thereby decreasing the input costs to some extent, particularly for industrial production of oligosaccharides.…”

Characterization of a New Intracellular Alginate Lyase with Metal Ions-Tolerant and pH-Stable Properties

“…The molecular weight of intracellular Alyw202 is similar to molecular weights of AlyV5 (37 kDa) from Vibrio sp. QY105 [ 19 ] and Aly1281 (40.65 kDa) classified as PL family 7 from Pseudoalteromonas carrageenovora ASY5 [ 20 ]. This intracellular alginate lyase was named Alyw202 and used in the following investigation.…”

Expression and Characterization of a Cold-Adapted Alginate Lyase with Exo/Endo-Type Activity from a Novel Marine Bacterium Alteromonas portus HB161718T

“…Alginate lyases from the PL7 family have been widely studied, e.g., NitAly from Nitratiruptor sp. SB155-2 [ 13 ], lyA from Isoptericola halotolerans NJ-05 [ 14 ], Aly1281 from Pseudoalteromonas carrageenovora ASY5 [ 15 ], and MtAl138 from Microbulbifer thermotolerans DAU221 [ 16 ]. Alginate lyases are widely derived from marine algae; mollusks; and microorganisms (including bacteria, fungi, and viruses), among which marine bacteria are the most common resources.…”