Characterization of a New Cold-Adapted and Salt-Activated Polysaccharide Lyase Family 7 Alginate Lyase from Pseudoalteromonas sp. SM0524

Alginate oligosaccharides produced by enzymatic degradation show versatile physiological functions and biological activities. In this study, a new alginate lyase encoding gene alyS02 from Flavobacterium sp. S02 was recombinantly expressed at a high level in Yarrowia lipolytica, with the highest extracellular activity in the supernatant reaching 36.8 ± 2.1 U/mL. AlyS02 was classified in the polysaccharide lyase (PL) family 7. The optimal reaction temperature and pH of this enzyme were 30 °C and 7.6, respectively, indicating that AlyS02 is a cold-adapted enzyme. Interestingly, AlyS02 contained more than 90% enzyme activity at 25 °C, higher than other cold-adapted enzymes. Moreover, AlyS02 is a bifunctional alginate lyase that degrades both polyG and polyM, producing di- and trisaccharides from alginate. These findings suggest that AlyS02 would be a potent tool for the industrial applications.

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Cloning, Secretory Expression and Characterization of a Unique pH-Stable and Cold-Adapted Alginate Lyase

Marine Drugs ◽

10.3390/md18040189 ◽

2020 ◽

Vol 18 (4) ◽

pp. 189 ◽

Cited By ~ 4

Author(s):

Zhi-Peng Wang ◽

Min Cao ◽

Bing Li ◽

Xiao-Feng Ji ◽

Xin-Yue Zhang ◽

...

Keyword(s):

Specific Activity ◽

Brown Seaweed ◽

Alginate Lyase ◽

Industrial Applications ◽

Degree Of Polymerization ◽

Cold Adapted ◽

Alginate Oligosaccharide ◽

Ph Range ◽

Alginate Lyases

Cold-adapted alginate lyases have unique advantages for alginate oligosaccharide (AOS) preparation and brown seaweed processing. Robust and cold-adapted alginate lyases are urgently needed for industrial applications. In this study, a cold-adapted alginate lyase-producing strain Vibrio sp. W2 was screened. Then, the gene ALYW201 was cloned from Vibrio sp. W2 and expressed in a food-grade host, Yarrowia lipolytica. The secreted Alyw201 showed the activity of 64.2 U/mL, with a molecular weight of approximate 38.0 kDa, and a specific activity of 876.4 U/mg. Alyw201 performed the highest activity at 30 °C, and more than 80% activity at 25–40 °C. Furthermore, more than 70% of the activity was obtained in a broad pH range of 5.0–10.0. Alyw201 was also NaCl-independent and salt-tolerant. The degraded product was that of the oligosaccharides of DP (Degree of polymerization) 2–6. Due to its robustness and its unique pH-stable property, Alyw201 can be an efficient tool for industrial production.

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Characterization of a bifunctional alginate lyase as a new member of the polysaccharide lyase family 17 from a marine strain BP-2

Biotechnology Letters ◽

10.1007/s10529-019-02722-1 ◽

2019 ◽

Vol 41 (10) ◽

pp. 1187-1200 ◽

Cited By ~ 5

Author(s):

Guiyuan Huang ◽

Shunhua Wen ◽

Siming Liao ◽

Qiaozhen Wang ◽

Shihan Pan ◽

...

Keyword(s):

Alginate Lyase ◽

Polysaccharide Lyase ◽

Marine Strain

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Characterization of a Novel PolyM-Preferred Alginate Lyase from Marine Vibrio splendidus OU02

Marine Drugs ◽

10.3390/md16090295 ◽

2018 ◽

Vol 16 (9) ◽

pp. 295 ◽

Cited By ~ 12

Author(s):

Jingjing Zhuang ◽

Keke Zhang ◽

Xiaohua Liu ◽

Weizhi Liu ◽

Qianqian Lyu ◽

...

Keyword(s):

Biological Activities ◽

Alginate Lyase ◽

Potential Candidate ◽

Vibrio Splendidus ◽

Polysaccharide Lyase ◽

Alginate Oligosaccharides ◽

Marine Vibrio ◽

Alginate Oligosaccharide ◽

Alginate Lyases

Alginate lyases are enzymes that degrade alginate into oligosaccharides which possess a variety of biological activities. Discovering and characterizing novel alginate lyases has great significance for industrial and medical applications. In this study, we reported a novel alginate lyase, AlyA-OU02, derived from the marine Vibrio splendidus OU02. The BLASTP searches showed that AlyA-OU02 belonged to polysaccharide lyase family 7 (PL7) and contained two consecutive PL7 domains, which was rare among the alginate lyases in PL7 family. Both the two domains, AlyAa and AlyAb, had lyase activities, while AlyAa exhibited polyM preference, and AlyAb was polyG-preferred. In addition, the enzyme activity of AlyAa was much higher than AlyAb at 25 °C. The full-length enzyme of AlyA-OU02 showed polyM preference, which was the same as AlyAa. AlyAa degraded alginate into di-, tri-, and tetra-alginate oligosaccharides, while AlyAb degraded alginate into tri-, tetra-, and penta-alginate oligosaccharides. The degraded products of AlyA-OU02 were similar to AlyAa. Our work provided a potential candidate in the application of alginate oligosaccharide production and the characterization of the two domains might provide insights into the use of alginate of this organism.

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Cloning, Expression, and Characterization of a Cold-Adapted and Surfactant-Stable Alginate Lyase from Marine Bacterium Agarivorans sp. L11

Journal of Microbiology and Biotechnology ◽

10.4014/jmb.1409.09031 ◽

2015 ◽

Vol 25 (5) ◽

pp. 681-686 ◽

Cited By ~ 24

Author(s):

Shangyong Li ◽

Xuemei Yang ◽

Lan Zhang ◽

Wengong Yu ◽

Feng Han

Keyword(s):

Marine Bacterium ◽

Alginate Lyase ◽

Cold Adapted ◽

Surfactant Stable

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Structural basis for the exolytic activity of polysaccharide lyase family 6 alginate lyase BcAlyPL6 from human gut microbe Bacteroides clarus

Biochemical and Biophysical Research Communications ◽

10.1016/j.bbrc.2021.02.040 ◽

2021 ◽

Vol 547 ◽

pp. 111-117

Author(s):

Bing Wang ◽

Sheng Dong ◽

Fu-Li Li ◽

Xiao-Qing Ma

Keyword(s):

Alginate Lyase ◽

Structural Basis ◽

Human Gut ◽

Polysaccharide Lyase ◽

Gut Microbe

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Specificities and Synergistic Actions of Novel PL8 and PL7 Alginate Lyases from the Marine Fungus Paradendryphiella salina

Journal of Fungi ◽

10.3390/jof7020080 ◽

2021 ◽

Vol 7 (2) ◽

pp. 80

Author(s):

Bo Pilgaard ◽

Marlene Vuillemin ◽

Jesper Holck ◽

Casper Wilkens ◽

Anne S. Meyer

Keyword(s):

Alginate Lyase ◽

Marine Fungus ◽

Brown Macroalgae ◽

Polysaccharide Lyases ◽

Alginate Lyases ◽

Encoding Genes ◽

Substrate Affinities ◽

Alginate Degradation ◽

Insight Into

Alginate is an anionic polysaccharide abundantly present in the cell walls of brown macroalgae. The enzymatic depolymerization is performed solely by alginate lyases (EC 4.2.2.x), categorized as polysaccharide lyases (PLs) belonging to 12 different PL families. Until now, the vast majority of the alginate lyases have been found in bacteria. We report here the first extensive characterization of four alginate lyases from a marine fungus, the ascomycete Paradendryphiella salina, a known saprophyte of seaweeds. We have identified four polysaccharide lyase encoding genes bioinformatically in P. salina, one PL8 (PsMan8A), and three PL7 alginate lyases (PsAlg7A, -B, and -C). PsMan8A was demonstrated to exert exo-action on polymannuronic acid, and no action on alginate, indicating that this enzyme is most likely an exo-acting polymannuronic acid specific lyase. This enzyme is the first alginate lyase assigned to PL8 and polymannuronic acid thus represents a new substrate specificity in this family. The PL7 lyases (PsAlg7A, -B, and -C) were found to be endo-acting alginate lyases with different activity optima, substrate affinities, and product profiles. PsAlg7A and PsMan8A showed a clear synergistic action for the complete depolymerization of polyM at pH 5. PsAlg7A depolymerized polyM to mainly DP5 and DP3 oligomers and PsMan8A to dimers and monosaccharides. PsAlg7B and PsAlg7C showed substrate affinities towards both polyM and polyG at pH 8, depolymerizing both substrates to DP9-DP2 oligomers. The findings elucidate how P. salina accomplishes alginate depolymerization and provide insight into an efficient synergistic cooperation that may provide a new foundation for enzyme selection for alginate degradation in seaweed bioprocessing.

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