Characterization of a Novel Alginate Lyase from Marine Bacterium Vibrio furnissii H1

Zhu, Xiaoyan; Li, Xiangqian; Shi, Hao; Zhou, Jia; Tan, Zhiyong; Yuan, Mengdi; Yao, Ping; Liu, Xiaoyan

doi:10.3390/md16010030

Cited by 35 publications

(26 citation statements)

References 42 publications

(53 reference statements)

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“…For instance, 0.2 mol/L NaCl can effectively increase the activity of AlyA-OU02 from Vibrio splendidus OU02 [24]. AlyH1 from Vibrio furnissii H1 has the highest activity in the presence of 0.3 mol/L NaCl [44]. A similar phenomenon is observed with AlgSH7.…”

Section: Discussionsupporting

confidence: 51%

Purification and Characterization of a Novel Endolytic Alginate Lyase from Microbulbifer sp. SH-1 and Its Agricultural Application

et al. 2020

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Alginate, an important acidic polysaccharide in marine multicellular algae, has attracted attention as a promising biomass resource for the production of medical and agricultural chemicals. Alginate lyase is critical for saccharification and utilization of alginate. Discovering appropriate and efficient enzymes for depolymerizing alginate into fermentable fractions plays a vital role in alginate commercial exploitation. Herein, a unique alginate lyase, AlgSH7, belonging to polysaccharide lyase 7 family is purified and characterized from an alginate-utilizing bacterium Microbulbifer sp. SH-1. The purified AlgSH7 shows a specific activity of 12,908.26 U/mg, and its molecular weight is approximately 66.4 kDa. The optimal temperature and pH of AlgSH7 are 40 °C and pH 9.0, respectively. The enzyme exhibits stability at temperatures below 30 °C and within an extensive pH range of 5.0–9.0. Metal ions including Na+, K+, Al3+, and Fe3+ considerably enhance the activity of the enzyme. AlgSH7 displays a preference for poly-mannuronic acid (polyM) and a very low activity towards poly-guluronic acid (polyG). TLC and ESI-MS analysis indicated that the enzymatic hydrolysates mainly include disaccharides, trisaccharides, and tetrasaccharides. Noteworthy, the alginate oligosaccharides (AOS) prepared by AlgSH7 have an eliciting activity against chilling stress in Chinese flowering cabbage (Brassica parachinensis L.). These results suggest that AlgSH7 has a great potential to design an effective process for the production of alginate oligomers for agricultural applications.

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Section: Discussionsupporting

confidence: 51%

Purification and Characterization of a Novel Endolytic Alginate Lyase from Microbulbifer sp. SH-1 and Its Agricultural Application

et al. 2020

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“…As shown in Figure 6 A, 200 mM NaCl could effectively enhance the activities of AlyA-OU02 and AlyA a , while moderately affecting AlyA b . Certain alginate lyases could be activated by NaCl, but were not resistant to high concentrations of NaCl, such as AlyH1 [ 36 ] and AlgA [ 39 ]. AlyA-OU02, AlyA a , and AlyA b all exhibited high salt tolerance, which was analogous to AlgM4 from marine bacterium Vibrio weizhoudaoensis M0101 [ 32 ].…”

Section: Resultsmentioning

confidence: 99%

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

et al. 2018

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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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“…from Sphingomonas sp. ZH0 (52°C) , the most commonly character- 5.6 mM 3.22 nmol/s 45.92 (Zhu, Li, et al, 2018) OalC6 Cellulophaga sp. SY116 It means that more than 80% of the enzyme activity can be maintained after treatment under certain conditions.…”

Section: Discussionmentioning

confidence: 99%

Cloning, expression, and characterization of a new pH‐ and heat‐stable alginate lyase from Pseudoalteromonas carrageenovora ASY5

et al. 2019

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Alginate lyase is important in marine alginate degradation, and its enzymatic hydrolysates are excellent antioxidants. Here, we cloned a new alginate lyase, that is, Alg823, from the Gram‐negative marine bacterium Pseudoalteromonas carrageenovora ASY5. The optimal temperature and pH of Alg823 were 55°C and pH 8.0, respectively. After 30 min of incubation at 50°C, Alg823 could maintain over 75.0% of the maximum enzyme activity, suggesting its thermostability. The recombinant alginate lyase retained more than 80.0% of the maximum enzyme activity after it was treated at pH 6.0–10.0 and 4°C for 24 hr, indicating its excellent pH stability. Mg2+, Ca2+, Na+, and K+ could promote enzyme activity. Alginate oligosaccharides obtained by degradation with Alg823 displayed an excellent ability to scavenge ABTS, hydroxyl, and DPPH radicals. Alg823 showed potential for novel applications in alginate oligosaccharide production because of its pH tolerance and heat adaptation. Practical applications Alginate oligosaccharides produced by alginate degradation possess favorable properties, such as low molecular weight, high stability, and co‐dissolution with water. These oligosaccharides also have many biological activities. As such, they have been widely explored. Alginate oligosaccharides are prepared via three methods, namely, physical, chemical, and enzymatic methods. In chemical method, operational processes are difficult to thereby possibly damaging the unique structure of polysaccharides and causing environmental pollution. Although physical methods can overcome some of the shortcomings of chemical methods, their reaction is still difficult to control, and products are complicated. Conversely, enzymatic methods can has advantages of mild conditions, single product, and less pollution. Furthermore, oligosaccharides prepared by enzymatic methods are more biologically active than those prepared by other methods. Thus, finding novel alginate lyase with high activity and stability is important for research and commercial purposes.

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Characterization of a Novel Alginate Lyase from Marine Bacterium Vibrio furnissii H1

Cited by 35 publications

References 42 publications

Purification and Characterization of a Novel Endolytic Alginate Lyase from Microbulbifer sp. SH-1 and Its Agricultural Application

Purification and Characterization of a Novel Endolytic Alginate Lyase from Microbulbifer sp. SH-1 and Its Agricultural Application

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

Cloning, expression, and characterization of a new pH‐ and heat‐stable alginate lyase from Pseudoalteromonas carrageenovora ASY5

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