Characterization of a novel PL 17 family alginate lyase with exolytic and endolytic cleavage activity from marine bacterium Microbulbifer sp. SH-1

Yang, Jong Oh; Cui, Dandan; Ma, Shuo; Chen, Wenkang; Chen, Diwen; Shen, Hong

doi:10.1016/j.ijbiomac.2020.12.196

Cited by 38 publications

(29 citation statements)

References 57 publications

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“…For instance, the activities of AlyPL17 towards sodium alginate, polyM and polyG are2.0, 1.71 and 3.97 times higher than the activities ofAlg17B(MacDonald et al, 2016). Moreover, the activities of AlgSH17 towards sodium alginate, polyM and polyG were 55.62 U/mg, 116.8U/mg, 30.28U/mg, respectively, which are 14.53, 7.73 and 26.50 times lower than that of AlyPL17 (Yang et al, 2021). Accordingly, AlyPL17wasanexcellent tool for the degradation of alginate.…”

Section: Expression and Puri Cation Of Alypl17 And Its Truncated Mutantsmentioning

confidence: 90%

“…Additionally, AlgSH17 from Microbulbifer sp. SH-1 also possesses both endolytic and exolytic activity (Yang et al, 2021). To explore the functions of the two domains, we analyzed the products distribution of AlyPL17-N and AlyPL17-C.As shown in Fig.…”

Section: Expression and Puri Cation Of Alypl17 And Its Truncated Mutantsmentioning

confidence: 99%

“…In terms of temperature stability, AlyPL17 retains about 40%activityafter being incubated at 40 o C for 1h (Fig.4B), which was better than several PL17 family alginate lyases. For instance, OalC17 retains 20% of maximal activity after being incubated at 40 o C for 1h(Li et al, 2018), and AlgSH17 could only retain stability at 20-25 o C(Yang et al, 2021). Interestingly, the two truncated mutants exhibited excellent thermal stability, AlyPL17-N and AlyPL17-C could retain about 95% and 80% of its maximal activities after being incubated at 40 o C for1 h (Fig.4C).…”

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confidence: 92%

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Efficient Degradation of Alginate And Preparation of Unsaturated Monosaccharides By A Novel Alginate Lyase And Effects of Domain Truncation On Biochemical Characteristics, Degradation Patterns

Cao

Zheng

et al. 2021

Preprint

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BackgroundBrown algae are considered promising crops for the production of sustainable biofuels. However, its commercial application has been limited by lack of efficient methods for converting alginate into fermentable sugars. Recently, exo-type alginate lyases have received extensive attention due to their excellent ability of conversion of alginate into 4-deoxy-L-erythro-5-hexoseulose uronate (DEH), a promising material for bioethanol production and biorefinery systems.ResultsHerein, we cloned and characterized a novel alginate lyase AlyPL17 from Pedobacter hainanensis NJ-02. It possessed outstanding catalytic efficiency towards polymannuronic acid (polyM), polyguluronic acid (polyG) and alginate sodium, with kcat of 39.42 + 1.9 s-1, 32.53 + 0.88 s-1, and 38.30 + 2.12 s-1, respectively. In addition, AlyPL17 adopts a unique hybrid action mode to degrade alginate by the synergistic effect of two domains. Furthermore, the combination of AlyPL17 and AlyPL6 exhibited apparently synergistic effect for the preparation of unsaturated monosaccharides. ConclusionOverall, the results show that AlyPL17 is a PL17 exo-type alginate lyase with high activity and a high conversion rate at low/moderate temperatures, which provides a useful enzymatic tool for the conversion of brown algae into biofuels and enhance our understanding of the function of modular domain of alginate lyase.

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Section: Expression and Puri Cation Of Alypl17 And Its Truncated Mutantsmentioning

confidence: 90%

Section: Expression and Puri Cation Of Alypl17 And Its Truncated Mutantsmentioning

confidence: 99%

mentioning

confidence: 92%

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Efficient Degradation of Alginate And Preparation of Unsaturated Monosaccharides By A Novel Alginate Lyase And Effects of Domain Truncation On Biochemical Characteristics, Degradation Patterns

Cao

Zheng

et al. 2021

Preprint

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“…Amazingly, alginate lyases with both exolytic and endolytic cleavage activity also exist, such as a novel PL17 family alginate lyase from marine bacterium Microbulbifer sp. SH-1 [25].…”

Section: Classification Of Alginate Lyasesmentioning

confidence: 99%

Structure Characteristics, Biochemical Properties, and Pharmaceutical Applications of Alginate Lyases

et al. 2021

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Alginate, the most abundant polysaccharides of brown algae, consists of various proportions of uronic acid epimers α-L-guluronic acid (G) and β-D-mannuronic acid (M). Alginate oligosaccharides (AOs), the degradation products of alginates, exhibit excellent bioactivities and a great potential for broad applications in pharmaceutical fields. Alginate lyases can degrade alginate to functional AOs with unsaturated bonds or monosaccharides, which can facilitate the biorefinery of brown algae. On account of the increasing applications of AOs and biorefinery of brown algae, there is a scientific need to explore the important aspects of alginate lyase, such as catalytic mechanism, structure, and property. This review covers fundamental aspects and recent developments in basic information, structural characteristics, the structure–substrate specificity or catalytic efficiency relationship, property, molecular modification, and applications. To meet the needs of biorefinery systems of a broad array of biochemical products, alginate lyases with special properties, such as salt-activated, wide pH adaptation range, and cold adaptation are outlined. Withal, various challenges in alginate lyase research are traced out, and future directions, specifically on the molecular biology part of alginate lyases, are delineated to further widen the horizon of these exceptional alginate lyases.

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“…Generally, the degraded products of the exo-type lyase are monosaccharides that cleave the substrate from the chain ends [19]; the endo-type alginate lyase products are unsaturated alginate disaccharides, trisaccharides, and other oligosaccharides [20]. In addition, individual alginate lyases exhibit both endo-and exo-type activity [21]. Alginate lyases can be divided into several families of polysaccharide lyases (PL) as follows: PL-5, PL-6, PL-7, PL-14, PL-15, PL-17, PL-18, PL-31, PL-32, PL-36, and PL-39 [22].…”

Section: Introductionmentioning

confidence: 99%

Biochemical Characterization and Cold-Adaption Mechanism of a PL-17 Family Alginate Lyase Aly23 from Marine Bacterium Pseudoalteromonas sp. ASY5 and Its Application for Oligosaccharides Production

Tang

Jiao

et al. 2022

Marine Drugs

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As an important enzyme involved in the marine carbon cycle, alginate lyase has received extensive attention because of its excellent degradation ability on brown algae, which is widely utilized for alginate oligosaccharide preparation or bioethanol production. In comparison with endo-type alginate lyases (PL-5, PL-7, and PL-18 families), limited studies have focused on PL-17 family alginate lyases, especially for those with special characteristics. In this study, a novel PL-17 family alginate lyase, Aly23, was identified and cloned from the marine bacterium Pseudoalteromonas carrageenovora ASY5. Aly23 exhibited maximum activity at 35 °C and retained 48.93% of its highest activity at 4 °C, representing an excellent cold-adaptation property. Comparative molecular dynamics analysis was implemented to explore the structural basis for the cold-adaptation property of Aly23. Aly23 had a high substrate preference for poly β-D-mannuronate and exhibited both endolytic and exolytic activities; its hydrolysis reaction mainly produced monosaccharides, disaccharides, and trisaccharides. Furthermore, the enzymatic hydrolyzed oligosaccharides displayed good antioxidant activities to reduce ferric and scavenge radicals, such as hydroxyl, ABTS+, and DPPH. Our work demonstrated that Aly23 is a promising cold-adapted biocatalyst for the preparation of natural antioxidants from brown algae.

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Characterization of a novel PL 17 family alginate lyase with exolytic and endolytic cleavage activity from marine bacterium Microbulbifer sp. SH-1

Cited by 38 publications

References 57 publications

Efficient Degradation of Alginate And Preparation of Unsaturated Monosaccharides By A Novel Alginate Lyase And Effects of Domain Truncation On Biochemical Characteristics, Degradation Patterns

Efficient Degradation of Alginate And Preparation of Unsaturated Monosaccharides By A Novel Alginate Lyase And Effects of Domain Truncation On Biochemical Characteristics, Degradation Patterns

Structure Characteristics, Biochemical Properties, and Pharmaceutical Applications of Alginate Lyases

Biochemical Characterization and Cold-Adaption Mechanism of a PL-17 Family Alginate Lyase Aly23 from Marine Bacterium Pseudoalteromonas sp. ASY5 and Its Application for Oligosaccharides Production

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