Optimization of enzymatic saccharification of fucoidan and alginate from brown seaweed using fucoidanase and alginate lyase from the marine fungus Dendryphiella arenaria

2018 ◽  
Vol 31 (3) ◽  
pp. 1955-1965 ◽  
Author(s):  
Mohamed Gomaa ◽  
Mustafa A. Fawzy ◽  
Awatief F. Hifney ◽  
Khayria M. Abdel-Gawad
Keyword(s):  
Enzymatic Saccharification ◽  
Brown Seaweed ◽  
Alginate Lyase ◽  
Marine Fungus

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

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.

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

Marine Drugs ◽  
2020 ◽  
Vol 18 (8) ◽  
pp. 416
Author(s):  
Yan Ma ◽  
Jie Li ◽  
Xin-Yue Zhang ◽  
Hao-Dong Ni ◽  
Feng-Biao Wang ◽  
...  
Keyword(s):  
Metal Ion ◽  
Brown Seaweed ◽  
Alginate Lyase ◽  
Industrial Applications ◽  
Alginate Oligosaccharides ◽  
Potential Applications ◽  
Pharmaceutical Industries ◽  
Ph Range ◽  
Alginate Lyases

Alginate lyases play an important role in alginate oligosaccharides (AOS) preparation and brown seaweed processing. Many extracellular alginate lyases have been characterized to develop efficient degradation tools needed for industrial applications. However, few studies focusing on intracellular alginate lyases have been conducted. In this work, a novel intracellular alkaline alginate lyase Alyw202 from Vibrio sp. W2 was cloned, expressed and characterized. Secretory expression was performed in a food-grade host, Yarrowia lipolytica. Recombinant Alyw202 with a molecular weight of approximately 38.3 kDa exhibited the highest activity at 45 °C and more than 60% of the activity in a broad pH range of 3.0 to 10.0. Furthermore, Alyw202 showed remarkable metal ion-tolerance, NaCl independence and the capacity of degrading alginate into oligosaccharides of DP2-DP4. Due to the unique pH-stable and high salt-tolerant properties, Alyw202 has potential applications in the food and pharmaceutical industries.

scholarly journals Mechanistic basis for understanding the dual activities of the bifunctional Azotobacter vinelandii mannuronan C-5 epimerase and alginate lyase AlgE7

2021 ◽  
Author(s):  
Margrethe Gaardløs ◽  
Tonje Marita Bjerkan Heggeset ◽  
Anne Tøndervik ◽  
David Tezé ◽  
Birte Svensson ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Functional Properties ◽  
Catalytic Mechanism ◽  
Azotobacter Vinelandii ◽  
Brown Seaweed ◽  
Alginate Lyase ◽  
High Sequence Identity ◽  
Monomer Composition ◽  
Lyase Activity ◽  
Mechanistic Basis

The structure and functional properties of alginates are dictated by the monomer composition and molecular weight distribution. Mannuronan C-5 epimerases determine the monomer composition by catalysing the epimerization of β- d -mannuronic acid residues (M) into α- l -guluronic acid residues (G). The molecular weight is affected by alginate lyases, which catalyse a β-elimination mechanism that cleaves alginate chains. The reaction mechanisms for the epimerization and lyase reactions are similar and some enzymes can perform both reactions. These dualistic enzymes share high sequence identity with mannuronan C-5 epimerases without lyase activity. The mechanism behind their activity and the amino acid residues responsible for it are still unknown. We investigate mechanistic determinants involved in the bifunctional epimerase and lyase activity of AlgE7 from Azotobacter vinelandii . Based on sequence analyses, a range of AlgE7 variants were constructed and subjected to activity assays and product characterization by NMR. Our results show that calcium promotes lyase activity whereas NaCl reduces the lyase activity of AlgE7. By using defined poly-M and poly-MG substrates, the preferred cleavage sites of AlgE7 were found to be M|XM and G|XM, where X can be either M or G. From the study of AlgE7 mutants, R148 was identified as an important residue for the lyase activity, and the point mutant R148G resulted in an enzyme with only epimerase activity. Based on the results obtained in the present study we suggest a unified catalytic reaction mechanism for both epimerase and lyase activity where H154 functions as the catalytic base and Y149 as the catalytic acid. Importance Post-harvest valorisation and upgrading of algal constituents is a promising strategy in the development of a sustainable bioeconomy based on algal biomass. In this respect, alginate epimerases and lyases are valuable enzymes for tailoring of the functional properties of alginate, a polysaccharide extracted from brown seaweed with numerous applications in food, medicine, and material industries. By providing a better understanding of the catalytic mechanism and of how the two enzyme actions can be altered by changes in reaction conditions, this study opens for further applications of bacterial epimerases and lyases in enzymatic tailoring of alginate polymers.

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

Marine Drugs ◽  
2020 ◽  
Vol 18 (2) ◽  
pp. 95 ◽  
Author(s):  
Yong-Hui Zhang ◽  
Yuan Shao ◽  
Chao Jiao ◽  
Qiu-Ming Yang ◽  
Hui-Fen Weng ◽  
...  
Keyword(s):  
Marine Bacterium ◽  
Simulation Analysis ◽  
Biological Activities ◽  
Brown Seaweed ◽  
Alginate Lyase ◽  
Maximum Activity ◽  
Property A ◽  
Activation Effect ◽  
Salt Activation ◽  
Alginate Oligosaccharides

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.

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

Marine Drugs ◽  
2020 ◽  
Vol 18 (4) ◽  
pp. 189 ◽  
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.

Purification and partial characterization of an extracellular alginate lyase from Aspergillus oryzae isolated from brown seaweed

2010 ◽  
Vol 23 (4) ◽  
pp. 755-762 ◽  
Author(s):  
Ravindra Pal Singh ◽  
Vishal Gupta ◽  
Puja Kumari ◽  
Manoj Kumar ◽  
C. R. K. Reddy ◽  
...  
Keyword(s):  
Aspergillus Oryzae ◽  
Brown Seaweed ◽  
Alginate Lyase ◽  
Partial Characterization

scholarly journals Proteomic enzyme analysis of the marine fungus Paradendryphiella salina reveals alginate lyase as a minimal adaptation strategy for brown algae degradation

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Bo Pilgaard ◽  
Casper Wilkens ◽  
Florian-Alexander Herbst ◽  
Marlene Vuillemin ◽  
Nanna Rhein-Knudsen ◽  
...  
Keyword(s):  
Brown Algae ◽  
Alginate Lyase ◽  
Adaptation Strategy ◽  
Marine Fungus ◽  
Enzyme Analysis

Brown seaweed processing: enzymatic saccharification of Laminaria digitata requires no pre-treatment

2015 ◽  
Vol 28 (2) ◽  
pp. 1287-1294 ◽  
Author(s):  
Dirk Manns ◽  
Stinus K. Andersen ◽  
Bodo Saake ◽  
Anne S. Meyer
Keyword(s):  
Enzymatic Saccharification ◽  
Brown Seaweed ◽  
Laminaria Digitata ◽  
Pre Treatment
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