ReviewMarine life science & technology2022
Evolving strategies for marine enzyme engineering: recent advances on the molecular modification of alginate lyase.
Review in Marine life science & technology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 23 citations in OpenAlex.
- Preparation of Alginate Oligosaccharides by Autoclaving Pretreatment Combined with Enzymatic Method.Marine drugs · 2026Article
- Enzyme therapy as a promising strategy to overcome multi-drug resistance in pathogens: current advances, key challenges, and future directions.RSC advances · 2026Review
- Alginate oligosaccharides derived from tropical brown seaweeds as sustainable alternatives to antibiotic growth promoters in poultry nutrition: Functional mechanisms and production perspectives.Veterinary world · 2026Review
- Article
- Sustainable Production ofFoods (Basel, Switzerland) · 2024Review
- A bifunctional endolytic alginate lyase with two different lyase catalytic domains fromFrontiers in microbiology · 2024Article
- Expanding the application range of theMarine life science & technology · 2023Article
- Response ofMarine life science & technology · 2023Article
- Identification and characterization of a critical loop for the high activity of alginate lyase VaAly2 from the PL7_5 subfamily.Frontiers in microbiology · 2023Article
- An exploration of alginate oligosaccharides modulating intestinal inflammatory networksFrontiers in microbiology · 2023Review
- Improving the thermostability of alginate lyase FlAlyA with high expression by computer-aided rational design for industrial preparation of alginate oligosaccharides.Frontiers in bioengineering and biotechnology · 2022Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Alginate, an acidic polysaccharide, is formed by β-d-mannuronate (M) and α-l-guluronate (G). As a type of polysaccharide lyase, alginate lyase can efficiently degrade alginate into alginate oligosaccharides, having potential applications in the food, medicine, and agriculture fields. However, the application of alginate lyase has been limited due to its low catalytic efficiency and poor temperature stability. In recent years, various structural features of alginate lyase have been determined, resulting in modification strategies that can increase the applicability of alginate lyase, making it important to summarize and discuss the current evidence. In this review, we summarized the structural features and catalytic mechanisms of alginate lyase. Molecular modification strategies, such as rational design, directed evolution, conserved domain recombination, and non-catalytic domain truncation, are also described in detail. Lastly, the application of alginate lyase is discussed. This comprehensive summary can inform future applications of alginate lyases.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.