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Alginate Lyase: Review of Major Sources and Enzyme Characteristics, Structure-Function Analysis, Biological Roles, and Applications
Abstract
Alginate lyases, characterized as either mannuronate (EC 4.2.2.3) or guluronate lyases (EC 4.2.2.11), catalyze the degradation of alginate, a complex copolymer of alpha-L-guluronate and its C5 epimer beta-D-mannuronate. Lyases have been isolated from a wide range of organisms, including algae, marine invertebrates, and marine and terrestrial microorganisms. This review catalogs the major characteristics of these lyases, the methods for analyzing these enzymes, as well as their biological roles. Analysis of primary sequence data identifies some markedly conserved motifs that should help elucidate functional domains. Information about the three-dimensional structure of a mannuronate lyase from Sphingomonas sp., combined with various mutagenesis studies, has identified residues that are important for catalytic activity in several lyases. Characterization of alginate lyases will enhance and expand the use of these enzymes to engineer novel alginate polymers for applications in various industrial, agricultural, and medical fields. In this review, we explore both past and present applications of this important enzyme and discuss its future prospects.
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“The degradation of alginate into unsaturated alginate oligomers (degree of polymerization 2-4) is carried out by endo-alginate lyases.”
From The Enzymatic Conversion of Major Algal and Cyanobacterial Carbohydrates to Bioethanol (2016) · cites this paper as Wong et al., 2000
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Metadata
- Authors
- Wong, T. Y., Preston, L. A., & Schiller, N. L.
- Affiliations
- University of California, Riverside (US)
- Venue
- Annual Review of Microbiology
- Publisher
- Annual Reviews
- Published
- 2000-10
- Volume
- 54
- Issue
- 1
- Pages
- 289-340
- ISSN
- 0066-4227 (ISSN-L)
- 1545-3251
- OpenAlex
- W2136250029
- Cited by
- 669
- References
- 267
- Citations by year
- 2026: 25 · 2025: 26 · 2024: 45 · 2023: 34 · 2022: 36 · 2021: 30 · 2020: 45 · 2019: 38 · 2018: 44 · 2017: 30 · 2016: 42 · 2015: 47 · 2014: 32 · 2013: 32 · 2012: 29
- FWCI
- 0.80
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Annual Review of Microbiology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01ai036325-05)
- National Institute of Allergy and Infectious Diseases (AI 36325)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Life Sciences › Agricultural and Biological Sciences › Food Science › Polysaccharides Composition and Applications
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Polysaccharides and Plant Cell Walls
- Keywords
- alginate lyase, alginate degradation, alginate depolymerization, enzyme structure-function, conserved motifs, Sphingomonas, catalytic residues, marine microorganisms, enzyme applications
- MeSH terms
- Alginates, Amino Acid Sequence, Animals, Gram-Negative Bacteria, Gram-Positive Bacteria, Invertebrates, Marine Biology, Molecular Sequence Data, Polysaccharide-Lyases, Eukaryota
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