Cited by 669Enzyme Production and CharacterizationPolysaccharides Composition and ApplicationsPolysaccharides and Plant Cell Walls

ALGINATE LYASE: review of major sources and enzyme characteristics, structure-function analysis, biological roles, and applications

Wong, Thiang Yian, Preston, Lori A., Schiller, Neal L.·2000·Annual Review of Microbiology

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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Crossref · 10.1146/annurev.micro.54.1.289

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Authors
Wong, T. Y., Preston, L. A., & Schiller, N. L.
Affiliations
University of California, Riverside (US)
Venue
Annual Review of Microbiology
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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