Alginate lyase: Review of major sources and classification, properties, structure-function analysis and applications

Bioengineered. 2015;6(3):125-31. doi: 10.1080/21655979.2015.1030543. Epub 2015 Apr 1.

Abstract

Alginate lyases catalyze the degradation of alginate, a complex copolymer of α-L-guluronate and its C5 epimer β-D-mannuronate. The enzymes have been isolated from various kinds of organisms with different substrate specificities, including algae, marine mollusks, marine and terrestrial bacteria, and some viruses and fungi. With the progress of structural biology, many kinds of alginate lyases of different polysaccharide lyases families have been characterized by obtaining crystal structures, and the catalytic mechanism has also been elucidated. Combined with various studies, we summarized the source, classification and properties of the alginate lyases from different polysaccharide lyases families. The relationship between substrate specificity and protein sequence was also investigated.

Keywords: alginate lyase; applications; classification; structure; substrate specificity.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Alginates / chemistry
  • Amino Acid Sequence
  • Animals
  • Bacteria / enzymology
  • Fungi / enzymology
  • Glucuronic Acid / chemistry
  • Hexuronic Acids / chemistry
  • Molecular Sequence Data
  • Mollusca / enzymology
  • Oligosaccharides / biosynthesis
  • Polysaccharide-Lyases / chemistry*
  • Polysaccharide-Lyases / genetics*
  • Protein Conformation
  • Substrate Specificity
  • Viruses / enzymology

Substances

  • Alginates
  • Hexuronic Acids
  • Oligosaccharides
  • Glucuronic Acid
  • Polysaccharide-Lyases
  • poly(beta-D-mannuronate) lyase