Format

Send to

Choose Destination
Appl Microbiol Biotechnol. 2008 May;79(2):165-78. doi: 10.1007/s00253-008-1423-4.

An overview of mannan structure and mannan-degrading enzyme systems.

Author information

1
Departamento de Biologia Celular, Laboratório de Enzimologia, Universidade de Brasília, CEP 70910-900 Brasília, DF, Brazil.

Abstract

Hemicellulose is a complex group of heterogeneous polymers and represents one of the major sources of renewable organic matter. Mannan is one of the major constituent groups of hemicellulose in the wall of higher plants. It comprises linear or branched polymers derived from sugars such as D-mannose, D-galactose, and D-glucose. The principal component of softwood hemicellulose is glucomannan. Structural studies revealed that the galactosyl side chain hydrogen interacts to the mannan backbone intramolecularly and provides structural stability. Differences in the distribution of D-galactosyl units along the mannan structure are found in galactomannans from different sources. Acetyl groups were identified and distributed irregularly in glucomannan. Some of the mannosyl units of galactoglucomannan are partially substituted by O-acetyl groups. Some unusual structures are found in the mannan family from seaweed, showing a complex system of sulfated structure. Endohydrolases and exohydrolases are involved in the breakdown of the mannan backbone to oligosaccharides or fermentable sugars. The main-chain mannan-degrading enzymes include beta-mannanase, beta-glucosidase, and beta-mannosidase. Additional enzymes such as acetyl mannan esterase and alpha-galactosidase are required to remove side-chain substituents that are attached at various points on mannan, creating more sites for subsequent enzymatic hydrolysis. Mannan-degrading enzymes have found applications in the pharmaceutical, food, feed, and pulp and paper industries. This review reports the structure of mannans and some biochemical properties and applications of mannan-degrading enzymes.

PMID:
18385995
DOI:
10.1007/s00253-008-1423-4
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Springer
Loading ...
Support Center