|PDB structures||RCSB PDB PDBe PDBsum|
Pullulanase (EC 18.104.22.168, limit dextrinase, amylopectin 6-glucanohydrolase, bacterial debranching enzyme, debranching enzyme, alpha-dextrin endo-1,6-alpha-glucosidase, R-enzyme, pullulan alpha-1,6-glucanohydrolase) is a specific kind of glucanase, an amylolytic exoenzyme, that degrades pullulan. It is produced as an extracellular, cell surface-anchored lipoprotein by Gram-negative bacteria of the genus Klebsiella. Type I pullulanases specifically attack α-1,6 linkages, while type II pullulanases are also able to hydrolyse α-1,4 linkages. It is also produced by some other bacteria and archaea. Pullulanase is used as a processing aid in grain processing biotechnology (production of ethanol and sweeteners).
Pullulanase is also known as pullulan-6-glucanohydrolase (Debranching enzyme). Its substrate, pullulan, is regarded as a chain of maltotriose units linked by alpha-1,6-glycosidic bonds. Pullulanase will hydrolytically cleave pullulan (alpha-glucan polysaccharides).
- Lee EY, Whelan WJ (1972). "Glycogen and starch debranching enzymes". In Boyer PD (ed.). The Enzymes. Vol. 5 (3rd ed.). New York: Academic Press. pp. 191–234.
- Bender H, Wallenfels K (1966). "Pullulanase (an amylopectin and glycogen debranching enzyme) from Aerobacter aerogenes". Methods Enzymol. Methods in Enzymology. 8: 555–559. doi:10.1016/0076-6879(66)08100-X. ISBN 9780121818081.
- Manners DJ (1997). "Observations on the specificity and nomenclature of starch debranching enzymes". J. Appl. Glycosci. 44: 83–85.