Pullulanase

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  1. isopullulanase EC 3.2.1.57; an enzyme that catalyses the hydrolysis of pullulan to isopanose (i.e. 6-α-maltosylglucose).
  2. neopullulanase EC 3.2.1.135; an enzyme that catalyses the hydrolysis of pullulan to panose (i.e. 6-α-d-glucosylmaltose).
  3. see α-dextrin endo-1,6-α-glucosidase.

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Pullulanase 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 (EC 3.2.1.41) 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).

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