Pullulanase (EC 3.2.1.41, limit dextrinase, amylopectin 6-glucanohydrolase, bacterial debranching enzyme, debranching enzyme, α-dextrin endo-1,6-α-glucosidase, R-enzyme, pullulan α-1,6-glucanohydrolase) is a specific kind of glucanase, an amylolytic exoenzyme, that degrades pullulan.^[1]^[2]^[3] 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 α-1,6-glycosidic bonds. Pullulanase will hydrolytically cleave pullulan (α-glucan polysaccharides).

Pullulanase enzyme in the food industry

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In the food industry, pullulanase works well as an ingredient. Pullulan can be applied directly to foods as a protective glaze or edible film due to its ability to form films. It can be used as a spice and flavoring agent for micro-encapsulation.^[4] It is used in mayonnaise to maintain consistency and quality. It is additionally used in low-calorie food formulations as a starch replacement.

Pullulanase can be used to convert starches in grains into fermentable sugars, which yeast can use to produce alcohol during fermentation.

References

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^ 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". Complex Carbohydrates. Methods in Enzymology. Vol. 8. pp. 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.
^ Yatmaz E, Turhan (1995). "Pullulan production by fermentation and usage in the food industry". GIDA-Journal of Food. 2: 95–102.

External links

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pullulanase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

Hydrolase: sugar hydrolases (EC 3.2)

3.2.1: Glycoside hydrolases

Disaccharidase	Sucrase/Sucrase-isomaltase/Invertase Maltase Trehalase Lactase
Glucosidases	Cellulase Alpha-glucosidase Acid Neutral AB Neutral C Beta-glucosidase cytosolic Debranching enzyme
Other	Amylase Alpha-amylase Chitinase Lysozyme Neuraminidase NEU1 NEU2 NEU3 NEU4 Bacterial neuraminidase Viral neuraminidase Galactosidases Alpha Beta alpha-Mannosidase Glucuronidase Klotho Hyaluronidase Pullulanase Glucosylceramidase lysosomal non-lysosomal Galactosylceramidase Alpha-N-acetylgalactosaminidase NAGA Alpha-N-acetylglucosaminidase Fucosidase Hexosaminidase HEXA HEXB Iduronidase Maltase-glucoamylase Heparanase HPSE2

3.2.2: Hydrolysing
N-Glycosyl compounds

DNA glycosylases: Oxoguanine glycosylase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)