関: limit dextrinase

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/08/03 08:29:42」(JST)

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Pullulanase (EC 3.2.1.41, 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.^[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 alpha-1,6-glycosidic bonds. Pullulanase will hydrolytically cleave pullulan (alpha-glucan polysaccharides).

References

^ Lee, E.Y.C. and Whelan, W.J. (1972). "Glycogen and starch debranching enzymes". In Boyer, P.D. The Enzymes 5 (3rd ed.). New York: Academic Press. pp. 191–234.
^ Bender, H. and 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, D.J. (1997). "Observations on the specificity and nomenclature of starch debranching enzymes". J. Appl. Glycosci. 44: 83–85.

External links

pullulanase at the US National Library of Medicine Medical Subject Headings (MeSH)

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English Journal

Characterization of a pH and detergent-tolerant, cold-adapted type I pullulanase from Exiguobacterium sp. SH3.

Rajaei S1,2, Noghabi KA1, Sadeghizadeh M2, Zahiri HS3.
Extremophiles : life under extreme conditions.Extremophiles.2015 Nov;19(6):1145-55. doi: 10.1007/s00792-015-0786-6. Epub 2015 Sep 8.
A pullulanase-encoding gene from psychrotrophic Exiguobacterium sp. SH3 was cloned and expressed in both E. coli and Bacillus subtilis. The functional recombinant enzyme (Pul-SH3) was purified as a His-tagged protein. Pul-SH3 was characterized to be a cold-adapted type I pullulanase with maximum act
PMID 26349928

Identification of a novel alkaline amylopullulanase from a gut metagenome of Hermetia illucens.

Lee YS1, Seo SH1, Yoon SH1, Kim SY1, Hahn BS1, Sim JS1, Koo BS1, Lee CM2.
International journal of biological macromolecules.Int J Biol Macromol.2015 Oct 23. pii: S0141-8130(15)30070-2. doi: 10.1016/j.ijbiomac.2015.10.067. [Epub ahead of print]
A novel pullulanase gene, PulSS4, was identified from the gut microflora of Hermetia illucens by a function-based metagenome screening. The PulSS4 gene had an open reading frame of 4455 base pairs, and encoded a mature protein of 1484 amino acids, with a signal peptide sequence of 44 amino acids. Th
PMID 26526170

A novel cold-adapted type I pullulanase of Paenibacillus polymyxa Nws-pp2: in vivo functional expression and biochemical characterization of glucans hydrolyzates analysis.

Wei W1, Ma J2, Chen SQ2, Cai XH2, Wei DZ3.
BMC biotechnology.BMC Biotechnol.2015 Oct 19;15:96. doi: 10.1186/s12896-015-0215-z.
BACKGROUND: Pullulanase is an important debranching enzyme and has been widely utilized to hydrolyse the α-1,6 glucosidic linkages in starch/sugar industry. Selecting new bacterial strains or improving bacterial strains is a prerequisite and effective solution in industrial applications. Although m
PMID 26481143

Japanese Journal

Development of a new selection method and quality improvement of sugary-1 rice mutants

Breeding science 63(5), 461-467, 2014-01
NAID 40020012941

Enzymatic Digestion Characteristics and Structure Analysis of Ginkgo (<i>Ginkgo biloba</i> L.) Starch Noodles

Food Science and Technology Research 20(5), 997-1004, 2014
NAID 130004704879

Effect of Resistant Starch as Dietary Fiber Substitute on Cookies Quality Evaluation

Food Science and Technology Research 20(2), 263-272, 2014
NAID 130004463422

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Pullulanase
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EC number	3.2.1.41
CAS number	9075-68-7
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
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PDB structures	RCSB PDB PDBe PDBsum
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