プルラナーゼ
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- 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 |
Identifiers |
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 |
PRIAM |
profile |
PDB structures |
RCSB PDB PDBe PDBsum |
Search |
PMC |
articles |
PubMed |
articles |
NCBI |
proteins |
|
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)
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
- Enzymatic Digestion Characteristics and Structure Analysis of Ginkgo (<i>Ginkgo biloba</i> L.) Starch Noodles
- Effect of Resistant Starch as Dietary Fiber Substitute on Cookies Quality Evaluation
Related Links
- Activity Pullulanase is an endo-type enzyme that cleaves α-1,6-glucosidic linkages in polysaccharides, such as amylopectin, glycogen, dextrin and pullulan. Pullulanase requires the branching chain to be of at least a maltose length ...
- 英語タイトル:Global Pullulanase (CAS 9075-68-7) Industry 2016 Market Research Report 商品コード:QYRCAS6083662 発行会社(調査会社):QYResearch 発行日:2016年12月 ページ数:約120 レポート言語:英語 ...
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