Molecular cloning, expression, and biochemical characterization of a novel cold-active α-amylase from Bacillus sp. dsh19-1 (Q57092025)

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scientific article published on 23 June 2018

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English	Molecular cloning, expression, and biochemical characterization of a novel cold-active α-amylase from Bacillus sp. dsh19-1	scientific article published on 23 June 2018

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Europe PubMed Central

PubMed publication ID

29936543

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:29936543%20AND%20SRC:MED&resulttype=core&format=json

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title

Molecular cloning, expression, and biochemical characterization of a novel cold-active α-amylase from Bacillus sp. dsh19-1 (English)

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Europe PubMed Central

PubMed publication ID

29936543

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author name string

Shaohua Dou

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1

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PubMed publication ID

29936543

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:29936543%20AND%20SRC:MED&resulttype=core&format=json

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Naiyu Chi

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2

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29936543

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Xinshang Zhou

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3

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29936543

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Qingfang Zhang

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4

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PubMed publication ID

29936543

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Fei Pang

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5

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PubMed publication ID

29936543

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Zhilong Xiu

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6

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29936543

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English

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publication date

23 June 2018

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29936543

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published in

Extremophiles

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29936543

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volume

22

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29936543

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issue

5

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PubMed publication ID

29936543

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page(s)

739-749

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29936543

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Purification, characterization, and nucleotide sequence of the thermolabile alpha-amylase from the antarctic psychrotroph Alteromonas haloplanctis A23

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Novel alpha-amylase that is highly resistant to chelating reagents and chemical oxidants from the alkaliphilic Bacillus isolate KSM-K38.

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Purification and characterization of a cold-adapted alpha-amylase produced by Nocardiopsis sp. 7326 isolated from Prydz Bay, Antarctic

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New thermostable amylase from Bacillus cohnii US147 with a broad pH applicability

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Structure ofBacillus amyloliquefaciensα-amylase at high resolution: implications for thermal stability

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Cloning, Expression, Purification, and Characterization of Cold-Adapted α-Amylase from Pseudoalteromonas arctica GS230

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Structural analysis of CPF_2247, a novel α-amylase from Clostridium perfringens

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Purification and characterization of maltooligosaccharide-forming α-amylase from moderately halophilic Marinobacter sp. EMB8.

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Recombinant expression and characterization of an organic-solvent-tolerant α-amylase from Exiguobacterium sp. DAU5.

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Biochemical characterization of an extracellular polyextremophilic α-amylase from the halophilic archaeon Halorubrum xinjiangense

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A novel cold-active and salt-tolerant α-amylase from marine bacterium Zunongwangia profunda: molecular cloning, heterologous expression and biochemical characterization

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[Funding for Division of Microbiology in 2014 by National Natural Science Foundation of China]

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Characterization of a thermostable raw-starch hydrolyzing α-amylase from deep-sea thermophile Geobacillus sp.

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Cloning, enhanced expression and characterization of an α-amylase gene from a wild strain in B. subtilis WB800.

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Purification and characterization of a novel intracellular α-amylase with a wide variety of substrates hydrolysis and transglycosylation activity from Paenibacillus sp. SSG-1.

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Cloning and Characterization of Cold-Adapted α-Amylase from Antarctic Arthrobacter agilis

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Identifiers

DOI

10.1007/S00792-018-1034-7

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stated in

Europe PubMed Central

PubMed publication ID

29936543

reference URL

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:29936543%20AND%20SRC:MED&resulttype=core&format=json

retrieved

1 April 2020

PubMed publication ID

29936543

1 reference

stated in

Europe PubMed Central

PubMed publication ID

29936543

reference URL

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:29936543%20AND%20SRC:MED&resulttype=core&format=json

retrieved

1 April 2020

 

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