(Q43020279)

English

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

scientific article published on 7 December 2013

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scholarly article

1 reference

Europe PubMed Central

12 November 2017

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

1 reference

Europe PubMed Central

12 November 2017

1 reference

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author name string

Yongjun Qin

1

1 reference

Europe PubMed Central

12 November 2017

Zongqing Huang

2

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Europe PubMed Central

12 November 2017

Ziduo Liu

3

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Europe PubMed Central

12 November 2017

publication date

7 December 2013

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Europe PubMed Central

12 November 2017

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Europe PubMed Central

12 November 2017

18

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Europe PubMed Central

12 November 2017

2

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Europe PubMed Central

12 November 2017

271-281

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Europe PubMed Central

12 November 2017

https://scigraph.springernature.com/pub.10.1007/s00792-013-0614-9

0 references

Highly thermostable, thermophilic, alkaline, SDS and chelator resistant amylase from a thermophilic Bacillus sp. isolate A3-15.

1 reference

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The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling

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Identification and characterization of a novel intracellular alkaline alpha-amylase from the hyperthermophilic bacterium Thermotoga maritima MSB8.

1 reference

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Toward the estimation of the absolute quality of individual protein structure models

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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Molecular basis of cold adaptation.

1 reference

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Cold-adapted enzymes: from fundamentals to biotechnology.

1 reference

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

1 reference

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A classification of glycosyl hydrolases based on amino acid sequence similarities

1 reference

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Characterisation of a highly stable alpha-amylase from the halophilic archaeon Haloarcula hispanica.

1 reference

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A highly thermoactive and salt-tolerant α-amylase isolated from a pilot-plant biogas reactor

1 reference

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Cloning, expression, purification, and characterization of cold-adapted α-amylase from Pseudoalteromonas arctica GS230.

1 reference

https://api.crossref.org/works/10.1007%2FS00792-013-0614-9

21 January 2018

Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes

1 reference

https://api.crossref.org/works/10.1007%2FS00792-013-0614-9

21 January 2018

Halophilic adaptation of enzymes

1 reference

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21 January 2018

Salt-dependent studies of NADP-dependent isocitrate dehydrogenase from the halophilic archaeon Haloferax volcanii

1 reference

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21 January 2018

Cloning, sequencing and expression of an alpha-amylase gene, amyA, from the thermophilic halophile Halothermothrix orenii and purification and biochemical characterization of the recombinant enzyme

1 reference

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Use of Dinitrosalicylic Acid Reagent for Determination of Reducing Sugar

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Alpha-amylase activity from the halophilic archaeon Haloferax mediterranei.

1 reference

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Phylogenetic diversity of sediment bacteria from the southern Cretan margin, Eastern Mediterranean Sea.

1 reference

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21 January 2018

Wangia profunda gen. nov., sp. nov., a novel marine bacterium of the family Flavobacteriaceae isolated from southern Okinawa Trough deep-sea sediment

1 reference

https://api.crossref.org/works/10.1007%2FS00792-013-0614-9

21 January 2018

The complete genome of Zunongwangia profunda SM-A87 reveals its adaptation to the deep-sea environment and ecological role in sedimentary organic nitrogen degradation

1 reference

https://api.crossref.org/works/10.1007%2FS00792-013-0614-9

21 January 2018

A neopullulanase-type alpha-amylase gene from Thermoactinomyces vulgaris R-47.

1 reference

https://api.crossref.org/works/10.1007%2FS00792-013-0614-9

21 January 2018

Purification and characterization of an organic-solvent-tolerant halophilic α-amylase from the moderately halophilic Nesterenkonia sp. strain F.

1 reference

https://api.crossref.org/works/10.1007%2FS00792-013-0614-9

21 January 2018

Molecular cloning and characterization of amylase from soil metagenomic library derived from Northwestern Himalayas

1 reference

https://api.crossref.org/works/10.1007%2FS00792-013-0614-9

21 January 2018

Cold-adapted enzymes.

1 reference

https://api.crossref.org/works/10.1007%2FS00792-013-0614-9

21 January 2018

Intrinsic halotolerance of the psychrophilic alpha-amylase from Pseudoalteromonas haloplanktis

1 reference

https://api.crossref.org/works/10.1007%2FS00792-013-0614-9

21 January 2018

Production and partial purification of alpha-amylase from a novel isolate Streptomyces gulbargensis

1 reference

https://api.crossref.org/works/10.1007%2FS00792-013-0614-9

21 January 2018

Crystal structure of the polyextremophilic alpha-amylase AmyB from Halothermothrix orenii: details of a productive enzyme-substrate complex and an N domain with a role in binding raw starch

1 reference

https://api.crossref.org/works/10.1007%2FS00792-013-0614-9

21 January 2018

Properties and applications of starch-converting enzymes of the α-amylase family

1 reference

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21 January 2018

Kinetic study of the irreversible thermal denaturation of Bacillus licheniformis alpha-amylase

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Salt-dependent thermo-reversible α-amylase: cloning and characterization of halophilic α-amylase from moderately halophilic bacterium, Kocuria varians

1 reference

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21 January 2018

Enzymatic analysis of an amylolytic enzyme from the hyperthermophilic archaeon Pyrococcus furiosus reveals its novel catalytic properties as both an alpha-amylase and a cyclodextrin-hydrolyzing enzyme

1 reference

https://api.crossref.org/works/10.1007%2FS00792-013-0614-9

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

1 reference

https://api.crossref.org/works/10.1007%2FS00792-013-0614-9

21 January 2018

Haloalkaliphilic maltotriose-forming alpha-amylase from the archaebacterium Natronococcus sp. strain Ah-36.

1 reference

https://pubmed.ncbi.nlm.nih.gov/24318109

12 December 2020

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Purification and characterization of the heat-labile alpha-amylase secreted by the psychrophilic bacterium TAC 240B

1 reference

https://pubmed.ncbi.nlm.nih.gov/24318109

12 December 2020

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Alpha-amylase from the hyperthermophilic archaebacterium Pyrococcus furiosus. Cloning and sequencing of the gene and expression in Escherichia coli

1 reference

https://pubmed.ncbi.nlm.nih.gov/24318109

12 December 2020

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/24318109

12 December 2020

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inferred from PubMed ID database lookup

Production of cold-adapted amylase by marine bacterium Wangia sp. C52: optimization, modeling, and partial characterization

1 reference

https://pubmed.ncbi.nlm.nih.gov/24318109

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based on heuristic

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Cloning and expression of an alpha-amylase encoding gene from the hyperthermophilic archaebacterium Thermococcus hydrothermalis and biochemical characterisation of the recombinant enzyme

1 reference

https://pubmed.ncbi.nlm.nih.gov/24318109

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based on heuristic

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Production and biochemical characterization of an Î±-amylase from the moderate halophileHalomonas meridiana

1 reference

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based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1007/S00792-013-0614-9

1 reference

Europe PubMed Central

12 November 2017

1 reference

Europe PubMed Central

12 November 2017

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