A hyper-thermostable α-amylase from Pyrococcus furiosus accumulates in Nicotiana tabacum as functional aggregates.

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An Insight Into Ameliorating Production, Catalytic Efficiency, Thermostability and Starch Saccharification of Acid-Stable α-Amylases From Acidophiles

P2860

Q57490030-119B398A-2924-4E64-8775-96D5FBADC727

P2860

A hyper-thermostable α-amylase from Pyrococcus furiosus accumulates in Nicotiana tabacum as functional aggregates.

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http://www.wikidata.org/entity/Q36409521

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年學術文章

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2017年學術文章

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2017年學術文章

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name

A hyper-thermostable α-amylase ...... acum as functional aggregates.

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A hyper-thermostable α-amylase ...... acum as functional aggregates.

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type

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A hyper-thermostable α-amylase ...... acum as functional aggregates.

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A hyper-thermostable α-amylase ...... acum as functional aggregates.

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prefLabel

A hyper-thermostable α-amylase ...... acum as functional aggregates.

@ast

A hyper-thermostable α-amylase ...... acum as functional aggregates.

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P1476

A hyper-thermostable α-amylase ...... acum as functional aggregates.

@en

P2093

Hong Zhu

http://www.w3.org/2001/XMLSchema#string

L Bruce Reynolds

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P2860

The purification and characterization of an extremely thermostable alpha-amylase from the hyperthermophilic archaebacterium Pyrococcus furiosus.

Structure and transcription of the nopaline synthase gene region of T-DNA.

Spider dragline silk proteins in transgenic tobacco leaves: accumulation and field production.

Production and characterization of in planta transiently produced polygalacturanase from Aspergillus niger and its fusions with hydrophobin or ELP tags

Cloning, sequencing, and expression of the gene encoding extracellular alpha-amylase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme.

Cloning, sequencing, and expression of the gene encoding amylopullulanase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme.

Physical stability of proteins in aqueous solution: mechanism and driving forces in nonnative protein aggregation.

Characterization of Amylolytic Enzyme Activities Associated with the Hyperthermophilic Archaebacterium Pyrococcus furiosus.

Low-cost production of proinsulin in tobacco and lettuce chloroplasts for injectable or oral delivery of functional insulin and C-peptide

A new strategy to express the extracellular α-amylase from Pyrococcus furiosus in Bacillus amyloliquefaciens

P2888

s12896-017-0372-3

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scholarly article

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10.1186/S12896-017-0372-3

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http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

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Rima Menassa

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2017-06-19T00:00:00Z

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1086108464

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28629346

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P921

Nicotiana tabacum

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5477289

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A hyper-thermostable α-amylase from Pyrococcus furiosus accumulates in Nicotiana tabacum as functional aggregates.

about

P2860

P2860

A hyper-thermostable α-amylase from Pyrococcus furiosus accumulates in Nicotiana tabacum as functional aggregates.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P50

P577

P6179

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P50

P577

P6179

P698

P921

P932