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

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

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

http://www.wikidata.org/entity/Q30643837

about

Crystal structure of calcium-free alpha-amylase from Bacillus sp. strain KSM-K38 (AmyK38) and its sodium ion binding sites Marine Microbiological Enzymes: Studies with Multiple Strategies and Prospects Cloning, sequencing, and characterization of a heat- and alkali-stable type I pullulanase from Anaerobranca gottschalkii.Improvement of alpha-amylase production by modulation of ribosomal component protein S12 in Bacillus subtilis 168.Structure-guided systems-level engineering of oxidation-prone methionine residues in catalytic domain of an alkaline α-amylase from Alkalimonas amylolytica for significant improvement of both oxidative stability and catalytic efficiency AmyM, a Novel Maltohexaose-Forming α-Amylase from Corallococcus sp. strain EGB.Heterologous expression, biochemical characterization, and overproduction of alkaline α-amylase from Bacillus alcalophilus in Bacillus subtilis.Structure-based engineering of methionine residues in the catalytic cores of alkaline amylase from Alkalimonas amylolytica for improved oxidative stability.Role of Trp140 at subsite -6 on the maltohexaose production of maltohexaose-producing amylase from alkalophilic Bacillus sp.707.Fusion of an oligopeptide to the N terminus of an alkaline α-amylase from Alkalimonas amylolytica simultaneously improves the enzyme's catalytic efficiency, thermal stability, and resistance to oxidation.Industrial applications of alkaliphiles and their enzymes--past, present and future.Alkaliphilic bacteria: applications in industrial biotechnology.A thermophilic alkalophilic α-amylase from Bacillus sp. AAH-31 shows a novel domain organization among glycoside hydrolase family 13 enzymes.Determination of the effects of initial glucose on the production of α-amylase from Penicillium sp. under solid-state and submerged fermentation High external pH enables more efficient secretion of alkaline α-amylase AmyK38 by Bacillus subtilis Close relationship of a novel Flavobacteriaceae α-amylase with archaeal α-amylases and good potentials for industrial applications.Amylase production by solid-state fermentation of agro-industrial wastes using Bacillus sp.Purification and characterization of a liquefying α-amylase from alkalophilic thermophilic Bacillus sp. AAH-31.A novel cold-active and salt-tolerant α-amylase from marine bacterium Zunongwangia profunda: molecular cloning, heterologous expression and biochemical characterization.Deduced amino-acid sequence of a calcium-free alpha-amylase from a strain of Bacillus: implications from molecular modeling of high oxidation stability and chelator resistance of the enzyme.Production and properties of alpha-amylase from Penicillium chrysogenum and its application in starch hydrolysis.Halotolerant, acid-alkali stable, chelator resistant and raw starch digesting α-amylase from a marine bacterium Bacillus subtilis S8-18.Some properties of free and immobilized alpha-amylase from Penicillium griseofulvum by solid state fermentation.Functional and cooperative stabilization of a two-metal (Ca, Zn) center in α-amylase derived from Flavobacteriaceae species.2,3-butanediol production from starch by engineered Klebsiella pneumoniae G31-A.Production and characterization of partially purified extracellular thermostable α-amylase by Bacillus subtilis in submerged fermentation (SmF).Identification of α-amylase by random and specific mutagenesis of Texcoconibacillus texcoconensis 13CCT strain isolated from extreme alkaline-saline soil of the former Lake Texcoco (Mexico).Cloning, Purification and Characterization of a Highly Thermostable Amylase Gene of Thermotoga petrophila into Escherichia coli.Production, Purification, and Characterization of Thermostableα-Amylase Produced byBacillus licheniformisIsolate AI20

P2860

Q27641093-7F8B2C3D-9CE9-475F-8015-604100EE568B Q28076256-AEBCABC6-45B2-40CA-A4E4-55434882F3A0 Q31074244-13BE6B30-D4A6-4ECF-9F23-A760932778B1 Q34316118-C7FD09FE-BE1C-4794-A489-A5658366440B Q34647814-ECC33EE5-782B-4803-BAD0-C3E042C389BE Q35134155-A9FCD76D-C7BD-4511-A6FD-0C0A2C3DE9FC Q35477336-B7F069C8-6739-44D5-BCE5-F58A80EFCE1B Q36361845-67930576-CA86-47B2-9275-FD36BE4BD60B Q36473999-9791A4E4-2388-4EF0-9D19-5B521734FE95 Q36757219-F35D1ADC-583C-4FF5-8433-F59E0241CD2A Q37775947-9812441A-4BD7-4CF4-9B95-016D22DAB7EC Q37863573-15179107-489D-4FF8-B23A-D9D1EF90A716 Q38312735-595491AB-46E1-4E51-97C6-8D9742624377 Q40735371-8BD5E209-C828-4799-B1EB-5834D3452FBF Q41824377-B9BC9BA4-4128-4EF1-B865-39B8ABEB7D45 Q41949796-42502197-1B75-4CA5-AE0C-D159D95C25AE Q42594030-92CA1A4A-792E-4155-9358-755241F45F89 Q43016035-9C89A107-4FCF-4C08-A229-B7932B4634C1 Q43020279-5B0C3C4C-6AD3-4D9F-983D-23ED6FC018E7 Q43674575-149A2D91-E221-4D52-BBAD-F0EA178B1AEC Q46479747-391F24E2-7B7C-425E-9589-353B099E10DE Q46534949-0C906309-7139-435C-A689-C51B9EDDA613 Q46905080-684F3966-FD5E-4FB8-A653-32249478886E Q47141338-7C295273-F678-4645-971C-B017F9A9E8ED Q48033327-A0065443-CBC2-4A83-9586-7D9F73204AA7 Q51003601-7F333F7B-F865-40D9-80F8-EDD4E3C258B3 Q51499352-7A129224-0E6D-4A47-9249-CC93BBF4DFA0 Q54257332-8B6CCB37-E9AD-4804-9463-F2FD451802BF Q59010389-1554FA28-C026-4BF9-BE57-6045B5B0041A

P2860

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

http://www.wikidata.org/entity/Q30643837

description

2001 nî lūn-bûn

@nan

2001 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2001 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2001年の論文

@ja

2001年論文

@yue

2001年論文

@zh-hant

2001年論文

@zh-hk

2001年論文

@zh-mo

2001年論文

@zh-tw

2001年论文

@wuu

name

Novel alpha-amylase that is hi ...... ilic Bacillus isolate KSM-K38.

@ast

Novel alpha-amylase that is hi ...... ilic Bacillus isolate KSM-K38.

@en

type

label

Novel alpha-amylase that is hi ...... ilic Bacillus isolate KSM-K38.

@ast

Novel alpha-amylase that is hi ...... ilic Bacillus isolate KSM-K38.

@en

prefLabel

Novel alpha-amylase that is hi ...... ilic Bacillus isolate KSM-K38.

@ast

Novel alpha-amylase that is hi ...... ilic Bacillus isolate KSM-K38.

@en

P1433

Q30643837-04EFA66A-F5F3-466C-847F-25349CFA2087

P1476

Q30643837-E4D643F9-1BE5-464C-B9D5-11A6426AB669

P2093

Q30643837-205D0D1E-4E7A-4196-AB77-ABA352FCCA48

Q30643837-3059A1A7-EB9A-466E-9E26-2822BD31993A

Q30643837-6E1B5E4F-B5D2-474A-9A3E-C105E0483920

Q30643837-79945294-D99D-4CE4-989F-169BB3DFC253

Q30643837-A1485BF8-A3E4-4D42-B0D0-F742959B47E8

Q30643837-D3E27451-C1D8-475B-A01B-5F288B0470B0

Q30643837-D56CAAB3-4A29-4E47-A380-32BF4017AD75

Q30643837-F13269E3-96C4-46A5-9AAE-E936B4A67A47

P2860

Q30643837-1CFC3200-4023-4819-AB2D-F92B6D06FFF9

Q30643837-29113EE5-C2E7-49D6-AD23-EE36E74C47C1

Q30643837-37607AE8-9B1E-4023-8BC7-D144FE6D2C89

Q30643837-41FB8C07-22A9-4A0C-AE90-7A02F2E32602

Q30643837-47FA2FB3-111A-4887-965D-7489B4B82CF7

Q30643837-4B01022F-4469-4C6D-8EEE-D356B4F8FB08

Q30643837-4F8957A8-05F1-4B39-B7CF-8A1486D378AA

Q30643837-58A8A215-6D62-485F-9E29-BFB1BDCAC9D5

Q30643837-672DE31B-5BDD-42DD-BB70-7382A83A94E4

Q30643837-6A61CA73-3D3B-4C04-BA55-3254F2B40333

P304

Q30643837-827693C9-5F19-496A-8A44-B37929DEE53C

P31

Q30643837-C1D8A2C8-CF0C-4A72-B479-78A9DAA12572

P356

Q30643837-33A0AE6D-91FC-47B2-BBAA-5E5B04A68269

P407

Q30643837-083943CB-8C33-4E44-B74D-F8D5A30383AC

P433

Q30643837-5ABCF941-AFC0-4AAA-81EB-A3521D365CFA

P478

Q30643837-9732FEB0-1D3A-4A89-BC8E-9AA513EAE94B

P577

Q30643837-281D5789-4FE2-45F4-A648-2C46F9B452C9

P698

Q30643837-7DA7DF2E-D20C-4507-9520-8570DFCEA75E

P932

Q30643837-B227C87C-09A0-4B1D-984F-0E52A29B39A9

P356

AEM.67.4.1744-1750.2001

P1433

Applied and Environmental Microbiology

P1476

Novel alpha-amylase that is hi ...... ilic Bacillus isolate KSM-K38.

@en

P2093

H Hagihara

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

K Endo

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

K Igarashi

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

K Ikawa-Kitayama

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

K Ozaki

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

S Ito

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

S Kawai

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

Y Hayashi

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

P2860

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

The neighbor-joining method: a new method for reconstructing phylogenetic trees

Alkaliphiles: some applications of their products for biotechnology

Engineering an enzyme by site-directed mutagenesis to be resistant to chemical oxidation.

The effect on subtilisin activity of oxidizing a methionine residue.

General Biochemical Characterization of Thermostable Extracellular beta-Amylase from Clostridium thermosulfurogenes.

Unrelatedness of Bacillus amyloliquefaciens and Bacillus subtilis.

Amino acid sequence and molecular structure of an alkaline amylopullulanase from Bacillus that hydrolyzes alpha-1,4 and alpha-1,6 linkages in polysaccharides at different active sites.

P304

1744-1750

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

P31

scholarly article

P356

10.1128/AEM.67.4.1744-1750.2001

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

P407

P433

4

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

P478

67

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

P577

2001-04-01T00:00:00Z

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

P698

11282629

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

P932

92793

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