Amination of enzymes to improve biocatalyst performance: coupling genetic modification and physicochemical tools - Wikidata - awgldk - TriplyDB

Amination of enzymes to improve biocatalyst performance: coupling genetic modification and physicochemical tools

Amination of enzymes to improve biocatalyst performance: coupling genetic modification and physicochemical tools

http://www.wikidata.org/entity/Q58881989

about

Immobilization of Glycoside Hydrolase Families GH1, GH13, and GH70: State of the Art and Perspectives Agarose and Its Derivatives as Supports for Enzyme Immobilization Preparation and characterization of a highly stable phenoxazinone synthase nanogel Cocoa pod husk, a new source of hydrolase enzymes for preparation of cross-linked enzyme aggregate.New Strategy for the Immobilization of Lipases on Glyoxyl-Agarose Supports: Production of Robust Biocatalysts for Natural Oil Transformation.Dual, Site-Specific Modification of Antibodies by Using Solid-Phase Immobilized Microbial Transglutaminase.Stabilization of Candida antarctica Lipase B (CALB) Immobilized on Octyl Agarose by Treatment with Polyethyleneimine (PEI).Stabilization of Phenylalanine Ammonia Lyase from Rhodotorula glutinis by Encapsulation in Polyethyleneimine-Mediated Biomimetic Silica.Polyethylenimine: a very useful ionic polymer in the design of immobilized enzyme biocatalysts Preparation and characterization of a Combi-CLEAs from pectinases and cellulases: a potential biocatalyst for grape juice clarification Importance of the Support Properties for Immobilization or Purification of Enzymes

P2860

Q26739991-82485B45-D04C-41E8-8C30-8114A067DFEA Q28076089-41FCF656-FDD5-48E9-AADA-2AC45C867F5E Q36945296-15C15934-1C34-4AA9-9EDF-0A638BAA6D53 Q38367396-9DE2720C-EA4A-4965-9617-3887DD58BFF2 Q43205121-D233C796-30B7-4D05-83E1-D8484AF0B2BD Q47994940-D521BF09-ADD8-4754-B3BF-2CAD521C603F Q51685336-6F632497-9218-459F-A117-A17ADF322856 Q53530059-308E1149-37B2-40B1-8A55-6E3894200E1A Q58881920-DD8E3C86-679B-41BE-BB3A-85954FE423CA Q58881949-C8F71853-D39A-4EBA-812B-68E58F7CAC3B Q58881972-BB36A10F-4342-45F1-9DD3-6D40EAB657D9

P2860

Amination of enzymes to improve biocatalyst performance: coupling genetic modification and physicochemical tools

http://www.wikidata.org/entity/Q58881989

description

im Jahr 2014 veröffentlichter wissenschaftlicher Artikel

@de

wetenschappelijk artikel

@nl

наукова стаття, опублікована у 2014

@uk

name

Amination of enzymes to improv ...... tion and physicochemical tools

@en

Amination of enzymes to improv ...... tion and physicochemical tools

@nl

type

label

Amination of enzymes to improv ...... tion and physicochemical tools

@en

Amination of enzymes to improv ...... tion and physicochemical tools

@nl

prefLabel

Amination of enzymes to improv ...... tion and physicochemical tools

@en

Amination of enzymes to improv ...... tion and physicochemical tools

@nl

P1433

Q58881989-802D065B-81D8-4A3A-A3C2-E93687F59889

P1476

Q58881989-083E1162-2337-41D2-AF8F-0F146265F4E2

P2093

Q58881989-35DC7B0C-3BA1-4B00-8CA1-39B797AF81A8

Q58881989-9479C217-FFCE-4C8F-ADFD-D30C99C09AE3

Q58881989-C3A1A587-6A57-402E-8B72-35691F7BA801

P2860

Q58881989-00FBD419-07B7-4D53-B2E5-BB4E2BF8084A

Q58881989-031D5747-DFEB-4C81-A250-8A0C0039C7FC

Q58881989-053FFD7A-6E9D-48E7-A51B-BA37BC6F455C

Q58881989-056251C4-8AD8-491F-A2C7-AEEB77F922B5

Q58881989-069689AF-D2DC-4D1A-A0D8-1C3932BB2C36

Q58881989-102467A2-2A16-4163-A2A5-FDF8EEE42F06

Q58881989-118B5803-9BA8-4BB6-9DB3-7F7154F359EB

Q58881989-11ADDCDF-CBF4-48F2-8CF8-68B1404F51D2

Q58881989-130BD9F7-CE1E-4FBF-889B-18078EE38D06

Q58881989-14363467-8BDF-469F-B2A4-B4B34D82B059

P304

Q58881989-D3BD9FAA-2C8F-401A-92BE-520C06F7EA4A

P31

Q58881989-4650D6C0-B233-4619-927E-869006F2755D

P356

Q58881989-330E4426-E0AB-4EF4-AD94-1B0903EFCD0F

P433

Q58881989-6A90C63E-F5A1-41A0-A396-1E4EF312248F

P478

Q58881989-00C4BD94-7854-4B0A-A61D-8EF4728CEDBC

P50

Q58881989-3015BC74-BBE7-4347-AB8C-BB6393DBC1FE

Q58881989-652364D5-E4C1-4440-B7AA-2AF81DC6AC9F

Q58881989-C8D51592-881E-4E72-BD39-F338FEC874DF

P577

Q58881989-D36B4C83-5E7E-4147-8701-9F135709131E

P356

P1433

P1476

Amination of enzymes to improv ...... tion and physicochemical tools

@en

P2093

Claudia Ortiz

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

Roberto Fernandez-Lafuente

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

Rodrigo Torres

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

P2860

Enzyme immobilization: an update

Structural origins of the interfacial activation in Thermomyces (Humicola) lanuginosa lipase

Crystal structures of penicillin acylase enzyme-substrate complexes: structural insights into the catalytic mechanism

Crystal structure of a laccase from the fungus Trametes versicolor at 1.90-A resolution containing a full complement of coppers

Crystal structures of glutaryl 7-aminocephalosporanic acid acylase: insight into autoproteolytic activation

Activation of bacterial thermoalkalophilic lipases is spurred by dramatic structural rearrangements

Preparation of potent cytotoxic ribonucleases by cationization: enhanced cellular uptake and decreased interaction with ribonuclease inhibitor by chemical modification of carboxyl groups

Directed evolution: tailoring biocatalysts for industrial applications

Polyionic and cysteine-containing fusion peptides as versatile protein tags.

Irreversible thermoinactivation of glucoamylase from Aspergillus niger and thermostabilization by chemical modification of carboxyl groups.

P304

38350-38374

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

P31

scholarly article

P356

10.1039/C4RA04625K

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

P433

72

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

P478

4

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

P50

Rafael C. Rodrigues

Ángel Berenguer-Murcia

Oveimar Barbosa

P577

2014-01-01T00:00:00Z

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