Effect of Tris Buffer in the Intensity of the Multipoint Covalent Immobilization of Enzymes in Glyoxyl-Agarose Beads

Authors: Braham, SA; Morellon-Sterling, R; de Andrades, D; Rodrigues, RC; Siar, EH; Aksas, A; Pedroche, J; Millan, MD; Fernandez-Lafuente, R

Article; Early Access.
Appl. Biochem. Biotechnol.. vol: . page: 0273-2289.
Date: . .
Doi: 10.1007/s12010-021-03570-4.

Abstract:
Tris is an extensively used buffer that presents a primary amine group on its structure. In the present work trypsin, chymotrypsin and penicillin G acylase (PGA) [read more]

Two additives to improve stability of immobilized lipase

Authors: Blanco, RM; Roldan, I

Article.
Biocatal. Biotransform.. vol: 36. page: 1024-2422.
Date: . 2018.
Doi: 10.1080/10242422.2017.1314466.

Abstract:
The presence of two different additives during non-covalent immobilization of lipase was studied. Lipase was immobilized via hydrophobic interactions on an amorphous silica with large pore size bearing octyl groups on the surface. Polyethyleneglycol (PEG) with different molecular weights (MW: 1500, 3000 and 10,000) [read more]

Optimization of the coating of octyl-CALB with ionic polymers to improve stability and decrease enzyme leakage

Authors: Fernandez-Lopez, L; Virgen-Ortiz, JJ; Pedrero, SG; Lopez-Carrobles, N; Gorines, BC; Otero, C; Fernandez-Lafuente, R

Article.
Biocatal. Biotransform.. vol: 36. page: 1024-2422.
Date: . 2018.
Doi: 10.1080/10242422.2016.1278212.

Abstract:
Lipase B from Candida antarctica (CALB) immobilized on octyl-agarose (OC) was submitted to coating with polyethylenimine (PEI) and dextran sulfate (DS). Using lowly loaded enzyme preparations, the properties of OC-CALB preparations hardly improved, suggesting [read more]

Calendar

septiembre 2021
L M X J V S D
 12345
6789101112
13141516171819
20212223242526
27282930  
Go to Top