Literature summary extracted from

Soares, L.N.; Falleiros, L.; Cabral, B.; Fischer, J.; Guidini, C.; Cardoso, V.; De Resende, M.; Ribeiro, E.
Improvement of recovered activity and stability of the aspergillus oryzae beta-galactosidase immobilized on duolite A568 by combination of immobilization methods (2017), Chem. Ind. Chem. Eng. Q., 23, 495-506 .

No PubMed abstract available

Application

EC Number	Application	Comment	Organism
3.2.1.23	synthesis	immobilization and stabilization of beta-galactosidase on Duolite A568 using a combination of physical adsorption, incubation at pH 9.0 and cross-linking with glutaraldehyde leads to a 44% increase in enzymatic activity as compared with a two-step immobilization process (adsorption and cross-linking). The immobilized enzyme presents a good thermal stability at temperatures around 50°C, and very good pH stability in the range from 1.5 to 9.0	Aspergillus oryzae

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.2.1.23	Aspergillus oryzae	-	-	-

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
3.2.1.23	commercial preparation	-	Aspergillus oryzae	-

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Release 2023.1 (January 2023)