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RevistaEnzyme and Microbial Technology
Año2020
Volumen132
Páginas 109397
Internacional

PECTIN LYASE IMMOBILIZATION USING THE GLUTARALDEHYDE CHEMISTRY INCREASES THE ENZYME OPERATION RANGE

Autores:Roberto Fernandez-Lafuente
Grupos de investigación:Optimización de biocatalizadores y bioprocesos enzimáticos
Lucas Dal Magro1,2, Jakub F. Kornecki2, Manuela P. Klein3, Rafael C. Rodrigues1* and Roberto Fernandez-Lafuente2*


Pectin lyase (from Rohapect 10L) was immobilized on glutaraldehyde supports at low ionic strength at pH 5, 6.5 or 8 and later incubated at pH 8 for 48 h. The activity recovery of the biocatalysts versus pectin was quite low, under 10 % for all of the immobilized biocatalyst at 20ºC. However, a high stabilization was found when the enzyme was immobilized at pH 5, (e.g., the immobilized enzyme kept 83 % of the activity when the free enzyme was fully inactivated (pH 4.8 and 55 ºC in 5 h)). This biocatalyst increased the activity versus pectin in an almost exponential way when temperature increased until reach the maximum temperature used in the study (90 ºC), conditions where the free enzyme was almost inactive. The immobilized biocatalyst was also active even at pH 9, where the free enzyme was fully inactive. This biocatalyst could be reused for pectin hydrolysis 5 times for 72 h reaction cycles at 40 ºC maintaining more than 90 % of the initial activity.
 
1Biotechnology, Bioprocess and Biocatalysis Group, Institute of Food Science and Technology, Federal University of Rio Grande do Sul, Av. Bento Gonçalves, 9500, P.O. Box 15090, ZC 91501-970, Porto Alegre, RS, Brazil.
2Department of Biocatalysis, ICP-CSIC, Campus UAM-CSIC, Cantoblanco, ZC 28049, Madrid, Spain
3Department of Nutrition, Federal University of Health Sciences of Porto Alegre (UFCSPA), ZC 90050-170, Porto Alegre, RS, Brazil.
Palabras clave:Enzyme stabilization, steric hindrances, pectin hydrolysis, diffusion limitations, enzyme hyperactivation under harsh conditions
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