2026-06-16T14:05:18Zhttps://repisalud.isciii.es/rest/oai/requestoai:repisalud.isciii.es:20.500.12105/52322024-09-27T10:05:09Zcom_20.500.12105_19604com_20.500.12105_2051col_20.500.12105_19607
Repisalud
author
Bassan, Juliana Cristina
author
de Souza Bezerra, Thais Milena
author
Peixoto, Guilherme
author
Paulino da Cruz, Clariana Zanutto
author
Martinez Galan, Julian Paul
author
dos Santos Vaz, Aline Buda
author
Garrido, Saulo Santesso
author
Filice, Marco
author
Monti, Rubens
funder
São Paulo Research Foundation
funder
Ministerio de Economía y Competitividad (España)
funder
Unión Europea. Fondo Europeo de Desarrollo Regional (FEDER/ERDF)
2017-10-30T13:32:24Z
2017-10-30T13:32:24Z
2016
Materials. 2016; 9(5):357
10.3390/ma9050357
1996-1944
Materials
http://hdl.handle.net/20.500.12105/5232
In this study, trypsin (Enzyme Comission 3.4.21.4) was immobilized in a low cost, lignocellulosic support (corn cob powder-CCP) with the goal of obtaining peptides with bioactive potential from cheese whey. The pretreated support was activated with glyoxyl groups, glutaraldehyde and IDA-glyoxyl. The immobilization yields of the derivatives were higher than 83\%, and the retention of catalytic activity was higher than 74\%. The trypsin-glyoxyl-CCP derivative was thermally stable at 65 degrees C, a value that was 1090-fold higher than that obtained with the free enzyme. The trypsin-IDA-glyoxyl-CCP and trypsin-glutaraldehyde-CCP derivatives had thermal stabilities that were 883-and five-fold higher, respectively, then those obtained with the free enzyme. In the batch experiments, trypsin-IDA-glyoxyl-CCP retained 91\% of its activity and had a degree of hydrolysis of 12.49\%, while the values for trypsin-glyoxyl-CCP were 87\% and 15.46\%, respectively. The stabilized derivative trypsin-glyoxyl-CCP was also tested in an upflow packed-bed reactor. The hydrodynamic characterization of this reactor was a plug flow pattern, and the kinetics of this system provided a relative activity of 3.04 +/- 0.01 U . g(-1) and an average degree of hydrolysis of 23\%, which were suitable for the production of potentially bioactive peptides.
eng
corn cob powder functionalized
Trypsin
Immobilization
Reactor
Whey protein hydrolysates
Peptides
LACTIC-ACID PRODUCTION
GREEN COCONUT FIBER
CORN COBS
HYDROTHERMAL TREATMENT
ACTIVATED SUPPORTS
AMINO-ACIDS
HYDROLYSIS
PRETREATMENT
BIOMASS
STABILIZATION
Immobilization of Trypsin in Lignocellulosic Waste Material to Produce Peptides with Bioactive Potential from Whey Protein
journal article
URL
https://repisalud.isciii.es/bitstreams/626ccc6b-ce9c-436a-9d98-ae3df74223c0/download
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MD5
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application/pdf
ImmobilizationOfTrypsinIn_2016
URL
https://repisalud.isciii.es/bitstreams/48f40c0a-68c4-4c70-a927-dc0f620f47a9/download
File
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8aa29009e2d3259726affce4e5fe762e
80811
text/plain
ImmobilizationOfTrypsinIn_2016.txt