<?xml version="1.0" encoding="UTF-8"?><?xml-stylesheet type="text/xsl" href="static/style.xsl"?><OAI-PMH xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd"><responseDate>2026-06-14T03:29:10Z</responseDate><request verb="GetRecord" identifier="oai:repisalud.isciii.es:20.500.12105/5232" metadataPrefix="marc">https://repisalud.isciii.es/rest/oai/request</request><GetRecord><record><header><identifier>oai:repisalud.isciii.es:20.500.12105/5232</identifier><datestamp>2024-09-27T10:05:09Z</datestamp><setSpec>com_20.500.12105_19604</setSpec><setSpec>com_20.500.12105_2051</setSpec><setSpec>col_20.500.12105_19607</setSpec></header><metadata><record xmlns="http://www.loc.gov/MARC21/slim" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:doc="http://www.lyncode.com/xoai" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.loc.gov/MARC21/slim http://www.loc.gov/standards/marcxml/schema/MARC21slim.xsd">
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      <subfield code="a">Bassan, Juliana Cristina</subfield>
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      <subfield code="a">de Souza Bezerra, Thais Milena</subfield>
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      <subfield code="a">Peixoto, Guilherme</subfield>
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      <subfield code="a">Paulino da Cruz, Clariana Zanutto</subfield>
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      <subfield code="a">Martinez Galan, Julian Paul</subfield>
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      <subfield code="a">dos Santos Vaz, Aline Buda</subfield>
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      <subfield code="a">Garrido, Saulo Santesso</subfield>
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      <subfield code="a">Filice, Marco</subfield>
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      <subfield code="a">Monti, Rubens</subfield>
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      <subfield code="c">2016</subfield>
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      <subfield code="a">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.</subfield>
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      <subfield code="a">Materials. 2016; 9(5):357</subfield>
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      <subfield code="a">10.3390/ma9050357</subfield>
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      <subfield code="a">1996-1944</subfield>
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      <subfield code="a">Materials</subfield>
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      <subfield code="a">http://hdl.handle.net/20.500.12105/5232</subfield>
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      <subfield code="a">corn cob powder functionalized</subfield>
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      <subfield code="a">Trypsin</subfield>
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      <subfield code="a">Immobilization</subfield>
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      <subfield code="a">Reactor</subfield>
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      <subfield code="a">Whey protein hydrolysates</subfield>
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      <subfield code="a">Peptides</subfield>
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      <subfield code="a">LACTIC-ACID PRODUCTION</subfield>
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   <datafield tag="653" ind2=" " ind1=" ">
      <subfield code="a">GREEN COCONUT FIBER</subfield>
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      <subfield code="a">CORN COBS</subfield>
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      <subfield code="a">HYDROTHERMAL TREATMENT</subfield>
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      <subfield code="a">ACTIVATED SUPPORTS</subfield>
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      <subfield code="a">AMINO-ACIDS</subfield>
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      <subfield code="a">HYDROLYSIS</subfield>
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      <subfield code="a">BIOMASS</subfield>
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      <subfield code="a">STABILIZATION</subfield>
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      <subfield code="a">Immobilization of Trypsin in Lignocellulosic Waste Material to Produce Peptides with Bioactive Potential from Whey Protein</subfield>
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