Porungo cheese whey: β-galactosidase production, characterization and lactose hydrolysis
Main Author: | |
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Publication Date: | 2021 |
Other Authors: | , |
Format: | Article |
Language: | eng |
Source: | Brazilian Journal of Food Technology |
Download full: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1981-67232021000100466 |
Summary: | Abstract This study evaluated the lactose hydrolysis by immobilized β-galactosidase, which was produced by Kluyveromyces marxianus using porungo cheese whey as substrate. Initially, the yeast was cultivated in porungo cheese medium at 30 °C and 200 rpm, showing a maximal β-galactosidase production of 14.19 U mL-1. The crude extract obtained was used to evaluate the enzymatic hydrolysis in lactose solution. The optimal pH and temperature of the free and immobilized enzyme was investigated, whereas the lactose hydrolysis was carried out using two enzyme solutions (total activities of 2 U and 6 U) for both forms of the biocatalyst. Ca-alginate immobilization of β-galactosidase increased optimal temperature range to 40 °C, compared to the value for the free enzyme, which was 37 °C. The optimal pH was also increased by immobilization to 7.0, from pH 6.5 observed for the free enzyme. The highest lactose hydrolysis conversion was 15.82% using 6 U of free enzyme and 13.77% for 2 U of immobilized enzyme. Although, free enzyme showed higher conversion rates in the initial reaction time, the immobilized enzyme kept operational stability throughout reaction time, suggesting the advantage of using this technology. The use of porungo cheese whey allowed to aggregate value to this agro-industrial by-product, with the concomitant production of β-galactosidase to be used in the food industry chain itself. |
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Porungo cheese whey: β-galactosidase production, characterization and lactose hydrolysisAgro-industrial residueβ-galactosidaseEnzymatic hydrolysisEnzyme immobilizationLactoseWheyAbstract This study evaluated the lactose hydrolysis by immobilized β-galactosidase, which was produced by Kluyveromyces marxianus using porungo cheese whey as substrate. Initially, the yeast was cultivated in porungo cheese medium at 30 °C and 200 rpm, showing a maximal β-galactosidase production of 14.19 U mL-1. The crude extract obtained was used to evaluate the enzymatic hydrolysis in lactose solution. The optimal pH and temperature of the free and immobilized enzyme was investigated, whereas the lactose hydrolysis was carried out using two enzyme solutions (total activities of 2 U and 6 U) for both forms of the biocatalyst. Ca-alginate immobilization of β-galactosidase increased optimal temperature range to 40 °C, compared to the value for the free enzyme, which was 37 °C. The optimal pH was also increased by immobilization to 7.0, from pH 6.5 observed for the free enzyme. The highest lactose hydrolysis conversion was 15.82% using 6 U of free enzyme and 13.77% for 2 U of immobilized enzyme. Although, free enzyme showed higher conversion rates in the initial reaction time, the immobilized enzyme kept operational stability throughout reaction time, suggesting the advantage of using this technology. The use of porungo cheese whey allowed to aggregate value to this agro-industrial by-product, with the concomitant production of β-galactosidase to be used in the food industry chain itself.Instituto de Tecnologia de Alimentos - ITAL2021-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1981-67232021000100466Brazilian Journal of Food Technology v.24 2021reponame:Brazilian Journal of Food Technologyinstname:Instituto de Tecnologia de Alimentos (ITAL)instacron:ITAL10.1590/1981-6723.03821info:eu-repo/semantics/openAccessMarim,Aline Vitória CorimGabardo,SabrinaAyub,Marco Antônio Záchiaeng2021-09-22T00:00:00Zoai:scielo:S1981-67232021000100466Revistahttp://bjft.ital.sp.gov.br/https://old.scielo.br/oai/scielo-oai.phpbjftsec@ital.sp.gov.br||bjftsec@ital.sp.gov.br1981-67231516-7275opendoar:2021-09-22T00:00Brazilian Journal of Food Technology - Instituto de Tecnologia de Alimentos (ITAL)false |
dc.title.none.fl_str_mv |
Porungo cheese whey: β-galactosidase production, characterization and lactose hydrolysis |
title |
Porungo cheese whey: β-galactosidase production, characterization and lactose hydrolysis |
spellingShingle |
Porungo cheese whey: β-galactosidase production, characterization and lactose hydrolysis Marim,Aline Vitória Corim Agro-industrial residue β-galactosidase Enzymatic hydrolysis Enzyme immobilization Lactose Whey |
title_short |
Porungo cheese whey: β-galactosidase production, characterization and lactose hydrolysis |
title_full |
Porungo cheese whey: β-galactosidase production, characterization and lactose hydrolysis |
title_fullStr |
Porungo cheese whey: β-galactosidase production, characterization and lactose hydrolysis |
title_full_unstemmed |
Porungo cheese whey: β-galactosidase production, characterization and lactose hydrolysis |
title_sort |
Porungo cheese whey: β-galactosidase production, characterization and lactose hydrolysis |
author |
Marim,Aline Vitória Corim |
author_facet |
Marim,Aline Vitória Corim Gabardo,Sabrina Ayub,Marco Antônio Záchia |
author_role |
author |
author2 |
Gabardo,Sabrina Ayub,Marco Antônio Záchia |
author2_role |
author author |
dc.contributor.author.fl_str_mv |
Marim,Aline Vitória Corim Gabardo,Sabrina Ayub,Marco Antônio Záchia |
dc.subject.por.fl_str_mv |
Agro-industrial residue β-galactosidase Enzymatic hydrolysis Enzyme immobilization Lactose Whey |
topic |
Agro-industrial residue β-galactosidase Enzymatic hydrolysis Enzyme immobilization Lactose Whey |
description |
Abstract This study evaluated the lactose hydrolysis by immobilized β-galactosidase, which was produced by Kluyveromyces marxianus using porungo cheese whey as substrate. Initially, the yeast was cultivated in porungo cheese medium at 30 °C and 200 rpm, showing a maximal β-galactosidase production of 14.19 U mL-1. The crude extract obtained was used to evaluate the enzymatic hydrolysis in lactose solution. The optimal pH and temperature of the free and immobilized enzyme was investigated, whereas the lactose hydrolysis was carried out using two enzyme solutions (total activities of 2 U and 6 U) for both forms of the biocatalyst. Ca-alginate immobilization of β-galactosidase increased optimal temperature range to 40 °C, compared to the value for the free enzyme, which was 37 °C. The optimal pH was also increased by immobilization to 7.0, from pH 6.5 observed for the free enzyme. The highest lactose hydrolysis conversion was 15.82% using 6 U of free enzyme and 13.77% for 2 U of immobilized enzyme. Although, free enzyme showed higher conversion rates in the initial reaction time, the immobilized enzyme kept operational stability throughout reaction time, suggesting the advantage of using this technology. The use of porungo cheese whey allowed to aggregate value to this agro-industrial by-product, with the concomitant production of β-galactosidase to be used in the food industry chain itself. |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021-01-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1981-67232021000100466 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1981-67232021000100466 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/1981-6723.03821 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Instituto de Tecnologia de Alimentos - ITAL |
publisher.none.fl_str_mv |
Instituto de Tecnologia de Alimentos - ITAL |
dc.source.none.fl_str_mv |
Brazilian Journal of Food Technology v.24 2021 reponame:Brazilian Journal of Food Technology instname:Instituto de Tecnologia de Alimentos (ITAL) instacron:ITAL |
instname_str |
Instituto de Tecnologia de Alimentos (ITAL) |
instacron_str |
ITAL |
institution |
ITAL |
reponame_str |
Brazilian Journal of Food Technology |
collection |
Brazilian Journal of Food Technology |
repository.name.fl_str_mv |
Brazilian Journal of Food Technology - Instituto de Tecnologia de Alimentos (ITAL) |
repository.mail.fl_str_mv |
bjftsec@ital.sp.gov.br||bjftsec@ital.sp.gov.br |
_version_ |
1752128702726012928 |