Drying of α-amylase by spray drying and freeze-drying - a comparative study
Autor(a) principal: | |
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Data de Publicação: | 2014 |
Outros Autores: | |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Brazilian Journal of Chemical Engineering |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322014000300005 |
Resumo: | This study is aimed at comparing two traditional methods of drying of enzymes and at verifying the efficiency of each one and their advantages and disadvantages. The experiments were performed with a laboratory spray dryer and freeze-dryer using α-amylase as the model enzyme. An experimental design in star revealed that spray drying is mainly influenced by the inlet air temperature and feed flow rate, which were considered to be the main factors influencing the enzymatic activity and water activity; the long period of material exposure to high temperatures causes a partial activity loss. In the experiments of freeze drying, three methods of freezing were used (freezer, acetone and dry ice, and liquid nitrogen) and samples subsequently freeze-dried for times ranging between 0-24 hours. The product obtained from the two techniques showed high enzymatic activity and low water activity. For the drying of heat-resistant enzymes, in which the product to be obtained does not have high added value, spray drying may be more economically viable because, in the freeze drying process, the process time can be considered as a limiting factor when choosing a technique. |
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Brazilian Journal of Chemical Engineering |
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Drying of α-amylase by spray drying and freeze-drying - a comparative studyα-amylaseSpray dryingFreeze-dryingExperimental designComparative studyThis study is aimed at comparing two traditional methods of drying of enzymes and at verifying the efficiency of each one and their advantages and disadvantages. The experiments were performed with a laboratory spray dryer and freeze-dryer using α-amylase as the model enzyme. An experimental design in star revealed that spray drying is mainly influenced by the inlet air temperature and feed flow rate, which were considered to be the main factors influencing the enzymatic activity and water activity; the long period of material exposure to high temperatures causes a partial activity loss. In the experiments of freeze drying, three methods of freezing were used (freezer, acetone and dry ice, and liquid nitrogen) and samples subsequently freeze-dried for times ranging between 0-24 hours. The product obtained from the two techniques showed high enzymatic activity and low water activity. For the drying of heat-resistant enzymes, in which the product to be obtained does not have high added value, spray drying may be more economically viable because, in the freeze drying process, the process time can be considered as a limiting factor when choosing a technique.Brazilian Society of Chemical Engineering2014-09-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322014000300005Brazilian Journal of Chemical Engineering v.31 n.3 2014reponame:Brazilian Journal of Chemical Engineeringinstname:Associação Brasileira de Engenharia Química (ABEQ)instacron:ABEQ10.1590/0104-6632.20140313s00002642info:eu-repo/semantics/openAccessJesus,S. S. deMaciel Filho,R.eng2014-09-17T00:00:00Zoai:scielo:S0104-66322014000300005Revistahttps://www.scielo.br/j/bjce/https://old.scielo.br/oai/scielo-oai.phprgiudici@usp.br||rgiudici@usp.br1678-43830104-6632opendoar:2014-09-17T00:00Brazilian Journal of Chemical Engineering - Associação Brasileira de Engenharia Química (ABEQ)false |
dc.title.none.fl_str_mv |
Drying of α-amylase by spray drying and freeze-drying - a comparative study |
title |
Drying of α-amylase by spray drying and freeze-drying - a comparative study |
spellingShingle |
Drying of α-amylase by spray drying and freeze-drying - a comparative study Jesus,S. S. de α-amylase Spray drying Freeze-drying Experimental design Comparative study |
title_short |
Drying of α-amylase by spray drying and freeze-drying - a comparative study |
title_full |
Drying of α-amylase by spray drying and freeze-drying - a comparative study |
title_fullStr |
Drying of α-amylase by spray drying and freeze-drying - a comparative study |
title_full_unstemmed |
Drying of α-amylase by spray drying and freeze-drying - a comparative study |
title_sort |
Drying of α-amylase by spray drying and freeze-drying - a comparative study |
author |
Jesus,S. S. de |
author_facet |
Jesus,S. S. de Maciel Filho,R. |
author_role |
author |
author2 |
Maciel Filho,R. |
author2_role |
author |
dc.contributor.author.fl_str_mv |
Jesus,S. S. de Maciel Filho,R. |
dc.subject.por.fl_str_mv |
α-amylase Spray drying Freeze-drying Experimental design Comparative study |
topic |
α-amylase Spray drying Freeze-drying Experimental design Comparative study |
description |
This study is aimed at comparing two traditional methods of drying of enzymes and at verifying the efficiency of each one and their advantages and disadvantages. The experiments were performed with a laboratory spray dryer and freeze-dryer using α-amylase as the model enzyme. An experimental design in star revealed that spray drying is mainly influenced by the inlet air temperature and feed flow rate, which were considered to be the main factors influencing the enzymatic activity and water activity; the long period of material exposure to high temperatures causes a partial activity loss. In the experiments of freeze drying, three methods of freezing were used (freezer, acetone and dry ice, and liquid nitrogen) and samples subsequently freeze-dried for times ranging between 0-24 hours. The product obtained from the two techniques showed high enzymatic activity and low water activity. For the drying of heat-resistant enzymes, in which the product to be obtained does not have high added value, spray drying may be more economically viable because, in the freeze drying process, the process time can be considered as a limiting factor when choosing a technique. |
publishDate |
2014 |
dc.date.none.fl_str_mv |
2014-09-01 |
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=S0104-66322014000300005 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-66322014000300005 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/0104-6632.20140313s00002642 |
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 |
Brazilian Society of Chemical Engineering |
publisher.none.fl_str_mv |
Brazilian Society of Chemical Engineering |
dc.source.none.fl_str_mv |
Brazilian Journal of Chemical Engineering v.31 n.3 2014 reponame:Brazilian Journal of Chemical Engineering instname:Associação Brasileira de Engenharia Química (ABEQ) instacron:ABEQ |
instname_str |
Associação Brasileira de Engenharia Química (ABEQ) |
instacron_str |
ABEQ |
institution |
ABEQ |
reponame_str |
Brazilian Journal of Chemical Engineering |
collection |
Brazilian Journal of Chemical Engineering |
repository.name.fl_str_mv |
Brazilian Journal of Chemical Engineering - Associação Brasileira de Engenharia Química (ABEQ) |
repository.mail.fl_str_mv |
rgiudici@usp.br||rgiudici@usp.br |
_version_ |
1754213174324756480 |