Proteinases encapsulated in stimulated release liposomes for cheese ripening
Chymosin, a neutral proteinase from Bacillus subtilis and cardoon cyprosins, were co-encapsulated with phospholipase C in stimulated release liposomes. Encapsulated enzymes were added separately to milk to make cheese. Chymosin and the neutral proteinase accelerated α(s)-casein degradation in comparison with control cheese, whereas β-casein degradation was accelerated by neutral proteinase and cyprosins. Neutral proteinase yielded the highest increase in soluble nitrogen. Cheese flavour intensity was enhanced by the neutral proteinase and cyprosins but not by chymosin.
Main Authors: | , , , |
---|---|
Format: | journal article biblioteca |
Language: | eng |
Published: |
1997
|
Online Access: | http://hdl.handle.net/20.500.12792/3513 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
id |
dig-inia-es-20.500.12792-3513 |
---|---|
record_format |
koha |
spelling |
dig-inia-es-20.500.12792-35132020-12-15T09:47:49Z Proteinases encapsulated in stimulated release liposomes for cheese ripening Picon, A. Gaya, P. Medina, M. Nuñez, M. Chymosin, a neutral proteinase from Bacillus subtilis and cardoon cyprosins, were co-encapsulated with phospholipase C in stimulated release liposomes. Encapsulated enzymes were added separately to milk to make cheese. Chymosin and the neutral proteinase accelerated α(s)-casein degradation in comparison with control cheese, whereas β-casein degradation was accelerated by neutral proteinase and cyprosins. Neutral proteinase yielded the highest increase in soluble nitrogen. Cheese flavour intensity was enhanced by the neutral proteinase and cyprosins but not by chymosin. 2020-10-22T14:50:24Z 2020-10-22T14:50:24Z 1997 journal article http://hdl.handle.net/20.500.12792/3513 10.1023/A1018350901132 eng Attribution-NonCommercial-ShareAlike 4.0 International http://creativecommons.org/licenses/by-nc-sa/4.0/ open access |
institution |
INIA ES |
collection |
DSpace |
country |
España |
countrycode |
ES |
component |
Bibliográfico |
access |
En linea |
databasecode |
dig-inia-es |
tag |
biblioteca |
region |
Europa del Sur |
libraryname |
Biblioteca del INIA España |
language |
eng |
description |
Chymosin, a neutral proteinase from Bacillus subtilis and cardoon cyprosins, were co-encapsulated with phospholipase C in stimulated release liposomes. Encapsulated enzymes were added separately to milk to make cheese. Chymosin and the neutral proteinase accelerated α(s)-casein degradation in comparison with control cheese, whereas β-casein degradation was accelerated by neutral proteinase and cyprosins. Neutral proteinase yielded the highest increase in soluble nitrogen. Cheese flavour intensity was enhanced by the neutral proteinase and cyprosins but not by chymosin. |
format |
journal article |
author |
Picon, A. Gaya, P. Medina, M. Nuñez, M. |
spellingShingle |
Picon, A. Gaya, P. Medina, M. Nuñez, M. Proteinases encapsulated in stimulated release liposomes for cheese ripening |
author_facet |
Picon, A. Gaya, P. Medina, M. Nuñez, M. |
author_sort |
Picon, A. |
title |
Proteinases encapsulated in stimulated release liposomes for cheese ripening |
title_short |
Proteinases encapsulated in stimulated release liposomes for cheese ripening |
title_full |
Proteinases encapsulated in stimulated release liposomes for cheese ripening |
title_fullStr |
Proteinases encapsulated in stimulated release liposomes for cheese ripening |
title_full_unstemmed |
Proteinases encapsulated in stimulated release liposomes for cheese ripening |
title_sort |
proteinases encapsulated in stimulated release liposomes for cheese ripening |
publishDate |
1997 |
url |
http://hdl.handle.net/20.500.12792/3513 |
work_keys_str_mv |
AT picona proteinasesencapsulatedinstimulatedreleaseliposomesforcheeseripening AT gayap proteinasesencapsulatedinstimulatedreleaseliposomesforcheeseripening AT medinam proteinasesencapsulatedinstimulatedreleaseliposomesforcheeseripening AT nunezm proteinasesencapsulatedinstimulatedreleaseliposomesforcheeseripening |
_version_ |
1758004854304800768 |