Matryoshka enzyme encapsulation: Development of zymoactive hydrogel particles with efficient lactose hydrolysis capability
This report describes an efficient procedure for enzyme encapsulation and its application for the hydrolysis of lactose. The enzymatic material that has been developed consists of hydrogel particles (ca. 3–4 mm of diameter) composed of either alginate or an alginate-agarose combination, in which bacterial cells loaded with a thermostable β-galactosidase are embedded. The cells were rendered fully permeable to the substrate, either chromogenic p-nitrophenyl galactose or lactose, by thermal treatment at 75 °C. Hydrogel particles made of a mixture of alginate and agarose displayed high catalytic activity (i.e. 1 g of beads hydrolyze the lactose equivalent of 100 mL of milk in 15 min) and thermal stability: they could be reused at 75 °C for complete hydrolysis of 5% (w/v) lactose solution at least six consecutive times without significant loss of activity.
Main Authors: | , , , , , , |
---|---|
Other Authors: | |
Format: | artículo biblioteca |
Language: | English |
Published: |
Elsevier
2019-05-15
|
Subjects: | β-Galactosidase, Cell permeabilization, Enzyme immobilization, Lactose, Thermostable enzyme, |
Online Access: | http://hdl.handle.net/10261/183325 http://dx.doi.org/10.13039/501100003329 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
id |
dig-iata-es-10261-183325 |
---|---|
record_format |
koha |
spelling |
dig-iata-es-10261-1833252022-12-20T16:50:49Z Matryoshka enzyme encapsulation: Development of zymoactive hydrogel particles with efficient lactose hydrolysis capability Fabra, María José Pérez Bassart, Zaida Talens Perales, David Martínez Sanz, Marta López-Rubio, Amparo Marín Navarro, Julia Polaina Molina, Julio Ministerio de Economía y Competitividad (España) β-Galactosidase Cell permeabilization Enzyme immobilization Lactose Thermostable enzyme This report describes an efficient procedure for enzyme encapsulation and its application for the hydrolysis of lactose. The enzymatic material that has been developed consists of hydrogel particles (ca. 3–4 mm of diameter) composed of either alginate or an alginate-agarose combination, in which bacterial cells loaded with a thermostable β-galactosidase are embedded. The cells were rendered fully permeable to the substrate, either chromogenic p-nitrophenyl galactose or lactose, by thermal treatment at 75 °C. Hydrogel particles made of a mixture of alginate and agarose displayed high catalytic activity (i.e. 1 g of beads hydrolyze the lactose equivalent of 100 mL of milk in 15 min) and thermal stability: they could be reused at 75 °C for complete hydrolysis of 5% (w/v) lactose solution at least six consecutive times without significant loss of activity. This work was funded by grant AGL2016-75245-R from Spain's 'Secretaría de Estado de Investigación, Desarrollo e Innovación'.MJF was supported by a Ramon y Cajal contract (RYC2014-158) from the Spanish Ministerio de Economia; Industria y Competitividad. Peer reviewed 2019-06-05T06:55:05Z 2019-06-05T06:55:05Z 2019-05-15 artículo http://purl.org/coar/resource_type/c_6501 Food Hydrocolloids 96:171-177 (2019) 0268-005X http://hdl.handle.net/10261/183325 10.1016/j.foodhyd.2019.05.026 http://dx.doi.org/10.13039/501100003329 en #PLACEHOLDER_PARENT_METADATA_VALUE# info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/AGL2016-75245-R Postprint https://doi.org/10.1016/j.foodhyd.2019.05.026 Sí open Elsevier |
institution |
IATA ES |
collection |
DSpace |
country |
España |
countrycode |
ES |
component |
Bibliográfico |
access |
En linea |
databasecode |
dig-iata-es |
tag |
biblioteca |
region |
Europa del Sur |
libraryname |
Biblioteca del IATA España |
language |
English |
topic |
β-Galactosidase Cell permeabilization Enzyme immobilization Lactose Thermostable enzyme β-Galactosidase Cell permeabilization Enzyme immobilization Lactose Thermostable enzyme |
spellingShingle |
β-Galactosidase Cell permeabilization Enzyme immobilization Lactose Thermostable enzyme β-Galactosidase Cell permeabilization Enzyme immobilization Lactose Thermostable enzyme Fabra, María José Pérez Bassart, Zaida Talens Perales, David Martínez Sanz, Marta López-Rubio, Amparo Marín Navarro, Julia Polaina Molina, Julio Matryoshka enzyme encapsulation: Development of zymoactive hydrogel particles with efficient lactose hydrolysis capability |
description |
This report describes an efficient procedure for enzyme encapsulation and its application for the hydrolysis of lactose. The enzymatic material that has been developed consists of hydrogel particles (ca. 3–4 mm of diameter) composed of either alginate or an alginate-agarose combination, in which bacterial cells loaded with a thermostable β-galactosidase are embedded. The cells were rendered fully permeable to the substrate, either chromogenic p-nitrophenyl galactose or lactose, by thermal treatment at 75 °C. Hydrogel particles made of a mixture of alginate and agarose displayed high catalytic activity (i.e. 1 g of beads hydrolyze the lactose equivalent of 100 mL of milk in 15 min) and thermal stability: they could be reused at 75 °C for complete hydrolysis of 5% (w/v) lactose solution at least six consecutive times without significant loss of activity. |
author2 |
Ministerio de Economía y Competitividad (España) |
author_facet |
Ministerio de Economía y Competitividad (España) Fabra, María José Pérez Bassart, Zaida Talens Perales, David Martínez Sanz, Marta López-Rubio, Amparo Marín Navarro, Julia Polaina Molina, Julio |
format |
artículo |
topic_facet |
β-Galactosidase Cell permeabilization Enzyme immobilization Lactose Thermostable enzyme |
author |
Fabra, María José Pérez Bassart, Zaida Talens Perales, David Martínez Sanz, Marta López-Rubio, Amparo Marín Navarro, Julia Polaina Molina, Julio |
author_sort |
Fabra, María José |
title |
Matryoshka enzyme encapsulation: Development of zymoactive hydrogel particles with efficient lactose hydrolysis capability |
title_short |
Matryoshka enzyme encapsulation: Development of zymoactive hydrogel particles with efficient lactose hydrolysis capability |
title_full |
Matryoshka enzyme encapsulation: Development of zymoactive hydrogel particles with efficient lactose hydrolysis capability |
title_fullStr |
Matryoshka enzyme encapsulation: Development of zymoactive hydrogel particles with efficient lactose hydrolysis capability |
title_full_unstemmed |
Matryoshka enzyme encapsulation: Development of zymoactive hydrogel particles with efficient lactose hydrolysis capability |
title_sort |
matryoshka enzyme encapsulation: development of zymoactive hydrogel particles with efficient lactose hydrolysis capability |
publisher |
Elsevier |
publishDate |
2019-05-15 |
url |
http://hdl.handle.net/10261/183325 http://dx.doi.org/10.13039/501100003329 |
work_keys_str_mv |
AT fabramariajose matryoshkaenzymeencapsulationdevelopmentofzymoactivehydrogelparticleswithefficientlactosehydrolysiscapability AT perezbassartzaida matryoshkaenzymeencapsulationdevelopmentofzymoactivehydrogelparticleswithefficientlactosehydrolysiscapability AT talensperalesdavid matryoshkaenzymeencapsulationdevelopmentofzymoactivehydrogelparticleswithefficientlactosehydrolysiscapability AT martinezsanzmarta matryoshkaenzymeencapsulationdevelopmentofzymoactivehydrogelparticleswithefficientlactosehydrolysiscapability AT lopezrubioamparo matryoshkaenzymeencapsulationdevelopmentofzymoactivehydrogelparticleswithefficientlactosehydrolysiscapability AT marinnavarrojulia matryoshkaenzymeencapsulationdevelopmentofzymoactivehydrogelparticleswithefficientlactosehydrolysiscapability AT polainamolinajulio matryoshkaenzymeencapsulationdevelopmentofzymoactivehydrogelparticleswithefficientlactosehydrolysiscapability |
_version_ |
1777670084144136192 |