Alginate Beads Containing Lactase: Stability and Microstructure

β-Galactosidase (lactase) is a widely used enzyme in the food industry; however, it has low stability against thermal and mechanical treatments. Due to this, the purpose of the present research was to analyze the encapsulation of lactase in alginate-Ca(II) beads in order to maintain its enzymatic ac...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autor principal: Santagapita, Patricio Román
Publicado: 2017
Materias:
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_15257797_v18_n6_p1785_TraffanoSchiffo
http://hdl.handle.net/20.500.12110/paper_15257797_v18_n6_p1785_TraffanoSchiffo
Aporte de:
id paper:paper_15257797_v18_n6_p1785_TraffanoSchiffo
record_format dspace
spelling paper:paper_15257797_v18_n6_p1785_TraffanoSchiffo2023-06-08T16:19:35Z Alginate Beads Containing Lactase: Stability and Microstructure Santagapita, Patricio Román Calcium Freezing Hybrid materials Microstructure Alginate beads Enzymatic activities Food industries Freezing/thawing Mechanical treatments Molecular mobility Outer diameters Technological improvements Alginate alginic acid alpha galactosidase excipient guar gum gum arabic lactase trehalose water alginic acid beta galactosidase galactan glucuronic acid hexuronic acid lactase mannan plant gum Article chemical composition crystallization enthalpy enzyme activity enzyme stability enzyme structure freeze thawing freezing glass transition temperature melting point moisture particle size preservation priority journal storage chemistry cold drug formulation drug stability kinetics procedures ultrastructure Alginates beta-Galactosidase Cold Temperature Drug Compounding Drug Stability Galactans Glucuronic Acid Gum Arabic Hexuronic Acids Kinetics Lactase Mannans Plant Gums Trehalose β-Galactosidase (lactase) is a widely used enzyme in the food industry; however, it has low stability against thermal and mechanical treatments. Due to this, the purpose of the present research was to analyze the encapsulation of lactase in alginate-Ca(II) beads in order to maintain its enzymatic activity toward freezing, freezing/thawing, and storage. Also, the effect of the addition of trehalose, and arabic and guar gums and their influence on the microstructure as well as on thermal properties and molecular mobility were studied. Lactase was successfully encapsulated in alginate-Ca(II) beads, and the inclusion of trehalose was critical for activity preservation toward treatments, being improved in guar gum-containing systems. The gums increased the Tm′ values, which represents a valuable technological improvement. Finally, the presence of secondary excipients affected the microstructure, showing rods with smaller outer diameter and with lower compactness than alginate-Ca(II) beads. Also, bead composition greatly affects the size, shape, and relaxation times. © 2017 American Chemical Society. Fil:Santagapita, P.R. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2017 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_15257797_v18_n6_p1785_TraffanoSchiffo http://hdl.handle.net/20.500.12110/paper_15257797_v18_n6_p1785_TraffanoSchiffo
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Calcium
Freezing
Hybrid materials
Microstructure
Alginate beads
Enzymatic activities
Food industries
Freezing/thawing
Mechanical treatments
Molecular mobility
Outer diameters
Technological improvements
Alginate
alginic acid
alpha galactosidase
excipient
guar gum
gum arabic
lactase
trehalose
water
alginic acid
beta galactosidase
galactan
glucuronic acid
hexuronic acid
lactase
mannan
plant gum
Article
chemical composition
crystallization
enthalpy
enzyme activity
enzyme stability
enzyme structure
freeze thawing
freezing
glass transition temperature
melting point
moisture
particle size
preservation
priority journal
storage
chemistry
cold
drug formulation
drug stability
kinetics
procedures
ultrastructure
Alginates
beta-Galactosidase
Cold Temperature
Drug Compounding
Drug Stability
Galactans
Glucuronic Acid
Gum Arabic
Hexuronic Acids
Kinetics
Lactase
Mannans
Plant Gums
Trehalose
spellingShingle Calcium
Freezing
Hybrid materials
Microstructure
Alginate beads
Enzymatic activities
Food industries
Freezing/thawing
Mechanical treatments
Molecular mobility
Outer diameters
Technological improvements
Alginate
alginic acid
alpha galactosidase
excipient
guar gum
gum arabic
lactase
trehalose
water
alginic acid
beta galactosidase
galactan
glucuronic acid
hexuronic acid
lactase
mannan
plant gum
Article
chemical composition
crystallization
enthalpy
enzyme activity
enzyme stability
enzyme structure
freeze thawing
freezing
glass transition temperature
melting point
moisture
particle size
preservation
priority journal
storage
chemistry
cold
drug formulation
drug stability
kinetics
procedures
ultrastructure
Alginates
beta-Galactosidase
Cold Temperature
Drug Compounding
Drug Stability
Galactans
Glucuronic Acid
Gum Arabic
Hexuronic Acids
Kinetics
Lactase
Mannans
Plant Gums
Trehalose
Santagapita, Patricio Román
Alginate Beads Containing Lactase: Stability and Microstructure
topic_facet Calcium
Freezing
Hybrid materials
Microstructure
Alginate beads
Enzymatic activities
Food industries
Freezing/thawing
Mechanical treatments
Molecular mobility
Outer diameters
Technological improvements
Alginate
alginic acid
alpha galactosidase
excipient
guar gum
gum arabic
lactase
trehalose
water
alginic acid
beta galactosidase
galactan
glucuronic acid
hexuronic acid
lactase
mannan
plant gum
Article
chemical composition
crystallization
enthalpy
enzyme activity
enzyme stability
enzyme structure
freeze thawing
freezing
glass transition temperature
melting point
moisture
particle size
preservation
priority journal
storage
chemistry
cold
drug formulation
drug stability
kinetics
procedures
ultrastructure
Alginates
beta-Galactosidase
Cold Temperature
Drug Compounding
Drug Stability
Galactans
Glucuronic Acid
Gum Arabic
Hexuronic Acids
Kinetics
Lactase
Mannans
Plant Gums
Trehalose
description β-Galactosidase (lactase) is a widely used enzyme in the food industry; however, it has low stability against thermal and mechanical treatments. Due to this, the purpose of the present research was to analyze the encapsulation of lactase in alginate-Ca(II) beads in order to maintain its enzymatic activity toward freezing, freezing/thawing, and storage. Also, the effect of the addition of trehalose, and arabic and guar gums and their influence on the microstructure as well as on thermal properties and molecular mobility were studied. Lactase was successfully encapsulated in alginate-Ca(II) beads, and the inclusion of trehalose was critical for activity preservation toward treatments, being improved in guar gum-containing systems. The gums increased the Tm′ values, which represents a valuable technological improvement. Finally, the presence of secondary excipients affected the microstructure, showing rods with smaller outer diameter and with lower compactness than alginate-Ca(II) beads. Also, bead composition greatly affects the size, shape, and relaxation times. © 2017 American Chemical Society.
author Santagapita, Patricio Román
author_facet Santagapita, Patricio Román
author_sort Santagapita, Patricio Román
title Alginate Beads Containing Lactase: Stability and Microstructure
title_short Alginate Beads Containing Lactase: Stability and Microstructure
title_full Alginate Beads Containing Lactase: Stability and Microstructure
title_fullStr Alginate Beads Containing Lactase: Stability and Microstructure
title_full_unstemmed Alginate Beads Containing Lactase: Stability and Microstructure
title_sort alginate beads containing lactase: stability and microstructure
publishDate 2017
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_15257797_v18_n6_p1785_TraffanoSchiffo
http://hdl.handle.net/20.500.12110/paper_15257797_v18_n6_p1785_TraffanoSchiffo
work_keys_str_mv AT santagapitapatricioroman alginatebeadscontaininglactasestabilityandmicrostructure
_version_ 1768546554846642176