NDLI: Trehalose–Water–Salt Interactions Related to the Stability of β-Galactosidase in Supercooled Media ( Food Biophysics , Volume 3 , Issue 1 )

Content Provider	Springer Nature Link
Author	Santagapita, Patricio R. Buera, M. Pilar
Copyright Year	2007
Abstract	The conservation of desirable properties in foods and ingredients is often based on the maintenance of the amorphous metastable properties of the systems. Enzymes may be stabilized by drying in saccharide matrices, but a second excipient is generally required to improve sugar protective effects. The effect of electrolytes on the thermophysical properties of sugar systems is of special interest because of their major influence on water structure and their possible interactions with biomolecules. Salts affect the kinetics of very important changes in sugar systems such as crystallization. The purpose of the present work was to analyze fungal β-galactosidase stability in supercooled systems of trehalose-containing electrolytes (water soluble acetates, citrates, and chlorides of magnesium and potassium). The degree of sugar crystallization was also related to enzyme stability. Potassium citrate and acetate improved enzyme stability during freeze-drying and thermal treatment of samples at water activity (a $_{w}$) of 0.22. However, trehalose crystallization inhibition at a $_{w}$ = 0.43 (which was about 50–60%, related to the system without salt) impaired enzyme protection. Certain salts may act retarding sugar crystallization, but in the presence of salts, trehalose crystallization is even more critical because the enzyme is confined in a highly salt-concentrated region. Thus, crystallization inhibition by sugar–salt combinations should be carefully conducted.
Starting Page	87
Ending Page	93
Page Count	7
File Format	PDF
ISSN	15571858
Journal	Food Biophysics
Volume Number	3
Issue Number	1
e-ISSN	15571866
Language	English
Publisher	Springer US
Publisher Date	2008-02-01
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Enzyme stability Trehalose Salts Crystallization Freeze-drying Amorphous systems β-galactosidase Analytical Chemistry Biophysics/Biomedical Physics Food Science
Content Type	Text
Resource Type	Article
Subject	Analytical Chemistry Biophysics Bioengineering Food Science Applied Microbiology and Biotechnology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Trehalose–Water–Salt Interactions Related to the Stability of β-Galactosidase in Supercooled Media ( Food Biophysics , Volume 3 , Issue 3 )

Trehalose–Water–Salt Interactions Related to the Stability of β-Galactosidase in Supercooled Media

Stability of Biopolymer Particles Formed by Heat Treatment of β-lactoglobulin/Beet Pectin Electrostatic Complexes

Phase Transition Stability of Cocoa Butter Emulsions

Food Biophysics : Volume 3, Issue 3, September 2008

The State of Aggregation of Casein Affects the Storage Stability of Amorphous Sucrose, Lactose, and Their Mixtures

Ice Morphology: Fundamentals and Technological Applications in Foods

Food Biophysics : Volume 11, Issue 3, September 2016

Food Biophysics : Volume 1, Issue 3, September 2006

Trehalose–Water–Salt Interactions Related to the Stability of β-Galactosidase in Supercooled Media ( Food Biophysics , Volume 3 , Issue 1 )

Similar Documents

Trehalose–Water–Salt Interactions Related to the Stability of β-Galactosidase in Supercooled Media ( Food Biophysics , Volume 3 , Issue 3 )

Trehalose–Water–Salt Interactions Related to the Stability of β-Galactosidase in Supercooled Media

Stability of Biopolymer Particles Formed by Heat Treatment of β-lactoglobulin/Beet Pectin Electrostatic Complexes

Phase Transition Stability of Cocoa Butter Emulsions

Food Biophysics : Volume 3, Issue 3, September 2008

The State of Aggregation of Casein Affects the Storage Stability of Amorphous Sucrose, Lactose, and Their Mixtures

Ice Morphology: Fundamentals and Technological Applications in Foods

Food Biophysics : Volume 11, Issue 3, September 2016

Food Biophysics : Volume 1, Issue 3, September 2006

Trehalose–Water–Salt Interactions Related to the Stability of β-Galactosidase in Supercooled Media ( Food Biophysics , Volume 3 , Issue 1 )