Related Experiment Video
Updated: Mar 19, 2026

08:50
Easy Manipulation of Architectures in Protein-based Hydrogels for Cell Culture Applications
Published on: August 4, 2017
7.3K
Freezing and Ice Structure Formed in Protein Gels
O Miyawaki1, T Abe1, T Yano1
1a Department of Agricultural Chemistry , The University of Tokyo , Bunkyo-ku, Tokyo 113 , Japan.
Bioscience, Biotechnology, and Biochemistry
|June 10, 2016
Summary
This study analyzed ice crystal growth in frozen soy protein and egg albumin gels. Findings show ice structure size is inversely related to freezing speed, highlighting molecular diffusion
Area of Science:
- Food science
- Materials science
- Physical chemistry
Background:
- Understanding ice crystal formation is crucial for food processing and preservation.
- Previous models for ice crystal growth have limitations in applicability.
Purpose of the Study:
- To photographically analyze ice structure in frozen soy protein curd and egg albumin gel.
- To investigate the relationship between ice structure size, freezing conditions, and heat flux.
- To validate a theoretical model for ice crystal growth.
Main Methods:
- Photographic analysis of ice structures in frozen food gels.
- Controlled freezing experiments under various conditions.
- Measurement of ice structure size at different locations relative to the cooling plate.
Main Results:
- Dendritic ice structures were observed growing parallel to heat flux.
- Mean ice structure size showed an inverse relationship with freezing front speed.
- Supercooling resulted in smaller ice structures due to rapid freezing.
Conclusions:
- Molecular diffusion plays a significant role in ice crystal growth.
- The proposed theoretical model offers a simpler basis and wider applicability than existing models.
Related Concept Videos
Protein and Protein Structure
91.6K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
A protein's shape is critical to its function. For example, an enzyme...
91.6K
Two-dimensional Gel Electrophoresis
8.1K
Two-dimensional gel electrophoresis is a high-resolution protein separation method first introduced by O' Farrell and Klose in 1975. This method involves protein separation by two dimensions, mass and charge, making it more accurate than one-dimensional gel electrophoresis.
The first dimension separation uses the isoelectric focusing or IEF technique performed on immobilized pH gradient (IPG) strips that separate proteins according to their isoelectric points.
Biological samples, such...
The first dimension separation uses the isoelectric focusing or IEF technique performed on immobilized pH gradient (IPG) strips that separate proteins according to their isoelectric points.
Biological samples, such...
8.1K
Protein Folding
130.0K
Overview
130.0K
SDS-PAGE
35.4K
Gel electrophoresis is a method that separates biological macromolecules like nucleic acids or proteins by forcing them to pass through a gel matrix under an electric field.
A variation of gel electrophoresis, termed polyacrylamide gel electrophoresis (PAGE), is commonly used for separating proteins according to their molecular size by passing them through a polyacrylamide gel. Because of the varying charges associated with amino acid side chains, PAGE can be used to separate intact...
A variation of gel electrophoresis, termed polyacrylamide gel electrophoresis (PAGE), is commonly used for separating proteins according to their molecular size by passing them through a polyacrylamide gel. Because of the varying charges associated with amino acid side chains, PAGE can be used to separate intact...
35.4K
Phase Transitions: Melting and Freezing
15.6K
Heating a crystalline solid increases the average energy of its atoms, molecules, or ions, and the solid gets hotter. At some point, the added energy becomes large enough to partially overcome the forces holding the molecules or ions of the solid in their fixed positions, and the solid begins the process of transitioning to the liquid state or melting. At this point, the temperature of the solid stops rising, despite the continual input of heat, and it remains constant until all of the solid is...
15.6K

