Related Experiment Video

Updated: Feb 16, 2026

Author Spotlight: Innovative Ice Cream Melting Behavior Analysis Through a Computer Vision System
08:02

Author Spotlight: Innovative Ice Cream Melting Behavior Analysis Through a Computer Vision System

Published on: October 4, 2024

3.1K

Ice cream structure modification by ice-binding proteins

Aleksei Kaleda1, Robert Tsanev1, Tiina Klesment1

  • 1Department of Chemistry and Biotechnology, School of Science, Tallinn University of Technology, Ehitajate tee 5, 19086 Tallinn, Estonia; Center of Food and Fermentation Technologies, Akadeemia tee 15A, 12618 Tallinn, Estonia.

Food Chemistry
|January 3, 2018
PubMed

Keywords:
Ice cream microstructureIce recrystallization inhibitionIce-binding protein (antifreeze protein)

More Related Videos

Identification of Plant Ice-binding Proteins Through Assessment of Ice-recrystallization Inhibition and Isolation Using Ice-affinity Purification09:43

Identification of Plant Ice-binding Proteins Through Assessment of Ice-recrystallization Inhibition and Isolation Using Ice-affinity Purification

Published on: May 5, 2017

9.2K
Determining the Ice-binding Planes of Antifreeze Proteins by Fluorescence-based Ice Plane Affinity08:46

Determining the Ice-binding Planes of Antifreeze Proteins by Fluorescence-based Ice Plane Affinity

Published on: January 15, 2014

9.6K

Related Concept Videos

Protein and Protein Structure02:15

Protein and Protein Structure

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...
89.4K
Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
Writers
The writer...
9.5K
Histone Modification02:32

Histone Modification

The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
16.3K
Structural Protein Function01:56

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to...
30.1K
Structural Protein Function01:56

Structural Protein Function

3.3K
Protein Modifications in the RER01:26

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
7.2K