相关实验视频

Updated: Jan 16, 2026

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast
11:04

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast

Published on: June 23, 2018

7.6K

大豆蛋白粉层机制隔离储存期间的功能恶化:聚合和氧化应激的相互作用

Hui Zhang1, Tong Zhang1, Xiong Zhang1

  • 1Beijing Key Laboratory of Plant Protein and Cereal Processing, College of Food Science and Science and Nutritional Engineering, China Agricultural University, Beijing 100083, PR China.

Food chemistry
|September 27, 2025
PubMed
概括

储存导致大豆蛋白分离物 (SPI) 由于聚合和氧化而失去功能. 这些粉末水平的变化会损害水合和分散,导致溶解性降低和乳化. 提高SPI稳定性需要解决这些与存储相关的问题.

关键词:
功能性衰退 功能性衰退粉末的特性 粉末的特性蛋白质氧化过程中的蛋白质氧化.这是一种大豆蛋白分离物.储存稳定性 储存的稳定性

更多相关视频

Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders11:14

Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders

Published on: April 14, 2015

16.8K
Author Spotlight: In Silico Creation and Impact of Carbonylated Amino Acids on Protein Structure and Function05:57

Author Spotlight: In Silico Creation and Impact of Carbonylated Amino Acids on Protein Structure and Function

Published on: April 26, 2024

833

相关概念视频

Protein Denaturation01:28

Protein Denaturation

The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
8.4K
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...
6.9K
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...
86.9K
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
11.1K
Protein Folding01:22

Protein Folding

Overview
126.3K
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
468