Related Experiment Video

Updated: Mar 5, 2026

Author Spotlight: Improving Beef Cattle Nutrition and Production with a Focus on Feed Efficiency and Meat Quality Traits Through Advanced Biochemical and Molecular Assays
07:46

Author Spotlight: Improving Beef Cattle Nutrition and Production with a Focus on Feed Efficiency and Meat Quality Traits Through Advanced Biochemical and Molecular Assays

Published on: July 12, 2024

1.1K

The effect of the packaging system and storage time on myofibrillar protein degradation and oxidation process in

Małgorzata Moczkowska1, Andrzej Półtorak1, Magdalena Montowska2

  • 1Department of Technique and Food Development, Faculty of Human Nutrition and Consumer Sciences, Warsaw University of Life Sciences-SGGW, 02-776 Warsaw, Poland.

Meat Science
|March 27, 2017
PubMed

Keywords:
BeefOxidationPolymerizationProtein degradationTenderness

More Related Videos

Introducing an Angle Adjustable Cutting Box for Analyzing Slice Shear Force in Meat09:30

Introducing an Angle Adjustable Cutting Box for Analyzing Slice Shear Force in Meat

Published on: April 26, 2013

13.4K
Preparation of High-Quality Fermented Fish Product05:17

Preparation of High-Quality Fermented Fish Product

Published on: August 23, 2019

11.1K

Related Concept Videos

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...
637
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...
10.2K
Protein Digestion01:02

Protein Digestion

Protein digestion begins in the stomach, where the highly acidic environment can easily disrupt protein structure by exposing the peptide bonds of polypeptide chains. After polypeptide chains are broken into individual amino acids by a series of digestive enzymes, the amino acids are transported to the liver via the bloodstream to produce energy.
112.4K
Drug Product Stability01:16

Drug Product Stability

The long-term stability of drug products is critical to ensuring their quality, safety, and effectiveness over time. Stability directly influences a product's ability to maintain its intended characteristics, ensuring it performs as expected during its intended shelf life. Key attributes such as drug potency, impurities, dissolution, and other physicochemical measures of performance are tested to assess stability. These parameters indicate how well the product retains its quality over time and...
320
The Effect of Aging on Tissues01:19

The Effect of Aging on Tissues

Several body functions deteriorate with age. The external signs of aging are easily identifiable. For example, the skin becomes dry, less elastic, and thins out, forming wrinkles. The skin of the face begins to appear looser due to a decrease in the levels of elastic and collagen fibers in the connective tissue. Additionally, melanin production in the hair follicle decreases with age, resulting in gray hair. Moreover, the senses of sight and hearing decline, so glasses and hearing aids may...
4.0K
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...
7.3K