role of protein denaturation Flashcards
- Gel Strength: The gelation properties of surimi are primarily influenced
influenced by the myofibrillar proteins, such as myosin and actin
. Denaturation can lead to the
loss of these proteins’ ability to form a strong gel matrix, resulting in a weaker, less elastic gel.
- Water-Holding Capacity: Properly functional myofibrillar proteins can
hold water within the gel matrix.
Denaturation disrupts this capacity, leading to a
lower water-holding capacity and resulting in a drier and less desirable texture in the final product.
- Opacity and Whiteness: Surimi’s desirable whiteness and opacity are affected
by the state of the proteins
Denatured proteins may result in a less white product
due to changes in their light-reflecting properties
- Protein Denaturation and Lipid Oxidation: Denatured proteins can expose
hydrophobic regions, which may interact with lipid
interact with lipids and
lead to increased lipid oxidation.
lipid oxidation
can result in off-flavors and odors, negatively affecting the sensory quality of surimi.
- Digestibility: While denaturation generally makes proteins more digestible by
exposing peptide bonds to digestive enzymes,
excessive denaturation can lead to
formation of aggregates that are less digestible.
aggregates
can reduce the overall nutritional value of the surimi.
- Microbial Stability: Denatured proteins can have altered binding properties
affecting the product’s ability to retain water and maintain its structure
altered binding properties
can influence the shelf life and microbial stability of surimi, potentially leading to spoilage.
- Freeze-Thaw Stability: Surimi products often undergo freezing and thawing. Denatured proteins can form
aggregates that reduce the freeze-thaw stability
