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Literature summary for 3.4.14.11 extracted from

  • Giannoglou, M.; Alexandrakis, Z.; Stavros, P.; Katsaros, G.; Katapodis, P.; Nounesis, G.; Taoukis, P.
    Effect of high pressure on structural modifications and enzymatic activity of a purified X-prolyl dipeptidyl aminopeptidase from Streptococcus thermophilus (2018), Food Chem., 248, 304-311 .
    View publication on PubMed

Application

Application Comment Organism
food industry activation of the enzyme is observed after processing at 100-200 MPa and 20-30°C. More intense processing conditions lead to enzyme inactivation. Pressures up to 200 MPa result in a structurally molten globule-like state where PepX maintains its secondary structure but the tertiary structure is substantially affected and enzyme activity increased. Both secondary and tertiary structures are affected severely by higher pressures (450 MPa), which reduce enzyme activity Streptococcus thermophilus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
170000
-
PAGE Streptococcus thermophilus

Organism

Organism UniProt Comment Textmining
Streptococcus thermophilus
-
-
-
Streptococcus thermophilus ACA-DC 0022
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Streptococcus thermophilus

Subunits

Subunits Comment Organism
dimer 2 * 86000, SDS-PAGE Streptococcus thermophilus