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Literature summary for 1.1.3.13 extracted from

  • Buchholz-Afari, M.; Halalipour, A.; Yang, D.; Reyes-De-Corcuera, J.
    Increased stability of alcohol oxidase under high hydrostatic pressure (2019), J. Food Eng., 246, 95-101 .
No PubMed abstract available
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Organism

Organism UniProt Comment Textmining
Komagataella phaffii
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Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
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 Komagataella phaffii
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Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
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 in a commercial preparation, one of AOX's isozymes is more resistant to thermal inactivation at atmospheric or high pressures. The resistant fraction is 4-34 times more stable than the labile fraction. High hydrostatic pressure stabilizes AOX against thermal inactivation. A 14fold stabilization is observed at 49.4°C for the labile fraction at 200 MPa relative to atmospheric pressure. The activation energy of inactivation at 40-160 MPa ranges from 95 to 184 kJ per mol for the resistant fraction and from 232 to 402 kJ per mol for the labile fraction Komagataella phaffii