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OJVRTM

Online Journal of Veterinary Research©

(Including Medical and Laboratory Research)

Established 1994

ISSN 1328-925X

 

Volume  29 (7): 456-464, 2025.

Thermal Inactivation of free Inulinase from Kluyveromyces Marxianus

 

Abdul Sattar Jabbar Taha1, Т.А. Коvalеva2

 

1Aesthetic and Laser , College of Health Medical Techniques, Al Bayan University, Iraq. 2Dept. Biophysics & Biotechnology. Faculty of Biology and Soil Sciences, Voronezh State University, Russia. sattaraldelemi@gmail.com

ABSTRACT

Jabbar Taha AS, Коvalеva TA, Thermal Inactivation of free Inulinase from Kluyveromyces Marxianus, Onl J Vet Res., 29 (7): 456-464, 2025. We describe thermal inactivation of free inulinase enzyme from Kluyveromyces marxianus between 30-80C0  to improve enzyme stability and reduce cost. The mechanism of inactivation is likely due to the increase in heat capacity of denatured protein, induced by increased surface contact of hydrophobic side groups with solvent. By differential thermal analysis, we found two distinct thermal peaks at 54 and 65°C, suggesting multi-stage conformational transitions ranging from simple local rearrangement to complete detection of random total disorder. To break down aniline, the enzyme takes on a suitable shape and configuration in terms of energy and space at optimum temperatures to enhance catalysis. Understanding these changes and transformations in the enzyme's denaturation may improve performance.

Key words: Inulinase, conformational transitions, Differential thermal analysis, denaturation,

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