FTIR Study of Aqueous Solutions of α -Amylase- Evidence of C-O-H Bond Formation at High Temperatures

Vibhor Chaswal and Arshad Khan
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Arshad Khan: Department of Chemistry, Eberly College of Science, Pennsylvania State University, USA

Biomedical Journal of Scientific & Technical Research, 2024, vol. 55, issue 3, 47002-47007

Abstract: Some years ago, Lecker & Khan (Biotechnology Progress, 1996, 1998) examined the effect of heat on α-amylase by UV-VIS spectroscopy and put forward a two-step inactivation mechanism for this enzyme. In the first step Ca2+ ion dissociates reversibly from the active enzyme followed by irreversible inactivation of the apoenzyme (enzyme without the calcium attached). The purpose of this FTIR (Fourier-transform infrared spectroscopy) study is to examine what happens at the molecular level when the protein is heated from 20 to 90 °C.

Keywords: Journals on Medical Drug and Therapeutics; Journals on Emergency Medicine; Physical Medicine and Rehabilitation; Journals on Infectious Diseases Addiction Science and Clinical Pathology; Open Access Clinical and Medical Journal; Journals on Biomedical Science; List of Open Access Medical Journal; Journals on Biomedical Engineering; Open Access Medical Journal; Biomedical Science Articles; Journal of Scientific and Technical Research (search for similar items in EconPapers)
Date: 2024
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Persistent link: https://EconPapers.repec.org/RePEc:abf:journl:v:55:y:2024:i:3:p:47002-47007

DOI: 10.26717/BJSTR.2024.55.008705

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