Influence of freezing down to 77.15 K on structure and antioxidant power of some proteins

• Published in: Физика низких температур
• Date: 2017
• Main Authors: Rozanova, S.L., Narozhnyi, S.V., Nardid, O.A.
• Format: Article
• Language: English
• Published: Фізико-технічний інститут низьких температур ім. Б.І. Вєркіна НАН України 2017
• Subjects: Низкоразмерные и неупорядоченные системы
• Online Access: https://nasplib.isofts.kiev.ua/handle/123456789/129506
• Journal Title: Digital Library of Periodicals of National Academy of Sciences of Ukraine
• Cite this: Influence of freezing down to 77.15 K on structure and antioxidant power of some proteins / S.L. Rozanova, S.V. Narozhnyi, O.A. Nardid // Физика низких температур. — 2017. — Т. 43, № 6. — С. 898-901. — Бібліогр.: 18 назв. — англ.

The purpose of the present work was to investigate influence of different freeze-thawing protocols on structure and antioxidant properties of isolated proteins. In our experiments we have studied human serum albumin, human hemoglobin and cytochrome C derived from equine heart frozen down to 77.15 K with 1–2 deg/min and 300 deg/min rate with following thawing on a water bath at 293.15 K. Native proteins were assumed as a control. Influence of freeze-thawing protocols on protein structure was investigated using spectrophotometric and fluorescent assays. Antioxidant activities of isolated proteins were estimated by their ability to reduce ABTS ⁺ radical. It has been established that unfolding derived from freeze-thawing exposure leads to protein antioxidant activity increasing while decreasing of such an activity may be connected with macromolecule aggregation. Character of freeze-thawing influence on antioxidant activity of proteins depends on molecule structure peculiarities and freezing protocols.