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Prof. Dr. Nevin Gül Karagüler and her team secure dual funding from the Research University Support Program (ADEP) and TÜBİTAK’s Polar Research Program (KUTUP-1001)

by Zeynep Kalaycıoğlu | Tem 05, 2025
Prof. Dr. Nevin Gül Karagüler and her team secure dual funding from the Research University Support Program (ADEP) and TÜBİTAK’s Polar Research Program (KUTUP-1001) for Enzyme Discovery in Extreme Environments: From Antarctica’s Freezing Soils to Turkey’s Acidic, Geothermal, and Hypersaline Habitats

Prof. Dr. Nevin Gül Karagüler and her team secure dual funding from the Research University Support Program (ADEP) and TÜBİTAK’s Polar Research Program (KUTUP-1001) for Enzyme Discovery in Extreme Environments: From Antarctica’s Freezing Soils to Turkey’s Acidic, Geothermal, and Hypersaline Habitats


1. Prof. Dr. Nevin Gül Karagüler Leads ADEP-Funded Project on Bioremediation Potential of Novel CYP153 Enzymes from Türkiye’s Extreme Environments

Petroleum hydrocarbon pollution remains one of the most pressing global environmental issues, posing significant threats to both ecosystems and human health. To address this problem through sustainable and innovative methods, researchers from Istanbul Technical University (ITU) have launched a new research project supported by the Research University Support Program (ADEP). This initiative is coordinated by the Council of Higher Education (YÖK) as part of Türkiye’s mission-oriented research university strategy.

The project, led by Prof. Dr. Nevin Gül Karagüler from the Department of Molecular Biology and Genetics, is entitled “Bioremediation Potential of Novel CYP153 Enzymes Identified from Türkiye’s Extreme Environments Using Metagenomics.” The study focuses on ten novel CYP153 enzymes discovered through advanced metagenomic analysis of diverse extreme habitats across Türkiye, including acidic, geothermal, and hypersaline environments. These cytochrome P450 (CYP153) enzymes, known for their ability to catalyze alkane hydroxylation reactions, are being recombinantly produced, biochemically characterized, and tested for their efficiency in breaking down petroleum-based compounds. The enzymes are evaluated on both model n-alkanes and crude oil samples, offering insights into their real-world applicability in bioremediation efforts.

Experimental work is being carried out in close collaboration with experts from the Faculty of Chemical and Metallurgical Engineering (Department of Chemical Engineering) and the Marine Research and Technologies Research Group (DATAG) under the Climate and Life Sciences Vice Presidency of TÜBİTAK Marmara Research Center (MAM). This interdisciplinary approach enhances the project’s capacity to bridge molecular biology, chemical engineering, and marine sciences. Supported by the ADEP program, this project explores the bioremediation potential of ten novel CYP153 enzymes identified through metagenomic analysis of Türkiye’s extreme environments. The enzymes are recombinantly produced, characterized, and tested on both model n-alkanes and crude oil. The study aims to develop innovative, sustainable biotechnological solutions to petroleum pollution using microbial enzymes adapted to harsh conditions.

The outcomes of this research are expected to contribute significantly to Türkiye’s national capacity in environmental biotechnology, potentially leading to scientific publications, patent applications, and novel industrial enzyme platforms. Ultimately, the project seeks to lay the groundwork for eco-friendly alternatives to traditional chemical remediation technologies, using naturally adapted microbial solutions to combat oil pollution more effectively and sustainably.

2. TÜBİTAK Supports Prof. Nevin Gül Karagüler’s Research on Antarctic Enzymes for Sustainable Biotechnology



 

Metagenomic approaches and protein engineering play a crucial role in the discovery and development of novel enzymes, particularly for environmentally friendly applications in green biotechnology. In this context, two novel cytochrome P450 monooxygenases belonging to the CYP102 family were recently identified from Antarctic soil samples through field-based metagenomic analysis. These enzymes were characterized by the Metagenomics and Protein Engineering Group at Istanbul Technical University (ITU), under the leadership of Prof. Dr. Nevin Gül Karagüler.

The newly identified enzymes, named CYP102A177 and CYP102M18, are cold-adapted P450s, containing a heme prosthetic group and capable of catalyzing the hydroxylation of fatty acids. Hydroxy fatty acids serve as precursors for various polymers and, thus, are highly valuable for numerous industries, including pharmaceuticals, cosmetics, surfactants, and bioplastics. Due to their high catalytic efficiency at low temperatures, these cold-active enzymes stand out as attractive candidates for industrial applications requiring energy-efficient and sustainable processes, such as bioremediation, green synthesis, and drug manufacturing.

The research project entitled “Investigation of Biotechnological Potentials of Novel CYP102 Enzymes Identified by Metagenomic Approach from Antarctica” has been officially awarded funding by the TÜBİTAK KUTUP-1001 Program, recognizing its scientific merit and potential impact. Within the scope of this project, the recombinant production of CYP102A177 and CYP102M18 will be carried out, followed by enzyme purification via affinity chromatography. The characteristic Soret maxima values and enzymatic activity will be assessed through CO-binding spectral analysis. Furthermore, substrate-binding assays and LC-MS-based quantification of product conversion will be used to explore their biotechnological capabilities.

By elucidating the structure-function relationships and catalytic mechanisms of these cold-active CYP102 enzymes, the project aims to contribute significantly to green chemistry and environmentally sustainable biotechnological innovation. The work not only expands the existing enzyme toolbox for industrial biotechnology but also showcases the untapped biocatalytic potential hidden in extreme environments such as Antarctica.