Geotrichum candidum aldehyde dehydrogenase-inorganic nanocrystal with enhanced activity

• Published in: Enzyme and microbial technology Vol. 150; p. 109866
• Main Authors: T.sriwong, Kotchakorn, Ogura, Kazuki, Hawari, Muhammad Arisyi, Matsuda, Tomoko
• Format: Journal Article
• Language: English
• Published: Elsevier Inc 01.10.2021
• Subjects: Aldehyde dehydrogenase; aldehydes; Biotransformation; Enzyme immobilization; Geotrichum candidum; Green chemistry; nanocrystals; Organic-inorganic nanocrystal; Oxidation; thermal stability; Oxidation; Enzyme immobilization; Green chemistry; Organic-inorganic nanocrystal; Aldehyde dehydrogenase; Biotransformation
• ISSN: 0141-0229; 1879-0909; 1879-0909
• DOI: 10.1016/j.enzmictec.2021.109866

•Geotrichum candidum aldehyde dehydrogenase (GcALDH) was firstly immobilized by organic-inorganic nanocrystal formation.•The GcALDH nanocrystal exhibited enhanced activity of benzaldehyde oxidation to be 261 % comparing to the free GcALDH.•The GcALDH nanocrystal retained broad substrate specificity property.•The thermostability and recyclability of the GcALDH were improved by immobilization.•The robustness and versatility of the GcALDH nanocrystal made it promising for further applications. A novel Geotrichum candidum aldehyde dehydrogenase (GcALDH) effectively oxidized aldehydes to carboxylic acids under mild conditions. Nonetheless, the free form of GcALDH still had a limitation in stability and recyclability. Herein, to overcome these limitations, this study achieved the immobilization of the GcALDH by the organic-inorganic nanocrystal formation. The GcALDH nanocrystal exhibited 261 ± 40 % of activity comparing to the free enzyme. It also exhibited improved thermostability and recyclability as well as remained excellent substrate promiscuity, which suggested its potential use in green industries. To the best of our knowledge, this is the first time to report the ALDH-inorganic nanocrystal formation with superior properties.