Identification of novel extracellular putative chitinase and hydrolase from Geomyces sp. B10I with the biodegradation activity towards polyesters

AMB Express

Miguel Arroyo¹  Isabel de la Mata¹  Aleksandra M. Mirończuk²  Aneta K. Urbanek² 

[1] Department of Biochemistry and Molecular Biology, Faculty of Biology, Universidad Complutense de Madrid, C. de José Antonio Novais, 12, 28040, Madrid, Spain;Department of Biotechnology and Food Microbiology, Faculty of Biotechnology and Food Science, Wroclaw University of Environmental and Life Sciences, Chełmońskiego 37, 51‑630, Wrocław, Poland;

关键词: Geomyces;    Polyesters;    Chitinase;    Hydrolase;    Cold-adapted microorganisms;   

DOI  :  10.1186/s13568-022-01352-7

来源: Springer

【 摘 要 】

Cold-adapted filamentous fungal strain Geomyces sp. B10I has been reported to decompose polyesters such as poly(e-caprolactone) (PCL), poly(butylene succinate) (PBS) and poly(butylene succinate-co-butylene adipate) (PBSA). Here, we identified the enzymes of Geomyces sp. B10I, which appear to be responsible for its biodegradation activity. We compared their amino acid sequences with sequences of well-studied fungal enzymes. Partial purification of an extracellular mixture of the two enzymes, named hydrGB10I and chitGB10I, using ammonium sulfate precipitation and ionic exchange chromatography gave 14.16-fold purity. The amino acid sequence of the proteins obtained from the MALDI-TOF analysis determined the molecular mass of 77.2 kDa and 46.5 kDa, respectively. Conserved domain homology analysis revealed that both proteins belong to the class of hydrolases; hydrGB10I belongs to the glycosyl hydrolase 81 superfamily, while chitGB10I contains the domain of the glycosyl hydrolase 18 superfamily. Phylogenetic analysis suggests a distinct nature of the hydrGB10I and chitGB10I of Geomyces sp. B10I when compared with other fungal polyester-degrading enzymes described to date.

【 授权许可】

CC BY