RT Journal Article
T1 Identifcation of novel extracellular putative chitinase and hydrolase from Geomyces sp. B10I with the biodegradation activity towards polyesters
A1 Urbanek, Aneta K.
A1 Arroyo Sánchez, Miguel
A1 De La Mata Riesco, Mª Isabel
A1 Mirończuk, Aleksandra M.
AB Cold-adapted flamentous 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 identifed 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 purifcation 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.
PB SpringerOpen
SN Electronic: 2191-0855
YR 2022
FD 2022-02-05
LK https://hdl.handle.net/20.500.14352/71824
UL https://hdl.handle.net/20.500.14352/71824
LA eng
NO Polish National Agency for Academic Exchange
NO National Science Centre (Poland)
DS Docta Complutense
RD 27 abr 2024