Additional file 1 of Identification of novel extracellular putative chitinase and hydrolase from Geomyces sp. B10I with the biodegradation activity towards polyesters
Creators: name: Urbanek, Aneta K.
name: Arroyo, Miguel
name: de la Mata, Isabel
name: Mirończuk, Aleksandra M.
Publisher: name: figshare
Year: 2022
Subjects: subject: Biophysics
subject: Biochemistry
subject: Microbiology
subject: FOS: Biological sciences
subject: Genetics
subject: Biotechnology
subject: Evolutionary Biology
subject: 39999 Chemical Sciences not elsewhere classified
subject: FOS: Chemical sciences
subject: Ecology
subject: Immunology
subject: FOS: Clinical medicine
subject: Plant Biology

description: Additional file 1: Figure S1. Geomyces sp. B10I and its biodegradation activity. A Microscopic morphology at total magnification 25.2 ×: growing hyphae; B spore release; C biodegradation activity towards 0.1% PBSA in a plate assay; D Biodegradation activity of free-cell supernatant collected at different growth stages: red square represents free-cell supernatant obtained during hyphae growth, whereas black square from spore release stage; numbers represent the number of the flask. Figure S2. Chromatographic profiles of purification: A pH 8.0; B pH 9.0; C pH 9.0. The peaks with biodegradable activity are marked as a red square in the chromatograms. The flow rate was maintained at 1 ml/min for each purification step. Figure S3. Peptide fingerprinting MS result for bands signed as PBSA1 (A) and PBSA2 (B). Molecular weight of the analysed proteins was 77248 Da and 46482 Da, respectively. The search within BLAST revealed that both proteins had shown essentially identical properties (100% identity) to proteins characterized as a hypothetical proteins from Pseudogymnoascus sp. VKM F-4515 with accession numbers KFY49210.1 and KFY57494.1, respectively. Figure S4. Amino acid sequences of (A) hydrGB10I and (B) chitGB10I. Figure S5. Multiple sequence alignment of hydrGB10I with other enzymes exhibiting biodegradable activity. Conserved columns in each group are coloured in blue. Alignment conservation, quality, consensus and occupancy are displayed below the alignments. EAL84505.1—PHB depolymerase (Aspergillus fumigatus Af293); AAB05922.1—cutinase (Fusarium petroliphilum); BAN42607.1—cutinase-like enzyme (Cryptococcus sp. BPD1A); B2NHN2—PHB depolymerase (Talaromyces funiculosus); QED41487.1—serine hydrolase (Pestalotiopsis microspore); PVH79176.1—glycoside hydrolase family 81 protein (Cadophora sp. DSE1049); KAF8866935.1—family 81 glycosyl hydrolase (Acephala macrosclerotiorum); A0A370T8Q3—PHB depolymerase (Venustampulla echinocandica); P52956—Cutinase 1 (Aspergillus oryzae RIB40). Figure S6. Multiple sequence alignment of chitGB10I with other enzymes exhibiting biodegradable activity. Conserved columns in each group are coloured in blue. Alignment conservation, quality, consensus and occupancy are displayed below the alignments. BAA88834.1—Chi25 (Streptomyces thermoviolaceus); ABV57861.1—chitinase CrCH1 (Clonostachys rosea); AMP42675.1—chitinase (Rhizomucor miehei); X0BTD8—cutinase (Fusarium oxysporum f. sp. raphani 54005); B2NHN2—PHB depolymerase (Talaromyces funiculosus); BAM28634.1—cutinase C (Aspergillus oryzae); BAN42607.1—cutinase-like enzyme (Cryptococcus sp. BPD1A), EAL84505.1—PHB depolymerase (Aspergillus fumigatus Af293); G9BY57.1—LC-cutinase. Figure S7. The scheme of purification procedure.