UPM Institutional Repository

Expression, characterisation and homology modelling of a novel hormone-sensitive lipase (HSL)-like esterase from Glaciozyma antarctica


Citation

Mohamad Tahir, Hiryahafira and Raja Abdul Rahman, Raja Noor Zaliha and Leow, Adam Thean Chor and Mohamad Ali, Mohd Shukuri (2020) Expression, characterisation and homology modelling of a novel hormone-sensitive lipase (HSL)-like esterase from Glaciozyma antarctica. Catalysts, 10 (1). art. no. 58. pp. 1-19. ISSN 2073-4344

Abstract

Microorganisms, especially those that survive in extremely cold places such as Antarctica, have gained research attention since they produce a unique feature of the protein, such as being able to withstand at extreme temperature, salinity, and pressure, that make them desired for biotechnological application. Here, we report the first hormone-sensitive lipase (HSL)-like esterase from a Glaciozyma species, a psychrophilic yeast designated as GlaEst12-like esterase. In this study, the putative lipolytic enzyme was cloned, expressed in E. coli, purified, and characterised for its biochemical properties. Protein sequences analysis showed that GlaEst12 shared about 30% sequence identity with chain A of the bacterial hormone-sensitive lipase of E40. It belongs to the H group since it has the conserved motifs of Histidine-Glycine-Glycine-Glycine (HGGG)and Glycine-Aspartate-Serine-Alanine-Glycine (GDSAG) at the amino acid sequences. The recombinant GlaEst12 was successfully purified via one-step Ni-Sepharose affinity chromatography. Interestingly, GlaEst12 showed unusual properties with other enzymes from psychrophilic origin since it showed an optimal temperature ranged between 50–60 °C and was stable at alkaline pH conditions. Unlike other HSL-like esterase, this esterase showed higher activity towards medium-chain ester substrates rather than shorter chain ester. The 3D structure of GlaEst12, predicted by homology modelling using Robetta software, showed a secondary structure composed of mainly α/β hydrolase fold, with the catalytic residues being found at Ser232, Glu341, and His371.


Download File

[img] Text
38187.pdf
Restricted to Repository staff only

Download (4MB)

Additional Metadata

Item Type: Article
Divisions: Faculty of Biotechnology and Biomolecular Sciences
DOI Number: https://doi.org/10.3390/catal10010058
Publisher: MDPI
Keywords: Psychrophilic yeast; Hormone-sensitive lipase; Glaciozyma antarctica; Antarctica; Homology modelling
Depositing User: Nabilah Mustapa
Date Deposited: 03 May 2020 23:05
Last Modified: 03 May 2020 23:05
Altmetrics: http://www.altmetric.com/details.php?domain=psasir.upm.edu.my&doi=10.3390/catal10010058
URI: http://psasir.upm.edu.my/id/eprint/38187
Statistic Details: View Download Statistic

Actions (login required)

View Item View Item