Cold-adapted serine protease from Antarctic yeast Leucosporidium antarcticum strain PI12

Cold-adapted serine protease from Antarctic yeast Leucosporidium antarcticum strain PI12

Leucosporidium antarcticum strain PI12 was isolated from Casey Station, Antarctica. It was shown to be protease-producer. Full-length cDNA of PI12 protease gene was amplified by rapid amplification of cDNA ends (RACE) strategy with an open reading frame (ORF) of 2892 bp that coded for 963 amino acid...

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Main Authors: Alias, Norsyuhada, Raja Abd. Rahman, Raja Noor Zaliha
Format: Conference or Workshop Item
Language:English
Published: 2014
Subjects:
QR Microbiology
Online Access:http://irep.iium.edu.my/53236/
http://irep.iium.edu.my/53236/1/3rd-BWC-Abstract-Book_53236_11216.pdf
id iium-53236
recordtype eprints
spelling iium-532362016-12-01T02:10:49Z http://irep.iium.edu.my/53236/ Cold-adapted serine protease from Antarctic yeast Leucosporidium antarcticum strain PI12 Alias, Norsyuhada Raja Abd. Rahman, Raja Noor Zaliha QR Microbiology Leucosporidium antarcticum strain PI12 was isolated from Casey Station, Antarctica. It was shown to be protease-producer. Full-length cDNA of PI12 protease gene was amplified by rapid amplification of cDNA ends (RACE) strategy with an open reading frame (ORF) of 2892 bp that coded for 963 amino acids. Homology search by BLAST web server has showed the PI12 protease sequence shared a significant homology to the subtilisin protease family from fungus but no similarity with other psychrophilic protease. The protease sequence was deposited into the GenBank Database with the accession no. CAQ76821. The gene encoding mature PI12 protease was cloned into Pichia pastoris expression vector, pPIC9, and positioned under the induction of methanol-alcohol oxidase (AOX) promoter. The recombinant PI12 protease was efficiently secreted into the culture medium driven by the Saccharomyces cerevisiae α-factor signal sequence. The highest protease production was obtained from P. pastoris GS115 host (GpPro2) with 20.3 U/mL activity at 15ºC after 3 days of induction time. The expressed protein was detected by SDS-PAGE and activity staining with a molecular weight of 99.3 kDa. 2014-02-10 Conference or Workshop Item PeerReviewed application/pdf en http://irep.iium.edu.my/53236/1/3rd-BWC-Abstract-Book_53236_11216.pdf Alias, Norsyuhada and Raja Abd. Rahman, Raja Noor Zaliha (2014) Cold-adapted serine protease from Antarctic yeast Leucosporidium antarcticum strain PI12. In: 3rd Biotechnology World Congress, 10-12 February 2014, Dubai, UAE. (Unpublished)
repository_type Digital Repository
institution_category Local University
institution International Islamic University Malaysia
building IIUM Repository
collection Online Access
language English
topic QR Microbiology
spellingShingle QR Microbiology
Alias, Norsyuhada
Raja Abd. Rahman, Raja Noor Zaliha
Cold-adapted serine protease from Antarctic yeast Leucosporidium antarcticum strain PI12
description Leucosporidium antarcticum strain PI12 was isolated from Casey Station, Antarctica. It was shown to be protease-producer. Full-length cDNA of PI12 protease gene was amplified by rapid amplification of cDNA ends (RACE) strategy with an open reading frame (ORF) of 2892 bp that coded for 963 amino acids. Homology search by BLAST web server has showed the PI12 protease sequence shared a significant homology to the subtilisin protease family from fungus but no similarity with other psychrophilic protease. The protease sequence was deposited into the GenBank Database with the accession no. CAQ76821. The gene encoding mature PI12 protease was cloned into Pichia pastoris expression vector, pPIC9, and positioned under the induction of methanol-alcohol oxidase (AOX) promoter. The recombinant PI12 protease was efficiently secreted into the culture medium driven by the Saccharomyces cerevisiae α-factor signal sequence. The highest protease production was obtained from P. pastoris GS115 host (GpPro2) with 20.3 U/mL activity at 15ºC after 3 days of induction time. The expressed protein was detected by SDS-PAGE and activity staining with a molecular weight of 99.3 kDa.
format Conference or Workshop Item
author Alias, Norsyuhada
Raja Abd. Rahman, Raja Noor Zaliha
author_facet Alias, Norsyuhada
Raja Abd. Rahman, Raja Noor Zaliha
author_sort Alias, Norsyuhada
title Cold-adapted serine protease from Antarctic yeast Leucosporidium antarcticum strain PI12
title_short Cold-adapted serine protease from Antarctic yeast Leucosporidium antarcticum strain PI12
title_full Cold-adapted serine protease from Antarctic yeast Leucosporidium antarcticum strain PI12
title_fullStr Cold-adapted serine protease from Antarctic yeast Leucosporidium antarcticum strain PI12
title_full_unstemmed Cold-adapted serine protease from Antarctic yeast Leucosporidium antarcticum strain PI12
title_sort cold-adapted serine protease from antarctic yeast leucosporidium antarcticum strain pi12
publishDate 2014
url http://irep.iium.edu.my/53236/
http://irep.iium.edu.my/53236/1/3rd-BWC-Abstract-Book_53236_11216.pdf
first_indexed 2018-09-07T07:18:28Z
last_indexed 2018-09-07T07:18:28Z
_version_ 1610932246093496320

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