Characterization Of A Highly Active Polyhydroxyalkanoate Synthase

Polyhydroxyalkanoate (PHA) synthase from a locally isolated Chromobacterium sp. USM2 (PhaCCs) exhibited superior polymerizing ability and broad in vivo substrate specificity with preferences for short chain length (SCL) [3-hydroxybutyrate (3HB) and 3-hydroxyvalerate (3HV)] and medium chain length (M...

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Main Author: Chuah, Jo-Ann
Format: Thesis
Language:English
Published: 2012
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Online Access:http://eprints.usm.my/44792/1/CHUAH%20JO-ANN.pdf
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spelling my-usm-ep.447922019-07-01T07:24:48Z Characterization Of A Highly Active Polyhydroxyalkanoate Synthase 2012-06 Chuah, Jo-Ann QH1 Natural history (General - Including nature conservation, geographical distribution) Polyhydroxyalkanoate (PHA) synthase from a locally isolated Chromobacterium sp. USM2 (PhaCCs) exhibited superior polymerizing ability and broad in vivo substrate specificity with preferences for short chain length (SCL) [3-hydroxybutyrate (3HB) and 3-hydroxyvalerate (3HV)] and medium chain length (MCL) [3-hydroxyhexanoate (3HHx)] monomers. For further characterization of the synthase, a Strep2-tagged PhaCCs for expression in and purification from Escherichia coli, was constructed in this study. In vitro enzymatic assay revealed an activity of 253 ± 13 U/mg for polymerization of 3-hydroxybutyryl-coenzyme A (3HB-CoA), which was approximately fivefold higher than that of model PHAproducing strain Cupriavidus necator (39 ± 5 U/mg). 2012-06 Thesis http://eprints.usm.my/44792/ http://eprints.usm.my/44792/1/CHUAH%20JO-ANN.pdf application/pdf en public phd doctoral Universiti Sains Malaysia Pusat Pengajian Sains Kajihayat
institution Universiti Sains Malaysia
collection USM Institutional Repository
language English
topic QH1 Natural history (General - Including nature conservation
geographical distribution)
spellingShingle QH1 Natural history (General - Including nature conservation
geographical distribution)
Chuah, Jo-Ann
Characterization Of A Highly Active Polyhydroxyalkanoate Synthase
description Polyhydroxyalkanoate (PHA) synthase from a locally isolated Chromobacterium sp. USM2 (PhaCCs) exhibited superior polymerizing ability and broad in vivo substrate specificity with preferences for short chain length (SCL) [3-hydroxybutyrate (3HB) and 3-hydroxyvalerate (3HV)] and medium chain length (MCL) [3-hydroxyhexanoate (3HHx)] monomers. For further characterization of the synthase, a Strep2-tagged PhaCCs for expression in and purification from Escherichia coli, was constructed in this study. In vitro enzymatic assay revealed an activity of 253 ± 13 U/mg for polymerization of 3-hydroxybutyryl-coenzyme A (3HB-CoA), which was approximately fivefold higher than that of model PHAproducing strain Cupriavidus necator (39 ± 5 U/mg).
format Thesis
qualification_name Doctor of Philosophy (PhD.)
qualification_level Doctorate
author Chuah, Jo-Ann
author_facet Chuah, Jo-Ann
author_sort Chuah, Jo-Ann
title Characterization Of A Highly Active Polyhydroxyalkanoate Synthase
title_short Characterization Of A Highly Active Polyhydroxyalkanoate Synthase
title_full Characterization Of A Highly Active Polyhydroxyalkanoate Synthase
title_fullStr Characterization Of A Highly Active Polyhydroxyalkanoate Synthase
title_full_unstemmed Characterization Of A Highly Active Polyhydroxyalkanoate Synthase
title_sort characterization of a highly active polyhydroxyalkanoate synthase
granting_institution Universiti Sains Malaysia
granting_department Pusat Pengajian Sains Kajihayat
publishDate 2012
url http://eprints.usm.my/44792/1/CHUAH%20JO-ANN.pdf
_version_ 1747821400021794816