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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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 |
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QH1 Natural history (General - Including nature conservation geographical distribution) |
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QH1 Natural history (General - Including nature conservation geographical distribution) Chuah, Jo-Ann Characterization Of A Highly Active Polyhydroxyalkanoate Synthase |
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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 |