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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| Format: | Thesis |
| Language: | English |
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2012
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| Online Access: | http://eprints.usm.my/44792/1/CHUAH%20JO-ANN.pdf |
| _version_ | 1825835033971130368 |
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| author | Chuah, Jo-Ann |
| author_facet | Chuah, Jo-Ann |
| author_sort | Chuah, Jo-Ann |
| collection | USM |
| 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). |
| first_indexed | 2024-03-06T15:31:39Z |
| format | Thesis |
| id | usm.eprints-44792 |
| institution | Universiti Sains Malaysia |
| language | English |
| last_indexed | 2024-03-06T15:31:39Z |
| publishDate | 2012 |
| record_format | dspace |
| spelling | usm.eprints-447922019-07-01T07:24:48Z http://eprints.usm.my/44792/ Characterization Of A Highly Active Polyhydroxyalkanoate Synthase 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 NonPeerReviewed application/pdf en http://eprints.usm.my/44792/1/CHUAH%20JO-ANN.pdf Chuah, Jo-Ann (2012) Characterization Of A Highly Active Polyhydroxyalkanoate Synthase. PhD thesis, Universiti Sains Malaysia. |
| spellingShingle | QH1 Natural history (General - Including nature conservation, geographical distribution) Chuah, Jo-Ann Characterization Of A Highly Active Polyhydroxyalkanoate Synthase |
| title | 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_short | Characterization Of A Highly Active Polyhydroxyalkanoate Synthase |
| title_sort | characterization of a highly active polyhydroxyalkanoate synthase |
| topic | QH1 Natural history (General - Including nature conservation, geographical distribution) |
| url | http://eprints.usm.my/44792/1/CHUAH%20JO-ANN.pdf |
| work_keys_str_mv | AT chuahjoann characterizationofahighlyactivepolyhydroxyalkanoatesynthase |