Gumel, A.M. and Annuar, M.S.M. and Heidelberg, T. (2013) Single-step lipase-catalyzed functionalization of medium-chain-length polyhydroxyalkanoates. Journal of Chemical Technology and Biotechnology. pp. 1328-1335. DOI https://doi.org/10.1002/jctb.3980.
PDF
00013161_103461.pdf Restricted to Registered users only Download (340kB) | Request a copy |
Abstract
BACKGROUND: Functionalization of aliphatic biopolymers such as bacterial polyhydroxyalkanoates (PHA) using biologically active hydrophilic moieties like sugars helps to improve the hydrophilicity and biodegradability of the biomaterial. RESULTS:Theeffects of reaction variables reaction time, temperature,enzyme concentration and substrate ratio on reaction rate and yield in the synthesis of poly(1’-O-3-hydroxyacyl-sucrose) using Candida antarctica lipase B (EC 3.1.1.3)were studied. Using H2O2 as micro-initiator, enzyme-mediated synthesis yielded reaction rate, vapp of 0.076 x 10−5 mol L−1 s−1. The biodegradability of the functionalized polymer was observed to increase by 1.5 fold compared with the non-functionalized material apart from showing better compostability. Increasing the reaction temperature (>50◦C), enzyme concentration (>15 g L−1) and reactant ratio (w/w) of sucrose:PHA (>2) did not increase further the rate or yield. The sucrose-functionalized mcl-PHAwas characterized with respect to the non-functionalized material. CONCLUSIONS: Novozym 435 can be used effectively to synthesize poly(1’-O-3-hydroxyacyl sucrose) in micro-aqueous medium bypassing the need for chemo-synthetic steps. The synthesized biomaterials have potential applications in biomedical and industrial niches
Item Type: | Article |
---|---|
Funders: | UNSPECIFIED |
Additional Information: | Correspondence to: SuffianMAnnuar, Institute of Biological Sciences, Faculty of Science, University ofMalaya, 50603 Kuala Lumpur, Malaysia. E-mail: suffian_annuar@um.edu.my |
Uncontrolled Keywords: | Biopolymer; Candida antarctica; Lipase; Polyhydroxyalkanoates; Sugar-ester; Sucrose. |
Subjects: | Q Science > Q Science (General) Q Science > QD Chemistry |
Divisions: | Faculty of Science > Institute of Biological Sciences |
Depositing User: | Ms. Norhamizah Tamizi |
Date Deposited: | 22 Apr 2014 01:51 |
Last Modified: | 22 Apr 2014 01:51 |
URI: | http://eprints.um.edu.my/id/eprint/9632 |
Actions (login required)
View Item |