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dc.contributor.author Ramnath, L
dc.contributor.author Sithole, Bishop B
dc.contributor.author Govinden, R
dc.date.accessioned 2018-01-04T10:44:14Z
dc.date.available 2018-01-04T10:44:14Z
dc.date.issued 2017-09
dc.identifier.citation Ramnath, L., Sithole, B.B. and Govinden, R. 2017. Identification of lipolytic enzymes isolated from bacteria indigenous to Eucalyptus wood species for application in the pulping industry. Biotechnology Reports, vol. 15: 114-124 en_US
dc.identifier.issn 2215-017X
dc.identifier.uri http://dx.doi.org/10.1016/j.btre.2017.07.004
dc.identifier.uri http://www.sciencedirect.com/science/article/pii/S2215017X17301108?via%3Dihub
dc.identifier.uri https://www.sciencedirect.com/science/article/pii/S2215017X17301108
dc.identifier.uri http://hdl.handle.net/10204/9911
dc.description This is an open access article, distributed under a Creative Commons license. en_US
dc.description.abstract This study highlights the importance of determining substrate specificity at variable experimental conditions. Lipases and esterases were isolated from microorganisms cultivated from Eucalyptus wood species and then concentrated (cellulases removed) and characterized. Phenol red agar plates supplemented with 1% olive oil or tributyrin was ascertained to be the most favourable method of screening for lipolytic activity. Lipolytic activity of the various enzymes were highest at 45–61 U/ml at the optimum temperature and pH of between at 30–35 °C and pH 4–5, respectively. Change in pH influenced the substrate specificity of the enzymes tested. The majority of enzymes tested displayed a propensity for longer aliphatic acyl chains such as dodecanoate (C12), myristate (C14), palmitate (C16) and stearate (C18) indicating that they could be characterised as potential lipases. Prospective esterases were also detected with specificity towards acetate (C2), butyrate (C4) and valerate (C5). Enzymes maintained up to 95% activity at the optimal pH and temperature for 2–3 h. It is essential to test substrates at various pH and temperature when determining optimum activity of lipolytic enzymes, a method rarely employed. The stability of the enzymes at acidic pH and moderate temperatures makes them excellent candidates for application in the treatment of pitch during acid bi-sulphite pulping, which would greatly benefit the pulp and paper industry. en_US
dc.language.iso en en_US
dc.publisher Elsevier en_US
dc.relation.ispartofseries Worklist;19963
dc.subject Lipase en_US
dc.subject Esterase en_US
dc.subject Substrate specificity en_US
dc.subject Pitch en_US
dc.subject Pulp en_US
dc.subject Paper en_US
dc.title Identification of lipolytic enzymes isolated from bacteria indigenous to Eucalyptus wood species for application in the pulping industry en_US
dc.type Article en_US


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