Ramnath, LSithole, Bishop BGovinden, R2018-01-042018-01-042017-09Ramnath, 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: 114-1242215-017Xhttp://dx.doi.org/10.1016/j.btre.2017.07.004http://www.sciencedirect.com/science/article/pii/S2215017X17301108?via%3Dihubhttps://www.sciencedirect.com/science/article/pii/S2215017X17301108http://hdl.handle.net/10204/9911This is an open access article, distributed under a Creative Commons license.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.enLipaseEsteraseSubstrate specificityPitchPulpPaperIdentification of lipolytic enzymes isolated from bacteria indigenous to Eucalyptus wood species for application in the pulping industryArticleRamnath, L., Sithole, B. B., & Govinden, R. (2017). Identification of lipolytic enzymes isolated from bacteria indigenous to Eucalyptus wood species for application in the pulping industry. http://hdl.handle.net/10204/9911Ramnath, L, Bishop B Sithole, and R Govinden "Identification of lipolytic enzymes isolated from bacteria indigenous to Eucalyptus wood species for application in the pulping industry." (2017) http://hdl.handle.net/10204/9911Ramnath L, Sithole BB, Govinden R. Identification of lipolytic enzymes isolated from bacteria indigenous to Eucalyptus wood species for application in the pulping industry. 2017; http://hdl.handle.net/10204/9911.TY - Article AU - Ramnath, L AU - Sithole, Bishop B AU - Govinden, R AB - 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. DA - 2017-09 DB - ResearchSpace DO - 10.1016/j.btre.2017.07.004 DP - CSIR KW - Lipase KW - Esterase KW - Substrate specificity KW - Pitch KW - Pulp KW - Paper LK - https://researchspace.csir.co.za PY - 2017 SM - 2215-017X T1 - Identification of lipolytic enzymes isolated from bacteria indigenous to Eucalyptus wood species for application in the pulping industry TI - Identification of lipolytic enzymes isolated from bacteria indigenous to Eucalyptus wood species for application in the pulping industry UR - http://hdl.handle.net/10204/9911 ER -