Production of phospholipase A2 from recombinant yarrowia lipolytica biopharmaceutical application

Phospholipase A2 (PLA2) is an enzyme that catalyzes the hydrolyisis of glycerophospholipids at the sn-2 position to yield the corresponding lysophospholpids and the free fatty acids. It catalytic properties which act as powerful emulsifier make it a widely used enzyme in various industrial applicati...

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Main Author:	Mokhtar, Nur'Ainun
Format:	Thesis
Language:	English
Published:	2013
Subjects:	Biopharmaceutics - instrumentation
Online Access:	http://psasir.upm.edu.my/id/eprint/38650/1/FPSK%28m%29%202013%2031%20IR.pdf
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spelling	my-upm-ir.386502016-02-26T09:12:10Z Production of phospholipase A2 from recombinant yarrowia lipolytica biopharmaceutical application 2013-10 Mokhtar, Nur'Ainun Phospholipase A2 (PLA2) is an enzyme that catalyzes the hydrolyisis of glycerophospholipids at the sn-2 position to yield the corresponding lysophospholpids and the free fatty acids. It catalytic properties which act as powerful emulsifier make it a widely used enzyme in various industrial application including laboratories, cosmeticeuticals, food industry as well as in pharmaceutical. However, in most industries, the PLA2 used are mainly isolated from mammalian pancreas (bovine and porcine). On the contrary, it had come to an issue regarding the origin of this animal based product which are rejected due to religious concern and the risk of viral infections to the consumers. To prevail the issue, an alternative PLA2 to replace the commercially available PLA2 has been initiated. Optimization of production parameters such as temperature, initial pH, inoculums size, inducer concentration and agitation speed are investigated using Two-Level Factorial Design and Central Composite Design by Design-Expert®. From this study, the optimal conditions PLA2 production are 6% (v/v) inoculums size; agitation speed, 225 rpm; pH 5.8; temperature of 34.5oC; inducer concentration, 0.03% (v/v) in basal salt medium. A verification run and scale up of PLA2 production yield 26.22 mg/L and 19.07 mg/L respectively compared to 27.15 mg/L predicted by the model. Purification of this enzyme through freeze drying and ultrafiltration and have shown a satisfactory purification factor of 1.15 and 1.35, respectively. The enzymatic properties (optimum activity at 37oC, pH 8.0) of the recombinant produced PLA2 from Y. lipolytica in this study shows similar properties to that of commercially available PLA2 in market which indicate that this recombinant PLA2 is a good and remarkable alternative of PLA2 sources for biopharmaceutical usage especially for HALAL applications. Biopharmaceutics - instrumentation Technology, Pharmaceutical - instrumentation 2013-10 Thesis http://psasir.upm.edu.my/id/eprint/38650/ http://psasir.upm.edu.my/id/eprint/38650/1/FPSK%28m%29%202013%2031%20IR.pdf application/pdf en public masters Universiti Putra Malaysia Biopharmaceutics - instrumentation Technology, Pharmaceutical - instrumentation
institution	Universiti Putra Malaysia
collection	PSAS Institutional Repository
language	English
topic	Biopharmaceutics - instrumentation Biopharmaceutics - instrumentation
spellingShingle	Biopharmaceutics - instrumentation Biopharmaceutics - instrumentation Mokhtar, Nur'Ainun Production of phospholipase A2 from recombinant yarrowia lipolytica biopharmaceutical application
description	Phospholipase A2 (PLA2) is an enzyme that catalyzes the hydrolyisis of glycerophospholipids at the sn-2 position to yield the corresponding lysophospholpids and the free fatty acids. It catalytic properties which act as powerful emulsifier make it a widely used enzyme in various industrial application including laboratories, cosmeticeuticals, food industry as well as in pharmaceutical. However, in most industries, the PLA2 used are mainly isolated from mammalian pancreas (bovine and porcine). On the contrary, it had come to an issue regarding the origin of this animal based product which are rejected due to religious concern and the risk of viral infections to the consumers. To prevail the issue, an alternative PLA2 to replace the commercially available PLA2 has been initiated. Optimization of production parameters such as temperature, initial pH, inoculums size, inducer concentration and agitation speed are investigated using Two-Level Factorial Design and Central Composite Design by Design-Expert®. From this study, the optimal conditions PLA2 production are 6% (v/v) inoculums size; agitation speed, 225 rpm; pH 5.8; temperature of 34.5oC; inducer concentration, 0.03% (v/v) in basal salt medium. A verification run and scale up of PLA2 production yield 26.22 mg/L and 19.07 mg/L respectively compared to 27.15 mg/L predicted by the model. Purification of this enzyme through freeze drying and ultrafiltration and have shown a satisfactory purification factor of 1.15 and 1.35, respectively. The enzymatic properties (optimum activity at 37oC, pH 8.0) of the recombinant produced PLA2 from Y. lipolytica in this study shows similar properties to that of commercially available PLA2 in market which indicate that this recombinant PLA2 is a good and remarkable alternative of PLA2 sources for biopharmaceutical usage especially for HALAL applications.
format	Thesis
qualification_level	Master's degree
author	Mokhtar, Nur'Ainun
author_facet	Mokhtar, Nur'Ainun
author_sort	Mokhtar, Nur'Ainun
title	Production of phospholipase A2 from recombinant yarrowia lipolytica biopharmaceutical application
title_short	Production of phospholipase A2 from recombinant yarrowia lipolytica biopharmaceutical application
title_full	Production of phospholipase A2 from recombinant yarrowia lipolytica biopharmaceutical application
title_fullStr	Production of phospholipase A2 from recombinant yarrowia lipolytica biopharmaceutical application
title_full_unstemmed	Production of phospholipase A2 from recombinant yarrowia lipolytica biopharmaceutical application
title_sort	production of phospholipase a2 from recombinant yarrowia lipolytica biopharmaceutical application
granting_institution	Universiti Putra Malaysia
publishDate	2013
url	http://psasir.upm.edu.my/id/eprint/38650/1/FPSK%28m%29%202013%2031%20IR.pdf
_version_	1747811743731548160

Production of phospholipase A2 from recombinant yarrowia lipolytica biopharmaceutical application

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