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Development and Validation of a Kinetic Model for Enzymatic Hydrolysis Using Candida rugosa Lipase | OMICS International | Abstract
ISSN: 2155-9821

Journal of Bioprocessing & Biotechniques
Open Access

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Research Article

Development and Validation of a Kinetic Model for Enzymatic Hydrolysis Using Candida rugosa Lipase

Ammar Jamie1, Ali S Alshami2*, Zuhair O Maliabari1 and Muataz A Ateih3

1King Fahd University of Petroleum and Minerals, Dhahran, Kingdom of Saudi Arabia

2University of North Dakota, Grand Forks, ND, USA

3Qatar Environment and Energy Research Institute, Qatar Foundation, Doha, Qatar

*Corresponding Author:
Ali S Alshami
University of North Dakota
241 Centennial Drive Stop 7101
Grand Forks, ND 58201, USA
Tel: 7017776838
Fax: 7017773773
E-mail: [email protected]

Received Date: December 22, 2017; Accepted Date: January 27, 2017; Published Date: January 30, 2017

Citation: Jamie A, Alshami AS, Maliabari ZO, Ateih MA (2017) Development and Validation of a Kinetic Model for Enzymatic Hydrolysis Using Candida rugosa Lipase. J Bioprocess Biotech 7:297. doi: 10.4172/2155-9821.1000297

Copyright: © 2017 Jamie A, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.


Biochemical processing involving enzymatic catalysis of hydrolysis reactions of oils and fats must overcome significant technological barriers before the full benefits of the technology can be realized. Owing to their selectivity and mild reaction conditions, lipases are becoming increasingly important as biocatalysts provided that their kinetics and optimum reaction conditions are well-understood. In this study we report on the development and validation of a kinetic model for the degradation of oils using Candida rugosa lipase, from which a better understanding of the influence of different reaction conditions on hydrolysis kinetics is elucidated. Variations of reaction temperature, mixing speed, enzyme loading and substrate concentrations yielded a maximum lipase activity of 25.67 lipase units (LU), and an activation energy of 4.32 Kcal/gmol. Significantly higher enzyme loading at 0.7 mg/ml was achieved, a 169% increase over most recently reported loading by other investigators. Optimum operating ranges for medium pH and substrate concentration were established to be 7.5 to 8.5, and 30 to 55%, respectively. Reported findings mark a significant improvements over previously reported much narrower ranges of 8.0 for pH and 30 to 43% for the substrate concentration under similar experimental conditions. Developed kinetics model closely predicted and matched experimental results, rendering it suitable for biochemical engineering design application.