Immobilization and Stabilization of Microbial Lipases
Само за регистроване кориснике
2018
Поглавље у монографији (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
Lipases (triacylglycerol acyl hydrolases, E.C. 3.1.1.3) are ubiquitous enzymes that catalyze numerous reactions such as hydrolysis, interesterification, esterification, alcoholysis, acidolysis and aminolysis. Broad substrate specificity and high stereo-, regio- and chemoselectivity make lipases attractive catalysts in a wide range of industrial applications. Lipases are used in the food, pharmaceutical, agrochemical, oleochemical, cosmetic and detergent industries. In spite of their tremendous potential, commercial application of lipases in industry is still limited due to their high cost and relatively low stability. This chapter describes the use of enzyme immobilization as an efficient strategy to overcome these drawbacks. Immobilization of lipases enhances properties such as thermostability and activity, facilitates separation of products and provides more flexibility with enzyme/substrate contact by using various reactor configurations.
Numerous methods for lipase immobilization ...are available. Baring in mind the scope of this book, the most common methods, including adsorption, cross-linking, adsorption followed by cross-linking, multipoint covalent attachment and physical entrapment will be discussed in detail. Advantages and disadvantages of commonly used immobilization methods and the design and selection of immobilization strategies are analyzed as well. Particular emphasis is placed on the most recent advances in the development of an efficient lipase immobilization system that would enable us to achieve the desired benefits. This chapter will also highlight benefits of immobilization in lipase stabilization, with respect to other employed methods such as chemical modification and recombinant DNA technology.
Кључне речи:
lipase / immobilization / immobilization methods / immobilization carriers / biotransformationsИзвор:
Lipases: Structure, Functions and Role in Health and Disease, 2018, 55-105Издавач:
- Nova Science Publishers, Inc.
Финансирање / пројекти:
- Алергени, антитела, ензими и мали физиолошки значајни молекули: дизајн, структура, функција и значај (RS-MESTD-Basic Research (BR or ON)-172049)
Колекције
Институција/група
Inovacioni centar / Innovation CentreTY - CHAP AU - Trbojević-Ivić, Jovana AU - Veličković, Dušan AU - Dimitrijević, Aleksandra AU - Milosavić, Nenad PY - 2018 UR - http://cherry.chem.bg.ac.rs/handle/123456789/5287 AB - Lipases (triacylglycerol acyl hydrolases, E.C. 3.1.1.3) are ubiquitous enzymes that catalyze numerous reactions such as hydrolysis, interesterification, esterification, alcoholysis, acidolysis and aminolysis. Broad substrate specificity and high stereo-, regio- and chemoselectivity make lipases attractive catalysts in a wide range of industrial applications. Lipases are used in the food, pharmaceutical, agrochemical, oleochemical, cosmetic and detergent industries. In spite of their tremendous potential, commercial application of lipases in industry is still limited due to their high cost and relatively low stability. This chapter describes the use of enzyme immobilization as an efficient strategy to overcome these drawbacks. Immobilization of lipases enhances properties such as thermostability and activity, facilitates separation of products and provides more flexibility with enzyme/substrate contact by using various reactor configurations. Numerous methods for lipase immobilization are available. Baring in mind the scope of this book, the most common methods, including adsorption, cross-linking, adsorption followed by cross-linking, multipoint covalent attachment and physical entrapment will be discussed in detail. Advantages and disadvantages of commonly used immobilization methods and the design and selection of immobilization strategies are analyzed as well. Particular emphasis is placed on the most recent advances in the development of an efficient lipase immobilization system that would enable us to achieve the desired benefits. This chapter will also highlight benefits of immobilization in lipase stabilization, with respect to other employed methods such as chemical modification and recombinant DNA technology. PB - Nova Science Publishers, Inc. T2 - Lipases: Structure, Functions and Role in Health and Disease T1 - Immobilization and Stabilization of Microbial Lipases SP - 55 EP - 105 UR - https://hdl.handle.net/21.15107/rcub_cherry_5287 ER -
@inbook{ author = "Trbojević-Ivić, Jovana and Veličković, Dušan and Dimitrijević, Aleksandra and Milosavić, Nenad", year = "2018", abstract = "Lipases (triacylglycerol acyl hydrolases, E.C. 3.1.1.3) are ubiquitous enzymes that catalyze numerous reactions such as hydrolysis, interesterification, esterification, alcoholysis, acidolysis and aminolysis. Broad substrate specificity and high stereo-, regio- and chemoselectivity make lipases attractive catalysts in a wide range of industrial applications. Lipases are used in the food, pharmaceutical, agrochemical, oleochemical, cosmetic and detergent industries. In spite of their tremendous potential, commercial application of lipases in industry is still limited due to their high cost and relatively low stability. This chapter describes the use of enzyme immobilization as an efficient strategy to overcome these drawbacks. Immobilization of lipases enhances properties such as thermostability and activity, facilitates separation of products and provides more flexibility with enzyme/substrate contact by using various reactor configurations. Numerous methods for lipase immobilization are available. Baring in mind the scope of this book, the most common methods, including adsorption, cross-linking, adsorption followed by cross-linking, multipoint covalent attachment and physical entrapment will be discussed in detail. Advantages and disadvantages of commonly used immobilization methods and the design and selection of immobilization strategies are analyzed as well. Particular emphasis is placed on the most recent advances in the development of an efficient lipase immobilization system that would enable us to achieve the desired benefits. This chapter will also highlight benefits of immobilization in lipase stabilization, with respect to other employed methods such as chemical modification and recombinant DNA technology.", publisher = "Nova Science Publishers, Inc.", journal = "Lipases: Structure, Functions and Role in Health and Disease", booktitle = "Immobilization and Stabilization of Microbial Lipases", pages = "55-105", url = "https://hdl.handle.net/21.15107/rcub_cherry_5287" }
Trbojević-Ivić, J., Veličković, D., Dimitrijević, A.,& Milosavić, N.. (2018). Immobilization and Stabilization of Microbial Lipases. in Lipases: Structure, Functions and Role in Health and Disease Nova Science Publishers, Inc.., 55-105. https://hdl.handle.net/21.15107/rcub_cherry_5287
Trbojević-Ivić J, Veličković D, Dimitrijević A, Milosavić N. Immobilization and Stabilization of Microbial Lipases. in Lipases: Structure, Functions and Role in Health and Disease. 2018;:55-105. https://hdl.handle.net/21.15107/rcub_cherry_5287 .
Trbojević-Ivić, Jovana, Veličković, Dušan, Dimitrijević, Aleksandra, Milosavić, Nenad, "Immobilization and Stabilization of Microbial Lipases" in Lipases: Structure, Functions and Role in Health and Disease (2018):55-105, https://hdl.handle.net/21.15107/rcub_cherry_5287 .