Kinetic Behaviour of Free Lipase and Mica-Based Immobilized Lipase Catalyzing the Synthesis of Sugar Esters

Zaidan, Uswatun Hasanah; Rahman, Mohd Basyaruddin Abdul; Othman, Siti Suriani; Basri, Mahiran; Abdulmalek, Emilia; Rahman, Raja Noor Zaliha Raja Abd; Salleh, Abu Bakar

doi:10.1271/bbb.110117

Cited by 3 publications

(1 citation statement)

References 21 publications

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“…Enzyme gave maximum binding efficiency 94.28 on silica matrix when cross linked with 2 of glutaraldehyde. In a previous study the binding efficiency of 86.4 was observed when lipase was immobilized on mica as a support 15 . Previously, the binding efficiency of 70 was observed when lipase from Bacillus coagulans was immobilized on nylon-6 16 and 64 when same enzyme was immobilized on polyethylene support 17 .…”

Section: Immobilization Of Lipase On Silica Matrixmentioning

confidence: 94%

Characterization and Catalytic Properties of Free and Silica-Bound Lipase: a Comparative Study

2014

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Section: Immobilization Of Lipase On Silica Matrixmentioning

confidence: 94%

Characterization and Catalytic Properties of Free and Silica-Bound Lipase: a Comparative Study

2014

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Determination of Lipolytic Enzyme Activities

Jaeger

Kovačić

2014

Methods in Molecular Biology

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Pseudomonas aeruginosa is a versatile human opportunistic pathogen that produces and secretes an arsenal of enzymes, proteins and small molecules many of which serve as virulence factors. Notably, about 40 % of P. aeruginosa genes code for proteins of unknown function, among them more than 80 encoding putative, but still unknown lipolytic enzymes. This group of hydrolases (EC 3.1.1) is known already for decades, but only recently, several of these enzymes have attracted attention as potential virulence factors. Reliable and reproducible enzymatic activity assays are crucial to determine their physiological function and particularly assess their contribution to pathogenicity. As a consequence of the unique biochemical properties of lipids resulting in the formation of micellar structures in water, the reproducible preparation of substrate emulsions is strongly dependent on the method used. Furthermore, the physicochemical properties of the respective substrate emulsion may drastically affect the activities of the tested lipolytic enzymes. Here, we describe common methods for the activity determination of lipase, esterase, phospholipase, and lysophospholipase. These methods cover lipolytic activity assays carried out in vitro, with cell extracts or separated subcellular compartments and with purified enzymes. We have attempted to describe standardized protocols, allowing the determination and comparison of enzymatic activities of lipolytic enzymes from different sources. These methods should also encourage the Pseudomonas community to address the wealth of still unexplored lipolytic enzymes encoded and produced by P. aeruginosa.

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Mathematical modeling of enzymatic syntheses of biosurfactants catalyzed by immobilized lipases

Torres

Lima

Tardioli

et al. 2020

Reac Kinet Mech Cat

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Kinetic Behaviour of Free Lipase and Mica-Based Immobilized Lipase Catalyzing the Synthesis of Sugar Esters

Cited by 3 publications

References 21 publications

Characterization and Catalytic Properties of Free and Silica-Bound Lipase: a Comparative Study

Characterization and Catalytic Properties of Free and Silica-Bound Lipase: a Comparative Study

Determination of Lipolytic Enzyme Activities

Mathematical modeling of enzymatic syntheses of biosurfactants catalyzed by immobilized lipases

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