Immobilization of Lipase from Candida Rugosa on Palm-Based Polyurethane Foam as a Support Material

Awang, Roila; Ghazuli, Mohd Rafaei; Basri, Mahiran

doi:10.3844/ajbbsp.2007.163.166

Cited by 36 publications

(14 citation statements)

References 8 publications

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“…Lipases which have been known to catalyze soy-based polyol production such as Pseudomonas sp. and Candida rugosa have been tested in different immobilized support material systems such CaCO 3 , CaSO 4 ·2H 2 O, Ca 2 P 2 O 7 , Celite, polyurethane foam, Eupergit®C, bentotite, alginate beads, silica gel, porous glass surface, and many others (Kuncova et al, 2002;Yesiloglu, 2005;Knezevic et al, 2006;Rosu et al, 1997;Awang et al, 2007).…”

Section: Enzymatic Routesmentioning

confidence: 99%

Soy-Based Polyols and Polyurethanes

Lubguban

Ruda

Aquiatan

et al. 2017

KIMIKA

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Polymers derived from plant oils have attracted major commercial interest and significant attention in scientific research because of the availability, biodegradability, and unique properties of triglycerides. Triglycerides rich in unsaturated fatty acids, such as soybean oil (SBO), are particularly susceptible to chemical modification for desired polymeric materials. Soy-based polyols are important industrial prepolymeric materials that use renewable resources; and can be produced or derived through different processing routes. This review paper discusses previous and recent researches about chemical and biochemical polymerization processes to produce soy-based polyols as prepolymers for the production of polyurethane materials in the form of foams (rigid or flexible) and elastomers. The central goal of these research fields is to find effective reaction routes to increase both equivalent weight and hydroxyl functionality of soy-based polyols while taking into consideration the simplicity and economics of these processes.

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Section: Enzymatic Routesmentioning

confidence: 99%

Soy-Based Polyols and Polyurethanes

Lubguban

Ruda

Aquiatan

et al. 2017

KIMIKA

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“…Proper strategy for the development of lipase immobilization technology provides a number of important benefits including: (a) enzyme reuse, (b) easy of separation of product from enzyme and (c) the potential to run continuous processes via packed-bed reactors (Peilow and Misbah, 2001). In some cases, the activity and stability in terms of thermal, chemical and mechanical properties of the enzyme are, also, improved, thereby allowing their applications under harsher environmental conditions such as pH, temperature and organic solvents (Awang et al, 2007;Bhushan et al, 2008).…”

Section: Immobilization Of Lipasementioning

confidence: 99%

Production of Biodiesel by Enzymatic Transesterification: Review

Ghaly¹,

Dave²,

Brooks³

et al. 2010

American Journal of Biochemistry and Biotechnology

224

108

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Problem Statement:The research on the production of biodiesel has increased significantly in recent years because of the need for an alternative fuel which endows with biodegradability, low toxicity and renewability. Plant oils, animal fats, microalgal oils and waste products such as animal rendering, fish processing waste and cooking oils have been employed as feedstocks for biodiesel production. In order to design an economically and environmentally sustainable biodiesel production process, a proper understanding of the factors affecting the process and their relative importance is necessary. Approach: A comprehensive review of the literature on the subject of biodiesel production was carried out. Traditionally biodiesel has been produced using either acid or base catalysts. The multi-step purification of end products, wastewater treatment and energy demand of the conventional process has lead to search for alternative option for production of biodiesel. The use the enzyme lipase as a biocatalyst for the transesterification reaction step in biodiesel production has been extensively investigated. Lipase is produced by all living organisms and can be used intracellularly or extracellularly. Conclusion: To date, the most popular microbes used for their lipases have been filamentous fungi and recombinant bacteria. A summary of lipases used in transesterification and their optimum operating conditions is provided. In addition to the choice of lipase employed, factors which make the transesterification process feasible and ready for commercialization are: enzyme modification, the selection of feedstock and alcohol, use of common solvents, pretreatment of the lipase, alcohol to oil molar ratio, water activity/content and reaction temperature. Optimization of these parameters is necessary in order toreduce the cost of biodiesel production. Use of no/low cost waste materials as feedstocks will have double environmental benefits by reducing the environmental pollution potential of the wastes and producing an environmentally friendly fuel.

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“…They are the most popular enzymes in biocatalysis, because they can be used in a variety of reactions due to their regio-and enantioselectivity [2][3][4][5]. During the last decade, lipases have gained more attention due to their applications in chemical and pharmaceutical industries in hydrolytic, esterification, transesterification, and various synthetic reactions in aqueous and organic media [6][7][8]. Lipases are able to catalyze the hydrolysis of triacylglycerides in aqueous and ester synthesis in organic media [9].…”

Section: Introductionmentioning

confidence: 99%

“…To exploit their technical and economical advantages, it is recommended to immobilize the enzymes to reduce their price and to enhance stability. Immobilized enzymes have many advantages over their non-immobilized counterparts due to their higher storing, operational, thermal and/or conformational stability, the simple recovery of catalyst and products after reaction, and the possibility of continuous reaction and easy operation and design of a bioreactor [6,11]. Many techniques for lipase immobilization have been developed over last three decades.…”

Section: Introductionmentioning

confidence: 99%

Stability of lipase immobilized on O-pentynyl dextran

Tahir

Adnan

Strömberg³

et al. 2011

Bioprocess Biosyst Eng

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O-Pentynyl dextran (PyD), an amphiphilic polysaccharide derivative with a degree of substitution (DS) of 0.43 was compared with ion exchange resins Lewatit VP OC 1600, Amberlite XAD 761 and Duolite A568 for immobilization of Lipase from Rhizopus arrhizus by adsorption method. The immobilized enzymes were employed for esterification of octanoic acid with geraniol in n-hexane as model reaction. PyD showed higher lipase adsorption and with 249 μmol min(-1) g(-1) significant higher esterification activity than the other supports (67-83 μmol min(-1) g(-1)). Biocatalysts from all types of supports except PyD became completely inactive within 8 weeks storing at -10 °C while lipase immobilized on PyD retained its full esterification activity for at least 14 weeks. In repeated use, yield decreased rapidly after two cycles for all supports except for PyD. For this biopolymeric support, constantly 90% yield was achieved even after eight cycles, when the biocatalyst was washed with n-hexane and water and then freeze-dried. To achieve this yield, prolonged reaction times were required, partly on the account of an increasing delay period, probably to adapt active conformation, until the reaction starts.

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Immobilization of Lipase from Candida Rugosa on Palm-Based Polyurethane Foam as a Support Material

Cited by 36 publications

References 8 publications

Soy-Based Polyols and Polyurethanes

Soy-Based Polyols and Polyurethanes

Production of Biodiesel by Enzymatic Transesterification: Review

Stability of lipase immobilized on O-pentynyl dextran

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