Esterification reactions catalyzed by lipases immobilized in organogels: effect of temperature and substrate diffusion

Zoumpanioti, Maria; Parmaklis, P.; Marı́a, Pablo Domı́nguez de; Stamatis, Haralambos; Sinisterra, J. V.; Xenakis, Aristotelis

doi:10.1007/s10529-008-9734-1

Cited by 23 publications

(21 citation statements)

References 15 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…4 shows that these lipase preparations are behaving similarly as the temperature is raised from 30°C to 70°C. This confirms that our system exhibits a similar temperature dependency as those reported elsewhere (Zoumpanioti et al, 2008). This further supports that our preparations can activate to a level that is commonly obtained for the same enzyme immobilized on supports with different chemical and physical properties.…”

Section: Resultssupporting

confidence: 91%

“…Immobilization of enzymes on porous and non-porous solid supports has been intensively explored (Long et al, 2007;Persson et al, 2002). The preferred matrices for immobilization include macroporous polypropylene particles (Bosley and Peilow, 1997), hydrophilic silicon wafers (van der Veen et al, 2007), microemulsions and organogels (Zoumpanioti et al, 2008). Additional efforts include improving compatibility with the solvents by chemical modification of the enzymes' surface (Sheldon et al, 2005), protein engineering (Hudson et al, 2005), and co-lyophilization of the enzyme with various adjuvants, such as cyclodextrin (Ghanem, 2003;Mine et al, 2003), inorganic salts (Lindsay et al, 2002(Lindsay et al, , 2004, and crown ethers (Mine et al, 2003;Santos et al, 2001;Secundo et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Enantioselective transesterification by Candida antarctica Lipase B immobilized on fumed silica

Kramer

Cruz

Pfromm

et al. 2010

Journal of Biotechnology

View full text Add to dashboard Cite

Enzymatic catalysis to produce molecules such as perfumes, flavors, and fragrances has the advantage of allowing the products to be labeled "natural" for marketing in the U.S., in addition to the exquisite selectivity and stereoselectivity of enzymes that can be an advantage over chemical catalysis. Enzymatic catalysis in organic solvents is attractive if solubility issues of reactants or products, or thermodynamic issues (water as a product in esterification) complicate or prevent aqueous enzymatic catalysis. Immobilization of the enzyme on a solid support can address the generally poor solubility of enzymes in most solvents.We have recently reported on a novel immobilization method for Candida antarctica Lipase B on fumed silica to improve the enzymatic activity in hexane. This research is extended here to study the enantioselective transesterification of (RS)-1-phenylethanol with vinyl acetate. The maximum catalytic activity for this preparation exceeded the activity (on an equal enzyme amount basis) of the commercial Novozyme 435® significantly. The steady-state conversion for (R)-1-phenylethanol was about 75% as confirmed via forward and reverse reaction. The catalytic activity steeply increases with increasing nominal surface coverage of the support until a maximum is reached at a nominal surface coverage of 230%. We hypothesize that the physical state of the enzyme molecules at a low surface coverage is dominated in this case by detrimental strong enzyme-substrate interactions. Enzyme-enzyme interactions may stabilize the active form of the enzyme as surface coverage increases while diffusion limitations reduce the apparent catalytic performance again at multi-layer coverage. The temperature-, solvent-, and long-term stability for CALB/fumed silica preparations showed that these preparations can tolerate temperatures up to 70°C, continuous exposure to solvents, and long term storage.2

show abstract

Section: Resultssupporting

confidence: 91%

Section: Introductionmentioning

confidence: 99%

Enantioselective transesterification by Candida antarctica Lipase B immobilized on fumed silica

Kramer

Cruz

Pfromm

et al. 2010

Journal of Biotechnology

View full text Add to dashboard Cite

show abstract

“…Shifting to biotechnological methods allows us to implement these processes under milder conditions using simpler and more environmentally friendly technology [2][3][4][5]. However, the use of enzy matic synthesis in the esterification of PEG is hin dered by the high viscosity of PEG and the low water solubility of FAs.…”

Section: Introductionmentioning

confidence: 99%

Enzymatic synthesis of polyethylene glycol-400 esters

et al. 2015

View full text Add to dashboard Cite

Esters of fatty acids (FAs) and polyethylene glycol 400 (PEG) are valuable chemically derived surfactants. In this work, it is shown that the chemical synthesis of PEG esters can be replaced by enzymatic synthesis under milder conditions and using simpler and more environmentally friendly technology. The main obstacles to enzymatic catalysis in a system of PEG and higher FAs are the high viscosity of the former and the low water solubility of the latter. These problems are solved by selecting organic media and other con ditions of the process mediated by pancreatic lipase. The optimum conditions for the synthesis of PEG esters of FAs are determined: reaction medium, benzene/hexane in a ratio of 2 : 3; optimum temperature, 25°C; water content in the system, no more than 0.2%; FA : PEG molar ratio, 1 : 1.8; reaction time, 48 h. Under these conditions, the yields in synthesizing PEG esters of capric, lauric, and palmitic acids are 80, 78, and 44%, respectively.

show abstract

“…However, the systems formed by amphiphilic networks have not been widely studied as tools for enzyme reactions in hydrophobic solvents [1, 2]. In such systems, the interfacial active enzyme, such as lipase, can effectively catalyze not only hydrolytic but also synthetic reactions [3, 4].…”

Section: Introductionmentioning

confidence: 99%

Catalyzed Ester Synthesis UsingCandida rugosaLipase Entrapped by Poly(N-isopropylacrylamide-co-itaconic Acid) Hydrogel

Milašinović¹,

Jakovetić

Knežević‐Jugović

et al. 2014

The Scientific World Journal

View full text Add to dashboard Cite

This study reports the synthesis of polymeric matrices based on N-isopropylacrylamide and itaconic acid and its application for immobilization of lipase from Candida rugosa. The lipase was immobilized by entrapment method. Free and immobilized lipase activities, pH and temperature optima, and storage stability were investigated. The optimum temperature for free and entrapped lipase was found to be 40 and 45°C, while the optimum pH was observed at pH 7 and 8, respectively. Both hydrolytic activity in an aqueous medium and esterolytic activity in an organic medium have been evaluated. Maximum reaction rate (V max) and Michaelis-Menten constants (K m) were also determined for immobilized lipase. Storage stability of lipase was increased as a result of immobilization process. Furthermore, the operational stability and reusability of the immobilized lipase in esterification reaction have been studied, and it was observed that after 10 cycles, the residual activity for entrapped lipase was as high as 50%, implying that the developed hydrogel and immobilized system could provide a promising solution for the flavor ester synthesis at the industrial scale.

show abstract

Esterification reactions catalyzed by lipases immobilized in organogels: effect of temperature and substrate diffusion

Cited by 23 publications

References 15 publications

Enantioselective transesterification by Candida antarctica Lipase B immobilized on fumed silica

Enantioselective transesterification by Candida antarctica Lipase B immobilized on fumed silica

Enzymatic synthesis of polyethylene glycol-400 esters

Catalyzed Ester Synthesis UsingCandida rugosaLipase Entrapped by Poly(N-isopropylacrylamide-co-itaconic Acid) Hydrogel

Contact Info

Product

Resources

About