Binary immobilization of Candida rugosa lipase on chitosan

Hung, Tien‐Chieh; Giridhar, R.; Chiou, Shao-Hua; Wu, Wen‐Teng

doi:10.1016/s1381-1177(03)00167-x

Cited by 172 publications

(75 citation statements)

References 18 publications

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“…It is worth noting that similar results were reported by other authors for immobilization of various enzymes on epoxy-activated supports, describing subtle changes in the pH/temperature activity profile after immobilization (Kunamneni et al 2008;Çelem and Önal, 2009). Overall, these results are similar or favorable compared with those reported in the literature for covalently immobilized CRL on different supports in terms of both recovered activity and thermal stability (Hung et al 2003;Gomes et al 2004;Knežević et al 2006), but much lower than those reported for the lipase covalently immobilized on different agarose (Otero et al 1988). …”

Section: Lipase Immobilization and Characterizationsupporting

confidence: 87%

Use of Candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: batch and fluidized bed reactor study

Saponjić¹,

Knežević‐Jugović²,

Bezbradica³

et al. 2010

Electron Journ of Biotechnol

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Lipase from Candida rugosa was covalently immobilized on Sepabeads EC-EP for application for amyl caprylate synthesis in an organic solvent system. Several solvents were tested in terms of biocatalyst stability and the best result was obtained with isooctane. The lipase-catalyzed esterification in the selected system was performed in batch and fluidized bed reactor systems. The influence of several important reaction parameters including temperature, initial water content, enzyme loading, acid/alcohol molar ratio, and time of addition of molecular sieves is carefully analyzed by means of an experimental design. Almost complete conversion (> 99%) of the substrate to ester could be performed in a batch reactor system, using lipase loading as low as 37 mg g -1 dry support and in a relatively short time (24 hrs) at 37ºC, when high initial substrate molar ratio of 2.2 is used. Kinetics in a fluidized bed reactor system seems to still have a slightly better profile than in the batch system (90.2% yields after 14 hrs). The fluidized bed reactor operated for up 70 hrs almost with no loss in productivity, implying that the proposed process and the immobilized system could provide a promising approach for the amyl caprylate synthesis at the industrial scale.

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Section: Lipase Immobilization and Characterizationsupporting

confidence: 87%

Use of Candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: batch and fluidized bed reactor study

Saponjić¹,

Knežević‐Jugović²,

Bezbradica³

et al. 2010

Electron Journ of Biotechnol

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“…are well-established enzymes for biocatalysis purposes, especially Candida antarctica lipase B (CALB) (Dominguez de Maria et al, 2005). CALB has been studied for potential applications Brazilian Journal of Chemical Engineering Printed in Brazil www.scielo.br/bjce in many different sectors, such as food and flavor making, detergent, pharmaceutical, textile, cosmetic, paper and oleochemical industries (Hasan et al, 2006;Hung et al, 2003). These applications are possible due to the wide range of specificity for substrates, high activity for several different reactions under mild conditions, resistance to organic solvents, high thermal and pH stability, and stereospecificity (Rodrigues et al, 2008, McCabe et al, 2005Deng et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

Production of flavor esters catalyzed by lipase B from Candida antarctica immobilized on magnetic nanoparticles

Souza

Santos

Freire

et al. 2017

Braz. J. Chem. Eng.

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-Candida antarctica Lipase B (CALB) immobilized onto iron magnetic nanoparticles was evaluated as biocatalyst for the synthesis of flavor esters. Methyl and ethyl butyrate were synthesized by esterification of butyric acid with methanol and ethanol, respectively, in a medium containing solvent. The nanoparticles were produced by the co-precipitation method. The process parameters (type of solvent, temperature, substrate concentration, molar ratio, amount of biocatalyst, stirring speed and reaction time) were studied. The optimum conditions for both esters were achieved at 25 °C, 0.5 mol/L (methyl butyrate) and 0.4 mol/L (ethyl butyrate), molar ratio of 1:1, amount of biocatalyst: 10 mg, 150 rpm and 8 h of reaction, using heptane as solvent. Under those conditions, the maximum conversions of methyl butyrate and ethyl butyrate were higher than 90 %. The synthesis of flavor esters was also conducted by using Novozym® 435, a commercial catalyst, for comparison purposes.

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“…Bu yöntem 410 nm dalga boyunda para-nitrofenil palmitatın spektrofotometrik olarak ölçüm esasına dayanır. Lipaz aktivitesinin bir birimi (U) 1 dakikada 1 mikromol p-nitrofenolü hidrolize etmek için gerekli enzim miktarı olarak tanımlanır [21].…”

Section: Analitik öLçüm Yöntemleri (Analytical Measurement Methods)unclassified

Candida utilis MAYASIYLA LİPAZ ENZİMİ AKTİVİTESİNİN FARKLI ORTAM KOŞULLARINDA İNCELENMESİ

Çakmak¹,

Açıkel²

2015

Gazi Üniversitesi Mühendislik-Mimarlık Fakültesi Dergisi

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ÖZETLipazlar (triaçilgliserol hidrolazlar, EC 3.1.1.3), yağ-su ara yüzeyinde, uzun zincirli açilgliserollerin, ester bağlarının hidrolizini katalizleyen hidrolitik enzimlerdir. Bu çalışmada Candida utilis mayasının lipaz enzimi aktivitesi üzerine başlangıç pH, başlangıç sakkaroz derişimi, aktivatör ve inhibitörlerin etkileri araştırılmıştır. Candida utilis mayasının üremesi ve lipaz enzimi üretimi için optimum pH değerinin 4 olduğu tayin edilmiştir. Lipaz enzimi aktivitesinin incelendiği deneysel çalışmalar için hazırlanan besin ortamlarında karbon kaynağı olarak bir şeker endüstrisi atığı olan melas kullanılmıştır. Melas sakkarozunun ana karbon kaynağı olarak kullanıldığı ortamda başlangıç sakkaroz derişiminin artmasıyla lipaz enzimi aktivitesinin arttığı görülmüştür. Besin ortamına soya, mısır, zeytin, ayçiçek ve kanola yağları eklenmiş ve enzim aktivitesini artırıcı etkileri incelendiğinde en yüksek aktivite artışı, ortama %1,25 soya yağı eklendiğinde 788,5 U/L olarak bulunmuştur. STUDY OF LIPASE ENZYM ACTIVITY WITH Candida utilis YEAST IN DIFFERENT MEDIA CONDITION ABSTRACTLipases (triacylglycerol hydrolases, EC 3.1.1.3) are hydrolytic enzymes that can catalyze the hydrolysis of the ester bond of long chain acylglycerols at the oil-water interface. In this study; the effects of initial pH, initial sucrose concentration, activators and inhibitors on Candida utilis yeast, lipase enzym are searched. It is qualified that the optimum pH value for growth rate of Candida utilis yeast and production of lipase enzym is 4. Molasses which is a remnant of sugar industry is used as a main carbon source in nutrient media that is prepared for experimental studies in which lipase enzym activity is worked out. In the media in which molasses is used as a main carbon source, it is observed that lipase enzym activity increases with the increase of initial sucrose concentration. Soybean oil, corn oil, olive oil, sunflower oil and canola oil are added to the nutrient media and when the additive effect of enzym activity is observed it is found out that the highest activity increase is 788,5 U/L with the addition of 1,25% soybean oil. The result is that; Cu(II) and Ni(II) metal ions in the fermantation media lower the lipase activity severly and besides, lowering effect of Ni(II) is much more than that of Cu(II).

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Binary immobilization of Candida rugosa lipase on chitosan

Cited by 172 publications

References 18 publications

Use of Candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: batch and fluidized bed reactor study

Use of Candida rugosa lipase immobilized on sepabeads for the amyl caprylate synthesis: batch and fluidized bed reactor study

Production of flavor esters catalyzed by lipase B from Candida antarctica immobilized on magnetic nanoparticles

Candida utilis MAYASIYLA LİPAZ ENZİMİ AKTİVİTESİNİN FARKLI ORTAM KOŞULLARINDA İNCELENMESİ

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