Design of biocompatible immobilized <i>Candida rugosa</i>
 lipase with potential application in food industry

Ivić, Jovana Trbojević; Veličković, Dušan; Dimitrijević, Aleksandra; Bezbradica, Dejan; Dragačević, Vladimir; Jankulović, Marija Gavrović; Milosavić, Nenad

doi:10.1002/jsfa.7641

Cited by 39 publications

(22 citation statements)

References 31 publications

(46 reference statements)

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“…Lipases (E.C. 3.1.1.3 triacylglycerol acylhydrolases) are one of the most widely used enzymes for biotechnological applications, such as the production of biodiesel, as well as in the food and pharmaceutical industries. To the best of our knowledge, only a limited number of works investigating the catalytic performance of lipases immobilized on MOFs in general, and on ZIFs in particular, have been reported.…”

Section: Introductionmentioning

confidence: 99%

Lipase Encapsulation onto ZIF‐8: A Comparison between Biocatalysts Obtained at Low and High Zinc/2‐Methylimidazole Molar Ratio in Aqueous Medium

et al. 2018

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Lipase AK from Pseudomonas fluorescens and Lipase RM from Rhizomucor miehei were encapsulated into a zeolite imidazolate framework (ZIF‐8) by a “one‐pot” synthesis to obtain AK@ZIF‐8 and RM@ZIF‐8 biocatalysts. The effect of a high (1:40) and low (1:4) Zn/2‐methylimidazole molar ratio on the biocatalysts synthesis was investigated. The different Zn/ligand (L) ratios affected both the surface area, the loading, and the specific activity of the biocatalysts. Samples synthesized by using a high Zn/L ratio had high values of surface area whereas those obtained by using a low Zn/L ratio had higher loadings and specific activities. The decrease of pH (from 11.6 to 9.4) during the synthesis at high Zn/L ratio produced ZIF‐8 samples with features similar to those observed for low Zn/L ratio samples. The low Zn/L (1:4) ratio AK@ZIF‐8 biocatalyst retained 99 % activity after storage for 15 days at 5 °C and 40 % activity after five reaction cycles.

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Section: Introductionmentioning

confidence: 99%

Lipase Encapsulation onto ZIF‐8: A Comparison between Biocatalysts Obtained at Low and High Zinc/2‐Methylimidazole Molar Ratio in Aqueous Medium

et al. 2018

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“…Such a low yield could be attributed to inappropriate solvent choice: in Kobata's paper transformations were carried out in polar organic solvents dioxan and acetone. In contrast, our previous study revealed that n-hexane was the most suitable solvent when working with CRL and there are numerous studies confirming the higher esterification activity of CRL in non-polar solvents (Bezbradica, Mijin, Siler-Marinkovic, & Knezevic, 2006, 2007Trbojević Ivić et al, 2016).…”

Section: Fatty Acid Specificity Of Crlmentioning

confidence: 58%

Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases

et al. 2017

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Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases, Food Chemistry (2016), doi: http://dx. ABSTRACTA commercial preparation of Candida rugosa lipases (CRL) was tested for the production of capsinoids by esterification of vanillyl alcohol (VA) with free fatty acids (FA) and coconut oil (CO) as acyl donors.Screening of FA chain length indicated that C8-C12 FA (the most common FA found in CO triglycerides) are the best acyl-donors, yielding 80-85 % of their specific capsinoids. Hence, when CO, which is rich in these FA, was used as the substrate, a mixture of capsinoids (vanillyl caprylate, vanillyl decanoate and vanillyl laurate) was obtained. The findings presented here suggest that our experimental method can be applied for the enrichment of CO with capsinoids, thus giving it additional health promoting properties.

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“… 8 , 9 In this perspective, it is an ideal carrier for the immobilized enzyme. 10 − 13 In these studies, enzyme immobilized onto the porous HAp supports are highly stable. 14 Although immobilized enzymes have many advantages, they still have disadvantages.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of Pectinase onto Porous Hydroxyapatite/Calcium Alginate Composite Beads for Improved Performance of Recycle

Gao

et al. 2020

ACS Omega

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Pectinase is an industrially important enzyme widely used in juice production, food processing, and other fields. The use of immobilized enzyme systems that allow several reuses of pectinase is beneficial to these fields. Herein, we developed mechanically strong and recyclable porous hydroxyapatite/calcium alginate composite beads for pectinase immobilization. Under the optimal immobilization parameters of 40 °C, pH 4.0, 5.2 U/L pectinase concentration and 4 h reaction time, pectinase showed the highest enzymatic activity (8995 U/mg) and immobilization yield (91%). The thermal stability and pH tolerance of the immobilized pectinase were superior to those of free pectinase. The storage stability of the free and immobilized pectinase for 30 days retained 20 and 50% of their initial activity, respectively. Therefore, these composite beads might be promising support for the efficient immobilization of industrially important enzymes.

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Design of biocompatible immobilized Candida rugosa lipase with potential application in food industry

Cited by 39 publications

References 31 publications

Lipase Encapsulation onto ZIF‐8: A Comparison between Biocatalysts Obtained at Low and High Zinc/2‐Methylimidazole Molar Ratio in Aqueous Medium

Lipase Encapsulation onto ZIF‐8: A Comparison between Biocatalysts Obtained at Low and High Zinc/2‐Methylimidazole Molar Ratio in Aqueous Medium

Synthesis of medium-chain length capsinoids from coconut oil catalyzed by Candida rugosa lipases

Immobilization of Pectinase onto Porous Hydroxyapatite/Calcium Alginate Composite Beads for Improved Performance of Recycle

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