scholarly journals Activated Carbon as Support for Lipase Immobilization

2007 ◽  
Vol 5 (2) ◽  
pp. 115
Author(s):  
Mohd Basyaruddin Abdul Rahman ◽  
Mahiran Basri, Mohd Zobir Hussein ◽  
Raja Nor Zaliha Raja Abdul Rahman ◽  
Yau Kim Yan ◽  
Abu Bakar Salleh
Keyword(s):  
Activated Carbon ◽  
Room Temperature ◽  
Storage Stability ◽  
Physical Adsorption ◽  
Immobilized Lipase ◽  
Candida Rugosa ◽  
Lipase Immobilization ◽  
Immobilized Lipases ◽  
Different Types ◽  
Native Lipase

Lipase from<em> Candida rugosa</em> was immobilized onto four different types of activated carbon; KI/2030, KI/3040, KI/5060 and KI/6070. The immobilized lipase was used in the esterification of oleic acid and 1-butanol in hexane. The effects of difference pore sizes, surface area, reaction temperature, thermostability of the immobilized lipases, storage stability in organic solvent and leaching studies were investigated. Among the four samples, KI/6070 gave the highest activities and stability in all the parameters investigated. Immobilized lipases generally exhibit activities higher than the native lipase for the parameters studied, with optimum temperature of 40°C. Immobilized lipases are more stable than native lipase in hexane at room temperature up to 12 days. Leaching study proved that the immobilization of lipase using physical adsorption is cheap and easy. This method was found to be suitable for the attachment of enzyme on the support.

Optimum Conditions for Lipase Immobilization on Halloysitum Rubrum

2013 ◽  
Vol 864-867 ◽  
pp. 465-471
Author(s):  
Tao Deng ◽  
Jun Wei Xu ◽  
Li Huang ◽  
Tao Li ◽  
Xu Ya Yu
Keyword(s):  
Response Surface Methodology ◽  
Experimental Design ◽  
Immobilized Lipase ◽  
Candida Rugosa ◽  
Initial Activity ◽  
Optimum Conditions ◽  
Lipase Immobilization ◽  
Support Materials ◽  
Optimum Ph ◽  
Support Ratio

In this study, we use natural halloysitum rubrum as novel support materials to immobilize Candida rugosa lipase. The response surface methodology with a four-factor three-level Box-Behnken experimental design was used to evaluate the effects of immobilization parameters, such as pH (4.0 to 6.0), immobilization temperature (25 °C to 35 °C), enzyme/support ratio (0.1 to 0.3, w/w), and immobilization time (1 h to 2 h), on the activity of immobilized lipase. The optimum pH, temperature, enzyme/support ratio, and time for immobilized lipase activity (376.09 U/g) were 5.17, 29.65 °C, 0.3 (w/w), and 1.63 h, respectively. After 15 repeated uses, the immobilized lipase still retained 80% of its initial activity, which indicates good reusability.

scholarly journals Preparation and Candida rugosa Lipase Immobilization on Nylon-6 Grafted and Aminated (Polyvinyl Benzyl Chloride) Microfibers

2019 ◽  
Vol 14 (2) ◽  
pp. 369
Author(s):  
Nur Iilani Abd Halin ◽  
Maan Fahmi Rashid Al-Khatib ◽  
Hamzah Mohd. Salleh ◽  
Mohamed Mahmoud Nasef
Keyword(s):  
Benzyl Chloride ◽  
Immobilized Lipase ◽  
Candida Rugosa ◽  
Candida Rugosa Lipase ◽  
Nylon 6 ◽  
Covalent Attachment ◽  
Effect Of Temperature ◽  
P Value ◽  
Lipase Immobilization ◽  
The Stability

This paper demonstrates a simplified procedure for the preparation of a nylon-6 microfibers based support for the immobilization of Candida rugosa lipase via covalent attachment to enhance the stability and reusability of lipase. The preparation of the support was done by radiation induced graft copolymerization (RIGC) of vinyl benzyl chloride (VBC) onto nylon-6 microfibers followed by amination with ethanolamine to facilitate the immobilization of lipase. Fourier transfer infra red (FTIR) and scanning electron microscope (SEM) were used to study the chemical and physical changes following grafting, amination and immobilization. Response surface methodology (RSM) was applied for the optimization of lipase immobilization on the aminated microfibers. The optimization parameters were incubation time, pH, and lipase concentration. Moreover, this study investigated the effect of temperature, pH, and storage stability and reusability on the lipase in its immobilized and free forms. The developed model from RSM showed an R2 value of 0.9823 and P-value < 0.001 indicating that the model is significant. The optimum temperatures for both immobilized and free lipases were 45 °C, whereas the best pH values for lipase activity were at pH 8 and pH 7, respectively. This study also identifies values for KM and Vmax for both immobilized and free lipase accordingly. Based on the results, immobilized lipase had significantly improved the stability and reusability of lipase compared to that in free forms. Copyright © 2019 BCREC Group. All rights reserved 

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

2014 ◽  
Vol 2014 ◽  
pp. 1-10 ◽  
Author(s):  
Nikola Milašinović ◽  
Sonja Jakovetić ◽  
Zorica Knežević-Jugović ◽  
Nedeljko Milosavljević ◽  
Marija Lučić ◽  
...  
Keyword(s):  
Itaconic Acid ◽  
Storage Stability ◽  
Immobilized Lipase ◽  
Candida Rugosa ◽  
Residual Activity ◽  
Hydrolytic Activity ◽  
Esterification Reaction ◽  
Ester Synthesis ◽  
Maximum Reaction Rate ◽  
Esterolytic Activity

This study reports the synthesis of polymeric matrices based onN-isopropylacrylamide and itaconic acid and its application for immobilization of lipase fromCandida 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 (Vmax) and Michaelis-Menten constants (Km) 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.

Synthesis of Fe3O4/P(St-AA) nanoparticles for enhancement of stability of the immobilized lipases

RSC Advances ◽  
2016 ◽  
Vol 6 (110) ◽  
pp. 108583-108589 ◽  
Author(s):  
Zhiming Chen ◽  
Leilei Liu ◽  
Xiaodong Wu ◽  
Renchun Yang
Keyword(s):  
Immobilized Lipase ◽  
Core Shell ◽  
Magnetic Carrier ◽  
Lipase Immobilization ◽  
Immobilized Lipases

Core–shell Fe3O4/P(St-AA) nanoparticles were synthesized and employed as a magnetic carrier for lipase immobilization, and the properties of the immobilized lipase were studied.

scholarly journals Activity and stability of immobilized Candida rugosa lipase on chitosan coated Fe3O4 nanoparticles in aqueous and organic media

2014 ◽  
Vol 10 (3) ◽  
pp. 2478-2483 ◽  
Author(s):  
Mohamed A. Abd-Elhakeem ◽  
Ahmed M. Elsayed ◽  
Taher A. Alkhulaqi
Keyword(s):  
Storage Stability ◽  
Immobilized Enzyme ◽  
Candida Rugosa ◽  
Chitosan Nanoparticles ◽  
Candida Rugosa Lipase ◽  
Initial Activity ◽  
Lipase Immobilization ◽  
Lipase Enzyme ◽  
Immobilized Candida Rugosa Lipase ◽  
And Storage

Fe3O4 (magnetite) nanoparticles were prepared by coprecipitation method, coated by chitosan and functionalized by glutaraldehyde. Lipase enzyme from Candida rugosa was immobilized on the prepared particles via cross linking reaction. Synthesis steps and characterization were examined by XRD, TEM, and FTIR.  The immobilization conditions were 10 mL of phosphate buffer (0.1 M, pH 6.5) containing 30 mg of  functionalized magnetic chitosan nanoparticles and 2.0 mg·mL-1 of lipase, immobilization temperature of 4 ℃ and immobilization time of 1 h. Under these conditions, lipase was successfully immobilized with loading capacity of 87 mg/g. The immobilized enzyme showed good operational and storage stability, where it remained stable after 30 days of storage at 4◦C.and retained about 61% of its initial activity after twenty repeated uses. Finally enzymatic catalyze synthesis of butyl and hexyl oleate at 40 ◦C with shaking (200 rpm) was realized in n-hexane and confirmed by GC analysis.

scholarly journals Immobilization of lipase onto mesoporous silica KIT-6 and montmorillonite K10 for enzymatic hydrolysis of tributyrin

2016 ◽  
Vol 12 (1) ◽  
Author(s):  
Noorulsyahidaini Golbaha ◽  
Zainab Ramli ◽  
Salasiah Endud
Keyword(s):  
Mesoporous Silica ◽  
Incubation Temperature ◽  
Physical Adsorption ◽  
Immobilized Lipase ◽  
High Surface ◽  
Candida Rugosa ◽  
High Surface Area ◽  
Nitrogen Adsorption ◽  
Surface Areas ◽  
Hydrolysis Of

Mesoporous silica KIT-6 and montmorillonite (MMT) K-10 clay were prepared and used for immobilization of the enzyme, Candida rugosa lipases (CRL), aiming at their use as biocatalysts for the hydrolysis of tributyrin. Immobilization of the enzymes onto the supports was performed by physical adsorption using 0.1 M phosphate buffer solutions (pH 7) as the dispersion medium. The activity of the immobilized CRL for tributyrin hydrolysis was investigated at incubation temperature of 40 °C during 120 min and different concentration of the lipase solution for both the supports. Characterization by XRD showed that the long-ranged ordering in the KIT-6 and crystallinity of the MMT K-10 material were affected slightly by the lipase immobilization. This result gives an indication to the present of lipase-support interaction in the immobilized lipase system. Additionally, the results of FTIR spectroscopy verified the presence of silanols on the surfaces of MMT K-10 and KIT-6 materials, while the nitrogen adsorption data showed the resulting immobilized enzyme catalysts were rendered porous, with the KIT-6 giving higher specific surface areas and higher pore diameters in a narrow distribution of sizes ranging from 4 to 12 nm. The immobilization of CRL on KIT-6 and MMT K-10 through hydrogen bonding with the silanol groups, led to an increase in the hydrolysis activity compared to that of free lipase. However, the activity of KIT-6 immobilized CRL was higher than was observed on MMT K-10 immobilized CRL. Furthermore, lipase immobilized on mesoporous silica KIT-6 was shown to be recyclable up to 5 times in aqueous medium. The high surface area and the unique pore system of the mesoporous silica KIT-6, having may be the crucial factors that play an important role in retaining the enzyme in the support, and consequently, improving the lipase activity and stability. 

scholarly journals A simple room temperature-static bioreactor for effective synthesis of hexyl acetate

2019 ◽  
Vol 9 (1) ◽  
pp. 48-55
Author(s):  
Wenwen Cao ◽  
Fangdi Cong ◽  
Jie Kang ◽  
Shulin Zhang ◽  
Xin Li ◽  
...  
Keyword(s):  
Room Temperature ◽  
Physical Adsorption ◽  
Initial Period ◽  
Fold Increase ◽  
Pseudomonas Cepacia ◽  
Hexyl Acetate ◽  
Static State ◽  
Excellent Activity ◽  
Effective Synthesis ◽  
Native Lipase

AbstractFor green synthesis in organic phases, the catalysis of lipases needs to be further improved. Here a strategy is to simulate the activation of lipases at water/oil interface by immobilizing lipase on an available carrier material, which can replace the water at the interface to stabilize enzyme against denaturation from organic phase. The carrier is selected as cotton fiber on which Pseudomonas cepacia lipase is immobilized by physical adsorption in a column glass bottle to form a simple bioreactor together with the bottle. In synthesis of fragrance ester hexyl acetate via transesterification of hexanol with vinyl acetate, the bioreactor exhibits a 3-fold increase in the ability to transform substrate, relative to native lipase in terms of the initial period of reaction at 37°C and 160 rpm. And also the bioreactor is very stable in catalysis for that it has an extra long half life t1/2 = 636 h, calculated from the decrease degree of molar conversions in six times of 6-hour transesterifications. More interestingly, the bioreactor behaves excellent activity at room temperature and in a static state, and can transform nearly 100% hexanol after 48 h. All these indicate that the bioreactor has great potential for industrial application.

scholarly journals Influence of Different Types of Polysaccharide-Based Coatings on the Storage Stability of Fresh-Cut Kiwi Fruit: Assessing the Physicochemical, Antioxidant and Phytochemical Properties

Foods ◽  
2021 ◽  
Vol 10 (11) ◽  
pp. 2806
Author(s):  
Ishrat Guroo ◽  
Amir Gull ◽  
Sajad Mohd Wani ◽  
Sajad Ahmad Wani ◽  
Asma A. Al-Huqail ◽  
...  
Keyword(s):  
Xanthan Gum ◽  
Room Temperature ◽  
Storage Stability ◽  
Total Phenolics ◽  
Titratable Acidity ◽  
Total Phenolic ◽  
Activity Levels ◽  
Kiwi Fruit ◽  
Different Types ◽  
Fresh Cut

The present study focuses on studying the influence of various edible biopolymer coatings at several concentrations on physicochemical, antioxidant and lipid peroxidation activity levels of biopolymer-coated fresh-cut kiwi slices stored at room temperature (relative humidity: 90%). Kiwi slices were coated by dipping in xanthan gum (0.1, 0.2, 0.3% w/v), alginate (1, 2, 3% w/v) and chitosan (0.25, 0.50, 0.75% w/v) solutions for 2 min. Kiwi fruit slices without any treatment were designated as the control. Compared to the control, all coated samples retained higher ascorbic acid, titratable acidity, total phenolic component and antioxidant capacity levels. However, xanthan-gum-coated slices retained significantly higher amounts of total phenolics in comparison to alginate- and chitosan-coated slices (p ≤ 0.05). HPLC analysis showed the presence of neochlorogenic acid, chlorogenic acid, ellagic acid and epicatechin. The results suggest that the xanthan gum can be utilized to enhance the shelf life of fresh-cut kiwi slices without compromising quality.

Candida rugosa lipase immobilization on magnetic silica aerogel nanodispersion

RSC Advances ◽  
2016 ◽  
Vol 6 (15) ◽  
pp. 12676-12687 ◽  
Author(s):  
Leila Amirkhani ◽  
Jafarsadegh Moghaddas ◽  
Hoda Jafarizadeh-Malmiri
Keyword(s):  
Silica Aerogel ◽  
Physical Adsorption ◽  
Candida Rugosa ◽  
Candida Rugosa Lipase ◽  
Lipase Immobilization ◽  
Magnetic Silica

C. rugosalipase was successfully immobilized on hydrophobic magnetic silica aerogel nanodispersion by simple physical adsorption.

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