scholarly journals Highly Efficient Lipase Catalyzed Monoaminolysis Reaction of Diesters with Benzylamine

2019 ◽  
Vol 14 (6) ◽  
pp. 1934578X1985998
Author(s):  
Gerardo Valerio-Alfaro ◽  
Patricia Harumi Castillo-Carrasco ◽  
Olaya Pirene Castellanos Onorio ◽  
Jorge Bautista Naranjos
Keyword(s):  
Immobilized Lipase ◽  
Candida Rugosa ◽  
Diethyl Malonate ◽  
Rhizomucor Miehei ◽  
Solvent Polarity ◽  
Pharmaceutical Products ◽  
Pseudomonas Cepacia ◽  
Butyl Ether ◽  
Highly Efficient ◽  
Diethyl Succinate

Preparation of amides by biocatalyzed aminolysis reactions has greatly increased because these processes play an important role in the preparation of some pharmaceutical products and their intermediates. A highly efficient synthesis of malonic (5), succinic (6), and malic (8) monoamide esters by desymmetrization transformations (mono aminolysis reactions) of their diesters is presented. The immobilized lipase from Candida antarctica (CaL-B, Novozym 435) catalyzed the mono aminolysis of bifunctional compounds: diesters such as diethyl malonate (1), diethyl succinate (2), and ( R, S)-malate (3), leading to their corresponding monoamides (5), (6), and (8), respectively, with high conversions after a 24 hour reaction in the presence of an organic solvent. Increasing the solvent polarity from toluene, methyl t-butyl ether to dioxane led to an improved conversion. According to qualitative and quantitative GC-MS analysis, conversions of diesters (1), (2), and (3) into their mono amide esters were in the range 65%-97%. CaL-B was the best biocatalyst of the commercial lipases used, including those from Candida rugosa, Rhizomucor miehei, Carica papaya, and Pseudomonas cepacia. Likewise, a yield of 91% regioisomeric, but virtually racemic ( R,S)-mono amide (8) was obtained as the single product in dioxane.

scholarly journals Improved Catalytic Performance of Carrier-Free Immobilized Lipase by Advanced Cross-Linked Enzyme Aggregates Technology

2021 ◽  
Author(s):  
Xia Jiaojiao ◽  
Yan Yan ◽  
Bin Zou ◽  
Adesanya Idowu Onyinye
Keyword(s):  
Low Cost ◽  
Immobilized Lipase ◽  
Candida Rugosa ◽  
Residual Activity ◽  
Candida Rugosa Lipase ◽  
Catalytic Performance ◽  
Functional Surface ◽  
Carrier Free ◽  
Effective Synthesis ◽  
Repeated Use

Abstract The cross-linked enzyme aggregates (CLEAs) are one of the technologies that quickly immobilize the enzyme without a carrier. This carrier-free immobilization method has the advantages of simple operation, high reusability and low cost. In this study, ionic liquid with amino group (1-aminopropyl-3-methylimidazole bromide，IL) was used as the novel functional surface molecule to modify industrialized lipase (Candida rugosa lipase, CRL). The enzymatic properties of the prepared CRL-FIL-CLEAs were investigated. The activity of CRL-FIL-CLEAs (5.51 U/mg protein) was 1.9 times higher than that of CRL-CLEAs without surface modification (2.86 U/mg protein). After incubation at 60℃ for 50 min, CRL-FIL-CLEAs still maintained 61% of its initial activity, while the value for CRL-CLEAs was only 22%. After repeated use for five times, compared with the 22% residual activity of CRL-CLEAs, the value of CRL-FIL-CLEAs was 51%. Further kinetic analysis indicated that the Km values for CRL-FIL-CLEAs and CRL-CLEAs were 4.80 mM and 8.06 mM, respectively, which was inferred that the affinity to substrate was increased after modification. Based on the above results, it was indicated that this method provided a new idea for the effective synthesis of immobilized enzyme.

scholarly journals Biosynthesis of ethyl butyrate with immobilized Candida rugosa lipase onto modified Eupergit®C

Biocatalysis ◽  
2014 ◽  
Vol 1 (1) ◽  
pp. 1-12 ◽  
Author(s):  
Daniele Spinelli ◽  
Simone Coppi ◽  
Riccardo Basosi ◽  
Rebecca Pogni
Keyword(s):  
Immobilized Lipase ◽  
Candida Rugosa ◽  
Product Yield ◽  
Candida Rugosa Lipase ◽  
Maximum Activity ◽  
Ethyl Butyrate ◽  
Molar Ratio ◽  
Practical Applications ◽  
Solvent Free Conditions ◽  
Immobilized Candida Rugosa Lipase

AbstractLipase from Candida rugosa was immobilized onto the modified Eupergit®C. The support was treated with ethylenediamine and subsequently activated with glutaraldehyde. Enzyme immobilization efficiency was 85%. The optimum pH was close to 6.5 for both the free and immobilized lipase. Immobilized lipase retained its maximum activity in a temperature range of 55 – 60°C. Subsequently, ethyl butyrate synthesis was investigated using immobilized enzyme by esterification of butyric acid with ethanol in solvent-free conditions (23% product yield) and using hexane as a solvent (65% product yield). The acid-alcohol molar ratio and different enzyme amounts were tested as efficient reaction parameters. The biocatalyst maintained 60% of its activity when reused in 8 successive batch reactions in organic solvent. Therefore, the immobilized lipase has demonstrated its potential in practical applications such as short-chain ester synthesis for the food industry.

scholarly journals Highly Efficient Synthesis of Phytosterol Linolenate Catalyzed by Candida Rugosa Lipase through Transesterification

2017 ◽  
Vol 23 (4) ◽  
pp. 525-533 ◽  
Author(s):  
Wen-Sen He ◽  
Dan-Dan Cui ◽  
Yi-Lu Zhang ◽  
Yu Liu ◽  
Ji Yin ◽  
...  
Keyword(s):  
Candida Rugosa ◽  
Efficient Synthesis ◽  
Highly Efficient

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.

Esterification of polyunsaturated fatty acids by various forms of immobilized lipase from Rhizomucor miehei

Lipids ◽  
2000 ◽  
Vol 35 (4) ◽  
pp. 461-466 ◽  
Author(s):  
Yoshitsugu Kosugi ◽  
Prodyut Kumar Roy ◽  
Qinglong Chang ◽  
Cao Shu-gui ◽  
Makoto Fukatsu ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Polyunsaturated Fatty Acids ◽  
Immobilized Lipase ◽  
Rhizomucor Miehei

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 The influence of composition of poly(n-isopropylacrylamide-co-itaconic acid) hydrogel on immobilized Candida rugosa lipase activity

2008 ◽  
Vol 62 (6) ◽  
pp. 339-344
Author(s):  
Nikola Milasinovic ◽  
Melina Kalagasidis-Krusic ◽  
Zorica Knezevic-Jugovic ◽  
Jovanka Filipovic
Keyword(s):  
Mechanical Properties ◽  
Itaconic Acid ◽  
Lipase Activity ◽  
Acid Content ◽  
Immobilized Enzyme ◽  
In Situ Polymerization ◽  
Immobilized Lipase ◽  
Candida Rugosa ◽  
Candida Rugosa Lipase

The application of lipases as catalysts in chemical reactions has been deterred by the high cost of isolation and purification of enzymes, the instability of their structure when they are isolated from their natural environment, contamination of products with residual protein, their sensitivity to process conditions, etc. These problems could be overcome using immobilized lipases. Immobilization is achieved by fixing enzymes to or within solid supports and as a result a heterogeneous system is obtained. The present paper reports on the immobilization of Candida rugosa lipase in hydrogels based on N-isopropylacrylamide and itaconic acid. Immobilization of lipase is carried out by two different methods. In the first method, lipase is added to the reaction mixture before polymerization and crosslinking (in situ polymerization), while in the second method the synthetized hydrogels are immersed in lipase solution and left to rich the equilibrium swelling. The specific activities of the immobilized lipase were determined in both cases and compared. The amount of the immobilized lipase is higher if the immobilization is carried out by immersing hydrogel in lipase solution. It was observed that in both cases lipase activity increases with an increase of the itaconic acid content up to 10 wt% and thereafter decreases. From the measurements of shear storage moduli (G') it was concluded that the increase of the itaconic acid content decreases the mechanical properties of the hydrogels. SEM analysis confirmed the highly porous structure of hydrogels. It was found that greater pores were achieved when the enzyme was immobilized by in situ polymerization. When the enzyme was immobilized by in situ polymerization the itaconic acid content had not great effect on the mass of the immobilized enzyme, except for the 100/0 sample. On the contrary, for the samples where the enzyme was immobilized by swelling, the increase of the itaconic acid content increases the mass of the immobilized enzyme. Concerning the activity of the immobilized lipase, the swelling degree and mechanical properties of the investigated hydrogels, the best results were performed by the 95/5 hydrogel sample.

scholarly journals Burkholderia cepacia Complex Bacteria: a Feared Contamination Risk in Water-Based Pharmaceutical Products

2020 ◽  
Vol 33 (3) ◽  
Author(s):  
Mariana Tavares ◽  
Mariya Kozak ◽  
Alexandra Balola ◽  
Isabel Sá-Correia
Keyword(s):  
Burkholderia Cepacia ◽  
Bacterial Species ◽  
Public Health Problem ◽  
Pharmaceutical Products ◽  
Health Care Facilities ◽  
Burkholderia Cepacia Complex ◽  
Pseudomonas Cepacia ◽  
Environmental Distribution ◽  
Content Type ◽  
Metabolic Versatility

SUMMARY Burkholderia cepacia (formerly Pseudomonas cepacia) was once thought to be a single bacterial species but has expanded to the Burkholderia cepacia complex (Bcc), comprising 24 closely related opportunistic pathogenic species. These bacteria have a widespread environmental distribution, an extraordinary metabolic versatility, a complex genome with three chromosomes, and a high capacity for rapid mutation and adaptation. Additionally, they present an inherent resistance to antibiotics and antiseptics, as well as the abilities to survive under nutrient-limited conditions and to metabolize the organic matter present in oligotrophic aquatic environments, even using certain antimicrobials as carbon sources. These traits constitute the reason that Bcc bacteria are considered feared contaminants of aqueous pharmaceutical and personal care products and the frequent reason behind nonsterile product recalls. Contamination with Bcc has caused numerous nosocomial outbreaks in health care facilities, presenting a health threat, particularly for patients with cystic fibrosis and chronic granulomatous disease and for immunocompromised individuals. This review addresses the role of Bcc bacteria as a potential public health problem, the mechanisms behind their success as contaminants of pharmaceutical products, particularly in the presence of biocides, the difficulties encountered in their detection, and the preventive measures applied during manufacturing processes to control contamination with these objectionable microorganisms. A summary of Bcc-related outbreaks in different clinical settings, due to contamination of diverse types of pharmaceutical products, is provided.

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