Optimized preparation and characterization of CLEA-lipase from cocoa pod husk

Khanahmadi, Soofia; Yusof, Faridah; Amid, Azura; Mahmod, Safa Senan; Mahat, Mohd Khairizal

doi:10.1016/j.jbiotec.2014.11.015

Cited by 42 publications

(38 citation statements)

References 63 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This can be seen as a limitation but, in practice, optimizing the aggregation plus cross-linking protocol is not a lengthy procedure and can be readily automated [117]. The response surface methodology (RSM) has been successfully used, for example, in the optimization of the preparation of a CaLB-CLEA 68, a lipase CLEA from cocoa pod husk [118] and a protease CLEA [64]. The optimization of CLEA preparation has been reviewed by several authors [119][120][121].…”

Section: Advantages Limitations and Optimization Of Cleasmentioning

confidence: 99%

CLEAs, Combi-CLEAs and ‘Smart’ Magnetic CLEAs: Biocatalysis in a Bio-Based Economy

2019

View full text Add to dashboard Cite

Biocatalysis has emerged in the last decade as a pre-eminent technology for enabling the envisaged transition to a more sustainable bio-based economy. For industrial viability it is essential that enzymes can be readily recovered and recycled by immobilization as solid, recyclable catalysts. One method to achieve this is via carrier-free immobilization as cross-linked enzyme aggregates (CLEAs). This methodology proved to be very effective with a broad selection of enzymes, in particular carbohydrate-converting enzymes. Methods for optimizing CLEA preparations by, for example, adding proteic feeders to promote cross-linking, and strategies for making the pores accessible for macromolecular substrates are critically reviewed and compared. Co-immobilization of two or more enzymes in combi-CLEAs enables the cost-effective use of multiple enzymes in biocatalytic cascade processes and the use of "smart" magnetic CLEAs to separate the immobilized enzyme from other solids has raised the CLEA technology to a new level of industrial and environmental relevance. Magnetic-CLEAs of polysaccharide-converting enzymes, for example, are eminently suitable for use in the conversion of first and second generation biomass.Catalysts 2019, 9, 261 2 of 31 and deprotection steps. This affords synthetic routes that, compared with conventional organic syntheses, are more step economic, more energy efficient, generate less waste and provide products in exquisite stereochemical purities that are difficult to compete with.Consequently, in the last two decades biocatalysis has emerged as an important technology for meeting the growing demand for green and sustainable processing [2][3][4]. This embraces the whole gamut of chemicals manufacture, from the enantioselective synthesis of chiral drugs [5][6][7][8][9][10][11][12] to the conversion of renewable biomass to liquid fuels and commodity chemicals [13][14][15]. This raises the perennial question: if biocatalysis is so superior why has it not been extensively used in the past? The answer is simple: thanks to advances in molecular biology and biotechnology, biocatalysis has undergone a spectacular leap forward in the last two decades:-Many more enzymes have been identified through (meta)genome mining, that is the in silico analysis of publicly accessible genome sequence data bases that have been generated as a result of next generation genome sequencing [16]. -Advances in gene synthesis have enabled the synthesis of identified genes, ready for cloning into a host production organism, in a few weeks at relatively low cost. This has significantly reduced the cost of development and subsequent production of enzymes at industrial scale. -Advances in protein engineering, using directed evolution techniques [17,18], have enabled optimization of enzyme performance under the challenging conditions encountered in industrial-scale processes, namely, high (stereo)selectivities, activities and space-time yields with non-natural substrates at high substrate concentrations, in the presence of organic solve...

show abstract

Section: Advantages Limitations and Optimization Of Cleasmentioning

confidence: 99%

CLEAs, Combi-CLEAs and ‘Smart’ Magnetic CLEAs: Biocatalysis in a Bio-Based Economy

2019

View full text Add to dashboard Cite

show abstract

“…A higher K m for CLEAs compared with soluble enzyme was also observed by other researchers. 62,63 The increase in K m value of CLEAs might be due to the limited diffusion and reduced accessibility of the substrate as well as the lowered conformational freedom of lipase caused by cross-linking. However, the V max for conventional CLEAs was lower than that of free lipase and spherical CLEAs ( Table 1).…”

Section: The Morphologies Of Cleas In a Microemulsion Systemmentioning

confidence: 99%

Preparation of spherical cross-linked lipase aggregates with improved activity, stability and reusability characteristic in water-in-ionic liquid microemulsion

Cui

Lin

Feng

et al. 2017

J. Chem. Technol. Biotechnol

View full text Add to dashboard Cite

BACKGROUND Cross‐linking enzyme aggregates (CLEAs) seem to be a promising immobilization method due to mild processing conditions and short preparation time. However, the CLEAs prepared in aqueous solution exhibit amorphous large clusters that cause significant mass‐transfer limitations, leading to low catalytic efficiency. In this work, novel spherical CLEAs of lipase from bovine pancreas (spherical CLEAs) were prepared within droplets dispersed in a water‐in‐hydrophobic ionic liquid microemulsion rather than a conventional aqueous solution. The properties of the spherical CLEAs were determined. RESULTS The resultant CLEAs exhibited spherical structure with good monodispersity instead of the amorphous clusters of conventional CLEAs, and showed higher activity recovery (84.6%) than that of conventional CLEAs (52.8%). The high activity recovery of spherical CLEAs could be attributed to both interfacial activation of the microemulsion system and the well‐defined structure of the spherical CLEAs, which not only activated lipases in an active form, but also decreased mass‐transfer limitations. Moreover, the thermostability, storage stability, tolerance against hydrophilic solvents, and mechanical stability of the spherical CLEAs were enhanced significantly. The spherical CLEAs evidenced excellent reusability in comparison with conventional CLEAs. CONCLUSIONS The novel strategy in this study might open an attractive way towards effectively improving the catalytic properties of traditional CLEAs. © 2016 Society of Chemical Industry

show abstract

“…It has been proved by many researchers that phenolic compounds and textile dyes can be degraded or decolored by peroxidase, which has shown that HRP plays an important role in the removal of aqueous phenols and dyes. [32][33][34][35] Compared to another effective biocatalyst-laccase (benzenediol: oxygen oxidoreductase, EC 1.10.3.2), HRP is more economical to produce, inactivates slowly, or acts on a wider variety of substrates.…”

Section: -31mentioning

confidence: 99%

Decolorization of Color Index Acid Orange 20 buffer solution using horseradish peroxidase immobilized on modified PAN-beads

et al. 2017

View full text Add to dashboard Cite

In the present work, horseradish peroxidase (HRP) is utilized to be immobilized onto polyacrylonitrile based beads (PAN-beads) for decolorization of Color Index (C. I.) Acid Orange 20 (AO20) in aqueous solution.Sodium hydroxide and hydrochloric acid were used to treat PAN-beads to obtain carboxyl groups, followed by being modified with ethanediamine to get more amino groups, and then were activated with glutaraldehyde. The enzyme was immobilized onto the activated beads by covalent crosslinking.Optimum factors for decolorization of AO20 were investigated both on free horseradish peroxidase (F-HRP) and immobilized horseradish peroxidase (I-HRP), including pH values, H 2 O 2 amount, enzyme amount, temperature and so on. Under optimum conditions, percent decolorization was about 90% or 98% respectively for F-HRP or I-HRP. A kinetic study showed that F-HRP possessed more affinity compared to I-HRP, but reusability experiments clarified that I-HRP was cost-efficient as about 90% decolorization was obtained after three cycles. The human normal hepatocytes cell line (L02 cell line) was utilized to assess cytotoxicity of metabolites, and the result was acceptable.

show abstract

Optimized preparation and characterization of CLEA-lipase from cocoa pod husk

Cited by 42 publications

References 63 publications

CLEAs, Combi-CLEAs and ‘Smart’ Magnetic CLEAs: Biocatalysis in a Bio-Based Economy

CLEAs, Combi-CLEAs and ‘Smart’ Magnetic CLEAs: Biocatalysis in a Bio-Based Economy

Preparation of spherical cross-linked lipase aggregates with improved activity, stability and reusability characteristic in water-in-ionic liquid microemulsion

Decolorization of Color Index Acid Orange 20 buffer solution using horseradish peroxidase immobilized on modified PAN-beads

Contact Info

Product

Resources

About