Cross-linked enzyme aggregates (CLEAs) with controlled particles: Application to Candida rugosa lipase

Yu, Hongwei; Chen, Haidan; Wang, Xuehang; Yang, Yin; Ching, Chi Bun

doi:10.1016/j.molcatb.2006.07.001

Cited by 132 publications

(79 citation statements)

References 9 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Any parameter that may change the aggregation or the aggregate cross-linking will possibly have an effect on the recovered activity and particle size. Likewise, the co-interaction among these three main factors (cross-linker, precipitant and additive) in many cases can affect CLEAs final form (Yu et al 2006).…”

Section: Optimization Of Clea-protease Preparation Conditionsmentioning

confidence: 99%

See 1 more Smart Citation

Optimizing the preparation conditions and characterization of a stable and recyclable cross-linked enzyme aggregate (CLEA)-protease

Mahmod

Yusof

Jami

et al. 2016

Bioresour. Bioprocess.

View full text Add to dashboard Cite

Background: Cross-linked enzyme aggregate (CLEA) is considered as an effective technique in the production of immobilized biocatalysts for its industrially attractive advantages. Simplicity, stability, low cost, time saving and reusability are proved to be some of CLEA's main advantages. Results:In this study, an active, stable and recyclable CLEA-protease from the viscera of channel catfish Ictalurus punctatus has been prepared. Optimization of the preparation parameters is carried out with the help of Response Surface Methodology. This methodology helped in studying the interaction between the most contributing factors such as cross-linker, precipitant and the additive concentrations. The optimum specific activity for CLEA-protease of 4.512 U/mg protein has shown a high stability against the denaturation forces such as temperature and pH as compared to free protease. It is further found from the study that the highest activity was achieved at the pH of 6.8 and at the temperature of 45 °C. After six cycles, CLEA-protease maintained 28 % of its original activity. Additionally, Michaelis-Menten models were used to determine the kinetic parameters i.e. K m and V max that helped in showing a significant difference after immobilization as compared to free protease. Conclusion:This work found that this novel CLEA-protease can be used as a very active biocatalyst in industrial applications.

show abstract

Section: Optimization Of Clea-protease Preparation Conditionsmentioning

confidence: 99%

“…The solvent stability of CLEA is important to be determined since many studies have reported some limitations of using organic solvent with CLEA (Yu et al 2006;Kartal et al 2011). Polar solvents (i.e.…”

Section: Organic Solvent Stability Of Clea-proteasementioning

confidence: 99%

Optimizing the preparation conditions and characterization of a stable and recyclable cross-linked enzyme aggregate (CLEA)-protease

Mahmod

Yusof

Jami

et al. 2016

Bioresour. Bioprocess.

View full text Add to dashboard Cite

show abstract

“…They compress the solvation layer and increase proteinprotein interaction. These precipitated aggregates are then cross-linked with the help of agents like glutaraldehyde, which is a bifunctional reactive agent, capable of reacting with the surface amino groups of enzymes [27,28].…”

Section: Cross-linked Enzyme Aggregatesmentioning

confidence: 99%

“…Also, increased amounts of enzyme and glutaraldehyde increase particle size. The particle size is important, as it influences the accessibility of the inner enzymes to the substrates in the reaction mixture [27]. Thus, greater particle size leads to wasted lipase activity.…”

Section: Figure 6: Aggregation and Cross-linking Of An Enzyme To Prepmentioning

confidence: 99%

“…This leads to a highly concentrated enzyme activity, high stability and low production cost due to the lack of additional carrier [27]. It is a one step purification and immobilization process, making it responsive to rapid optimization, which translates to low cost and short time-tomarket process [28].…”

Section: Figure 6: Aggregation and Cross-linking Of An Enzyme To Prepmentioning

confidence: 99%

See 1 more Smart Citation

Lipase Immobilization Techniques for Biodiesel Production: An Overview

Nigam¹,

Mehrotra²,

Vani³

et al. 2014

IJREB

View full text Add to dashboard Cite

The growing energy needs and depleting fuel sources compel us to look towards production of biodiesel, an appropriate alternative. The industrially used chemical catalysis process is beset with problems that enzymatic production using lipases could avoid. In this light, the immobilization of lipases plays an important role in the optimization of the production process. This review discusses the various techniques that have been studied for lipase immobilization, namely adsorption, covalent attachment, entrapment, cross-linked enzyme agglomerates and whole-cell biocatalysts, while highlighting their benefits and drawbacks. It also sheds light on the future of enzyme immobilization and its industrial application.

show abstract

Ionic Liquids as (Co‐)Solvents for Hydrolytic Enzymes

Zhao¹

2012

Ionic Liquids in Biotransformations and Organocatalysis

View full text Add to dashboard Cite

Cross-linked enzyme aggregates (CLEAs) with controlled particles: Application to Candida rugosa lipase

Cited by 132 publications

References 9 publications

Optimizing the preparation conditions and characterization of a stable and recyclable cross-linked enzyme aggregate (CLEA)-protease

Optimizing the preparation conditions and characterization of a stable and recyclable cross-linked enzyme aggregate (CLEA)-protease

Lipase Immobilization Techniques for Biodiesel Production: An Overview

Ionic Liquids as (Co‐)Solvents for Hydrolytic Enzymes

Contact Info

Product

Resources

About