Immobilization of<i>Candida rugosa</i>lipase by cross-linking with glutaraldehyde followed by entrapment in alginate beads

Wu, Jin; Selvam, Vicknesh; Teo, Hui Hui; Chow, Yvonne; Talukder, Md. Mahabubur Rahman; Choi, Won Jae

doi:10.1080/10242420600787326

Cited by 19 publications

(2 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Nonetheless, the practical application of entrapment is limited because of the requirements, like small substrate size and delicate balance between physical properties of the matrix and enzymatic activity [43]. Insufficient substrate interaction and leakage of enzymes due to continuous use are major disadvantages of the entrapment method [67].…”

Section: Entrapment and Encapsulationmentioning

confidence: 99%

“…It was reported that entrapment of Candida lipase prior to its co-adsorption with lipase-activating chemical additives not only protected the enzyme from desorption, but also was a cheaper and more efficient method of biodiesel production from waste cooking oil, compared to immobilization methods described in previous studies [57]. Combination of enzyme cross-linking prior to entrapment in sol-gel beads was determined to be a viable technique for stabilizing enzymes in glucose biosensors [67]. In some cases, filtration-enabled reusability of CLEAs may be problematic due to similar size of the particles and the substrate.…”

Section: Combinatory Physicochemical Approachesmentioning

confidence: 99%

See 1 more Smart Citation

Biocatalysis and Strategies for Enzyme Improvement

Osbon¹,

Kumar²

2020

Biophysical Chemistry - Advance Applications

View full text Add to dashboard Cite

Biotransformation with the help of enzymes can greatly improve the rate and stereospecificity of reactions in organic chemistry. However, the use of organic solvents and harsh conditions in biotechnological applications often correlates with enzyme deactivation or a dramatic drop in catalytic activity. Detailed molecular understanding of the protein structure and conformational dynamics allows us to address such limitations and to finely tune catalytic activity by modifying the solvent, the support, or the active site of the enzyme. Along with physico-chemical methods of enzyme stabilization, such as additive approach, chemical modification, and immobilization of enzymes, approaches of enzyme engineering based on DNA recombination can be used to enhance the performance of biocatalysts. Since successful synthetic and industrial applications of biocatalysts require systems that are not only stable and active, but can also be reused in a continuous flow process reducing the production cost, the goal of this chapter is to introduce the reader to the vast scope of techniques available for enzyme improvement, highlighting their opportunities and limitations for the real-world technological processes.

show abstract

Section: Entrapment and Encapsulationmentioning

confidence: 99%

Section: Combinatory Physicochemical Approachesmentioning

confidence: 99%

Biocatalysis and Strategies for Enzyme Improvement

Osbon¹,

Kumar²

2020

Biophysical Chemistry - Advance Applications

View full text Add to dashboard Cite

show abstract

Coupling Chemical Modification and Immobilization to Improve the Catalytic Performance of Enzymes

Rodrigues¹,

2011

View full text Add to dashboard Cite

Chemical modification and immobilization of enzymes have been usually considered unrelated tools to improve biocatalyst features. However, there are many examples where a chemically modified enzyme is finally used in an immobilized form, and that exemplifies how both tools may be complementary resulting in a synergism in the final results. In this review we present some of the strategies that may give that result. For example, the chemical modification of soluble enzymes may be used to improve their immobilization (reinforcing adsorption or improving multipoint covalent attachment), or just to improve enzyme stability and facilitate the selection of the immobilization conditions. Chemical modification of previously immobilized enzymes benefits from solid-phase chemistry due to the nature of enzymes (e.g., prevention of inactivation, aggregation, etc.). The use of different targets for chemical modifications with small molecules or multifunctional polymers are also discussed: intramolecular or intersubunit cross-linking, one-point modification, generation of artificial microenvironments, etc.

show abstract

Current awareness on yeast

2007

Yeast

View full text Add to dashboard Cite

In order to keep subscribers up‐to‐date with the latest developments in their field, this current awareness service is provided by John Wiley & Sons and contains newly‐published material on yeasts. Each bibliography is divided into 10 sections. 1 Reviews; 2 General; 3 Biochemistry; 4 Biotechnology; 5 Cell Biology; 6 Gene Expression; 7 Genetics; 8 Physiology; 9 Medical Mycology; 10 Recombinant DNA Technology. Within each section, articles are listed in alphabetical order with respect to author. If, in the preceding period, no publications are located relevant to any one of these headings, that section will be omitted. (4 weeks journals ‐ search completed 4th. Apr. 2007)

show abstract

Immobilization ofCandida rugosalipase by cross-linking with glutaraldehyde followed by entrapment in alginate beads

Cited by 19 publications

References 21 publications

Biocatalysis and Strategies for Enzyme Improvement

Biocatalysis and Strategies for Enzyme Improvement

Coupling Chemical Modification and Immobilization to Improve the Catalytic Performance of Enzymes

Current awareness on yeast

Contact Info

Product

Resources

About