Biodiesel production using cross-linked Staphylococcus haemolyticus lipase immobilized on solid polymeric carriers

Kim, Sang Hyeon; Kim, Soon-Ja; Park, Seongsoon; Kim, Hyung Kwoun

doi:10.1016/j.molcatb.2012.08.012

Cited by 36 publications

(10 citation statements)

References 31 publications

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“…The first crosslinking strategy was using glutaraldehyde as crosslinking reagent (Kim et al, 2013;Pujari et al, 2006). This small reagent can only work in a massive enzyme molecules intermolecular crosslinking if the immobilized enzyme molecules are really close to each other (Fernandez-Lafuente et al, 1995).…”

Section: Glutaraldehydementioning

confidence: 99%

Immobilization of lipases on hydrophobic supports: immobilization mechanism, advantages, problems, and solutions

Rodrigues

Virgen-Ortíz

Santos

et al. 2019

Biotechnology Advances

468

291

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Lipases are the most widely used enzymes in biocatalysis, and the most utilized method for enzyme immobilization is using hydrophobic supports at low ionic strength. This method allows the one step immobilization, purification, stabilization, and hyperactivation of lipases, and that is the main cause of their popularity. This review focuses on these lipase immobilization supports. First, the advantages of these supports for lipase immobilization will be presented and the likeliest immobilization mechanism (interfacial activation on the support surface) will be revised. Then, its main shortcoming will be discussed: enzyme desorption under certain conditions (such as high temperature, presence of cosolvents or detergent molecules). Methods to overcome this problem include physical or chemical crosslinking of the immobilized enzyme molecules or using heterofunctional supports. Thus, supports containing hydrophobic acyl chain plus epoxy, glutaraldehyde, ionic, vinylsulfone or glyoxyl groups have been designed. This prevents enzyme desorption and improved enzyme stability, but it may have some limitations, that will be discussed and some additional solutions will be proposed (e.g., chemical amination of the enzyme to have a full covalent enzyme-support reaction). These immobilized lipases may be subject to unfolding and refolding strategies to reactivate inactivated enzymes. Finally, these biocatalysts have been used in new strategies for enzyme coimmobilization, where the most stable enzyme could be reutilized after desorption of the least stable one after its inactivation.

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Section: Glutaraldehydementioning

confidence: 99%

Immobilization of lipases on hydrophobic supports: immobilization mechanism, advantages, problems, and solutions

Rodrigues

Virgen-Ortíz

Santos

et al. 2019

Biotechnology Advances

468

291

View full text Add to dashboard Cite

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“…The immobilized enzyme demonstrated high stability for temperature, pH and alcohols. Besides that, for biodiesel production, this enzyme could maintain its conversion yield up to the 10th cycle and thus is suitable for economic biodiesel production …”

Section: Biodiesel Production With Immobilized Lipasementioning

confidence: 99%

Biodiesel production using immobilized lipase: feasibility and challenges

Sankaran

Show

Chang

2016

Biofuels Bioprod Bioref

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Fatty acid alkyl esters (FAAE, also known as biodiesel) is one of the best alternatives to fossil fuels. Biodiesel can be synthesized via transesterification of oil with alcohol by either chemical or enzymatic catalysis. In particular, immobilized lipase as biocatalyst for transesterification has recently drawn great attention due to its environmental and economic benefits over conventional chemical catalytic processes. This paper provides an in‐depth review of the feasibility and the challenges of biodiesel production catalyzed by immobilized lipase, with the emphasis on lipase immobilization techniques, factors affecting biodiesel synthesis, and whole cell catalysis. It is necessary to upgrade the existing methods and to further exploit new techniques to make the immobilized lipase‐catalyzed biodiesel synthesis technically feasible and commercially viable for practical applications. © 2016 Society of Chemical Industry and John Wiley & Sons, Ltd

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“…As reported in Table , Serratia marcescens N3 lipase is used to hydrolyze different kinds of edible oils and shown to exhibit maximum activity with Gingily oil; Serratia marcescens H30 lipase is utilized for efficient kinetic resolution of racemic alcohols in organic solvents; Staphylococcal lipases isolated from facial sebaceous skin found their application as biocatalyst in the cosmetic, medicinal, food, or detergent industries . The bacterial lipases that have shown promising application in biodiesel production are Geobacillus thermodenitrificans AV‐5, cross‐linked Staphylococcus haemolyticus lipase immobilized on solid polymeric carriers, Psuedomonas (P.) fluorescens lipase, Staphylococcus haemolyticus L62 lipase expressed in Escherichia coli cells, Staphylococcus haemolyticus L62 lipase, etc. Further, bacterial lipases can also be effectively utilized in waste management and treatment as demonstrated by elite‐immobilized crude lipase prepared from Staphylococcus pasteuri for pretreatment of coconut mill effluent and by the lipase from P. aeruginosa AAU2 in treating the lipid‐rich industrial effluents …”

Section: Sources Of Lipasesmentioning

confidence: 99%

Recent advances on sources and industrial applications of lipases

Sarmah

Revathi

Sheelu

et al. 2017

Biotechnology Progress

298

165

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Lipases are the industrially important biocatalysts, which are envisioned to have tremendous applications in the manufacture of a wide range of products. Their unique properties such as better stability, selectivity and substrate specificity position them as the most expansively used industrial enzymes. The research on production and applications of lipases is ever growing and there exists a need to have a latest review on the research findings of lipases. The present review aims at giving the latest and broadest overall picture of research and development on lipases by including the current studies and progressions not only in the diverse industrial application fields of lipases, but also with regard to its structure, classification and sources. Also, a special emphasis has been made on the aspects such as process optimization, modeling, and design that are very critical for further scale-up and industrial implementation. The detailed tabulations provided in each section, which are prepared by the exhaustive review of current literature covering the various aspects of lipase including its production and applications along with example case studies, will serve as the comprehensive source of current advancements in lipase research. This review will be very useful for the researchers from both industry as well as academia in promoting lipolysis as the most promising approaches to intensified, greener and sustainable processes. © 2017 American Institute of Chemical Engineers Biotechnol. Prog., 34:5-28, 2018.

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Biodiesel production using cross-linked Staphylococcus haemolyticus lipase immobilized on solid polymeric carriers

Cited by 36 publications

References 31 publications

Immobilization of lipases on hydrophobic supports: immobilization mechanism, advantages, problems, and solutions

Immobilization of lipases on hydrophobic supports: immobilization mechanism, advantages, problems, and solutions

Biodiesel production using immobilized lipase: feasibility and challenges

Recent advances on sources and industrial applications of lipases

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