Evaluation of diatomaceous earth as a support for sol–gel immobilized lipase for transesterification

Meunier, Sarah M.; Legge, Raymond L.

doi:10.1016/j.molcatb.2009.09.002

Cited by 37 publications

(20 citation statements)

References 27 publications

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“…There are several materials that may be used as supports for enzyme immobilization, or rather, natural materials such as alginate (ELLAIAH et al, 2004), agar (LI et al, 2008) and agarose (RODRIGUES et al, 2008); synthetic ones, such as nylon (PAHUJANI et al, 2008), polyacrylamide (ELLAIAH et al, 2004); inorganic ones, such as silica (CRUZ et al, 2009;YANG et al, 2010) and glass (KAHRAMAN et al, 2007) and others. Among the methodologies used to obtain silica, the supports produced by sol-gel technique are known as hydrophobic matrices (MEUNIER;LEGGE, 2010).…”

Section: Introductionmentioning

confidence: 99%

“…Compared to other immobilization processes, the advantages of lipases' immobilization in sol-gel matrices comprise higher thermal and chemical stability and higher hydrolytic activity of the biocatalyst (MEUNIER; LEGGE, 2010). Several researchers have immobilized microbial lipases in silica matrices obtained with solgel technique (MEUNIER;LEGGE, 2010;SIMÕES et al, 2011;SOARES et al, 2004b;UYANIK et al, 2011). Current study investigated the immobilization of lipase from Aspergillus niger (obtained from SSF pumpkin seed flour) in sol-gel matrix and also the enzyme's biochemical characterization in free and immobilized form.…”

Section: Introductionmentioning

confidence: 99%

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<b>Microbial lipase obtained from the fermentation of pumpkin seeds: immobilization potential of hydrophobic matrices<b>

et al. 2014

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ABSTRACT. Immobilization potential of lipase from Aspergillus niger on sol-gel matrix was evaluated by physical adsorption and covalent binding and the biochemical characterization of free and immobilized enzyme was performed. Lipase was produced by solid state fermentation of pumpkin seed flour with 30% moisture, at 30°C for 120h. The enzyme was pre-purified with ammonium sulfate and immobilized in the sol-gel matrix by covalent attachment and physical adsorption. A higher yield of immobilization (81.88%) was obtained in the latter. The free enzyme presented higher hydrolytic activity with pH 4.0, at 37°C; moreover, it was more stable with pH between 6.0 and 7.0, at 35°C. The immobilized lipase showed maximum hydrolytic activity with pH 11.0, at 50°C; it was more stable with pH 11.0, at 37°C. Parameters K m and V max were best determined by Hanes-Woolf linearization.Keywords: enzyme, sol-gel, agroindustrial residue.Lipase microbiana obtida pela fermentação de sementes de abóbora: potencial de imobilização em matrizes hidrofóbicas RESUMO. O objetivo deste trabalho foi avaliar o potencial de imobilização da lipase de Aspergillus niger em sílica por adsorção física e ligação covalente, e realizar a caracterização bioquímica da mesma na forma livre e imobilizada. A lipase foi produzida por fermentação em estado sólido da farinha de sementes de abóbora, contendo 30% de umidade, à temperatura de 30°C em 120h. A seguir, a enzima foi pré-purificada com sulfato de amônio e imobilizada em matriz sol-gel por ligação covalente e adsorção física, obtendo-se nesta última maior rendimento de imobilização (81,88%). A enzima livre apresentou maior atividade hidrolítica em pH 4,0 a 37°C, sendo mais estável em valores de pH entre 6,0 e 7,0 e temperatura de 35°C. A lipase imobilizada por adsorção física apresentou máxima atividade hidrolítica em pH 11,0 e temperatura de 50°C sendo mais estável em pH 11,0 e temperatura de 37°C. Os parâmetros K m e V máx foram melhor determinados pela linearização de Hanes-Woolf.Palavras-chave: enzima, sol-gel, resíduo agroindustrial.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

<b>Microbial lipase obtained from the fermentation of pumpkin seeds: immobilization potential of hydrophobic matrices<b>

et al. 2014

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“…Adsorption of protein to the surface of a carrier is, in principle, reversible, but careful selection of the carrier material and the immobilization conditions can render desorption negligible. Entrapment of enzyme in a cross-linking polymer is accomplished by carrying out the polymerization reaction in the presence of enzyme; the enzyme becomes trapped in interstitial spaces in the polymer matrices (Winayanuwattikun et al 2005, Yagiz et al 2007, Meunier and Legge 2010. Encapsulation of enzymes results in regions of high enzyme concentration is being separated from the bulk solvent system by a semi-permeable membrane, through which substrate, but not enzyme, may diffuse (Li et al 2011).…”

Section: Immobilized Lipase In Support Materialsmentioning

confidence: 99%

“…Immobilization is studied using covalent bonding, cross-linking, entrapment, adsorption, and encapsulation. Selection of an immobilization strategy greatly influences the properties of biocatalyst (Iso et al 2001, Yagiz et al 2007, Meunier et al 2010, Xie and Ma 2010.…”

Section: Introductionmentioning

confidence: 99%

Trend in enzyme immobilization on nano materials for transesterification to produce biodiesel: A review

Hindryawati¹,

Maniam²,

Feng³

et al. 2018

J bio-sci.

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Biodiesel is a non-toxic and very low sulfur containing, renewable and biodegradable diesel fuel substitute with low volatility and high cetane number. It is derived from fresh or waste vegetable oils and animal fats transesterified with short chain alcohol such as ethanol or methanol in the presence of a catalyst. Several new types of carriers and technologies have been adopted in the recent past to improve the ability of a catalyst in transesterification. One of the new trends is nanoparticles-based immobilization of enzyme as a catalyst. The combination of the precise physical, chemical, optical and electrical properties of nanoparticles with the specific recognition site or catalytic properties has led them to appear in a myriad of novel nanomaterial application. Enzyme immobilized on nanoparticles showed a broader working temperature and pH range and thermal stability than the native enzyme. Enhancement in the reactivity of nanocatalysts is associated with their increased surface area, greater concentrations of highly reactive edge, unusual and stabilized lattice planes. The greater activity of nanomaterial immobilized biocatalyst affords operational simplicity, low energy consumption, and greater safety, in the process of transesterification. This review article highlights the issues including the exploration of the ability of nanomaterial to immobilize biocatalyst and factors that influence the activity of biocatalysts upon immobilization.

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“…Various supports could be used to improve the stability of the entrapped/encapsulated enzymes. Celite supported lipase sol-gels were investigated aiming such problems as www.intechopen.com activity, stability and reusability of the enzyme (Meunier & Legge, 2010). The three types of Celite considered (R633, R632, and R647) were compared to unsupported lipase sol-gels.…”

Section: Lipases Immobilization By Adsorptionmentioning

confidence: 99%

The Immobilized Lipases in Biodiesel Production

Stoytcheva¹,

Montero²,

Toscano³

et al. 2011

Biodiesel - Feedstocks and Processing Technologies

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Evaluation of diatomaceous earth as a support for sol–gel immobilized lipase for transesterification

Cited by 37 publications

References 27 publications

<b>Microbial lipase obtained from the fermentation of pumpkin seeds: immobilization potential of hydrophobic matrices<b>

<b>Microbial lipase obtained from the fermentation of pumpkin seeds: immobilization potential of hydrophobic matrices<b>

Trend in enzyme immobilization on nano materials for transesterification to produce biodiesel: A review

The Immobilized Lipases in Biodiesel Production

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