Effect of temperature and mixing speed on immobilization of crude enzyme from Aspergillus niger on chitosan for hydrolyzing cellulose

Hamzah, Afan; Kumala, P Gek Ela; Ramadhani, Dwi; Maziyah, Nurul; Rahmah, Laila Nur; Soeprijanto, Soeprijanto; Widjaja, Arief

doi:10.1063/1.4982266

Cited by 3 publications

(3 citation statements)

References 6 publications

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“…Another important factor influencing the expressed activity of immobilized enzymes is rotation speed, where high rotation speed preferably results in higher expressed activity, since the bond between epoxy-activated MNPs and the enzyme is stronger and therefore more successful, as it allows more contact between the enzyme and the support 109 . When optimizing the rotation speed of immobilization, the same conditions were used as those for activation of CMD-MNPs, which were 4% (v/v) of EClH with a sodium phosphate buffer (pH 7.5) and a duration of 1 h at 300 rpm and 20 °C.…”

Section: Resultsmentioning

confidence: 99%

Immobilization of alcohol dehydrogenase from Saccharomyces cerevisiae onto carboxymethyl dextran-coated magnetic nanoparticles: a novel route for biocatalyst improvement via epoxy activation

Vasić

Knez

Leitgeb

2020

Sci Rep

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A novel method is described for the immobilization of alcohol dehydrogenase (ADH) from Saccharomyces cerevisiae onto carboxymethyl dextran (CMD) coated magnetic nanoparticles (CMD-MNPs) activated with epoxy groups, using epichlorohydrin (EClH). EClH was used as an activating agent to bind ADH molecules on the surface of CMD-MNPs. Optimal immobilization conditions (activating agent concentration, temperature, rotation speed, medium pH, immobilization time and enzyme concentration) were set to obtain the highest expressed activity of the immobilized enzyme. ADH that was immobilized onto epoxy-activated CMD-MNPs (ADH-CMD-MNPs) maintained 90% of the expressed activity. Thermal stability of ADH-CMD-MNPS after 24 h at 20 °C and 40 °C yielded 79% and 80% of initial activity, respectively, while soluble enzyme activity was only 19% at 20 °C and the enzyme was non-active at 40 °C. Expressed activity of ADH-CMD-MNPs after 21 days of storage at 4 °C was 75%. Kinetic parameters (KM, vmax) of soluble and immobilized ADH were determined, resulting in 125 mM and 1.2 µmol/min for soluble ADH, and in 73 mM and 4.7 µmol/min for immobilized ADH.

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Section: Resultsmentioning

confidence: 99%

Immobilization of alcohol dehydrogenase from Saccharomyces cerevisiae onto carboxymethyl dextran-coated magnetic nanoparticles: a novel route for biocatalyst improvement via epoxy activation

Vasić

Knez

Leitgeb

2020

Sci Rep

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“…While in the saccharification process, the substrates were almost completely converted (Lyu et al, 2021). The enzymatic hydrolysis was selected in this study due to its high selectivity, produce higher yield, and able to operate in various conditions (Hamzah et al, 2017…”

Section: 1enzymatic Hydrolysismentioning

confidence: 99%

“…The enzymatic hydrolysis was used in this study due to its high selectivity, produce higher yield, and able to operate under various conditions (Hamzah et al, 2017.…”

Section: The Yield Of Reducing Sugar From Enzymatic Hydrolysismentioning

confidence: 99%

Bioconversion of Industrial Cassava Solid Waste (Onggok) to Bioethanol Using a Saccharification and Fermentation process

Soeprijanto

Qomariyah

Hamzah

et al. 2021

Int. J. Renew. Energy Dev.

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Cassava solid waste (Onggok) is a by-product of the starch industry containing a lot of fiber, especially cellulose and hemicellulose. It has the potential to be converted to bioethanol. This work aimed to evaluate the effect of feedstocks ratio for the optimal bioethanol production via enzymatic and acidic hydrolysis process in a batch fermentation process. The effect of alpha-amylase and glucoamylase activities was studied. The sulfuric acid concentrations in the hydrolysis process in converting cassava into reducing sugar were also investigated. The reducing sugar was then fermented to produce ethanol. Enzymatic and chemical hydrolysis was carried out with the ratio of onggok(g)/water(L), 50/1, 75/1, and 100/1 (w/v). In the enzymatic hydrolysis, 22.5, 45, and 67.5 KNU (Kilo Novo alpha-amylase Unit) for liquefaction; and 65, 130, and 195 GAU (Glucoamylase Unit) for saccharification, respectively of enzymes were applied. The liquefaction was carried out at 90-100⁰C for 2 hours. The saccharification was executed at 65 ⁰C for 4 hours. Meanwhile, the acidic hydrolysis operating condition was at 90-100 ⁰C for 3 hours. The fermentation was performed at pH 4.5 for 3 days. Fourier Transform Infra-Red (FTIR) analysis was conducted to evaluate the hydrolysis process. The highest ethanol was yielded in the fermentation at 8.89% with the ratio of onggok to water 100:1, 67.5 KNU of alpha-amylase, and 195 GAU of glucoamylase. Ethanol was further purified utilizing fractional distillation. The final ethanol concentration was at 93-94%.

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A mild oxidation strategy for oxidation-hydrolysis of cellulose without additional catalyst

Zhou

Han

et al. 2022

Biomass Conv. Bioref.

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Effect of temperature and mixing speed on immobilization of crude enzyme from Aspergillus niger on chitosan for hydrolyzing cellulose

Cited by 3 publications

References 6 publications

Immobilization of alcohol dehydrogenase from Saccharomyces cerevisiae onto carboxymethyl dextran-coated magnetic nanoparticles: a novel route for biocatalyst improvement via epoxy activation

Immobilization of alcohol dehydrogenase from Saccharomyces cerevisiae onto carboxymethyl dextran-coated magnetic nanoparticles: a novel route for biocatalyst improvement via epoxy activation

Bioconversion of Industrial Cassava Solid Waste (Onggok) to Bioethanol Using a Saccharification and Fermentation process

A mild oxidation strategy for oxidation-hydrolysis of cellulose without additional catalyst

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