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Chusnul Hidayat
Graduate Program on Estate Crop Product Technology, Faculty of Agricultural Technology, Universitas Gadjah Mada, Jl. Flora, Bulaksumur, Yogyakarta 55281
Chemical Engineering, Chemistry & Bioengineering Chemistry

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Enzymatic Phorbol Esters Degradation using the Germinated Jatropha Curcas Seed Lipase as Biocatalyst: Optimization Process Conditions by Response Surface Methodology Avita Kusuma Wardhani; Chusnul Hidayat; Pudji Hastuti
Bulletin of Chemical Reaction Engineering & Catalysis 2016: BCREC Volume 11 Issue 3 Year 2016 (December 2016)
Publisher : Department of Chemical Engineering - Diponegoro University

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (468.334 KB) | DOI: 10.9767/bcrec.11.3.574.346-353

Abstract

Utilization of Jatropha curcas seed cake is limited by the presence of phorbol esters (PE), which are the main toxic compound and heat stable. The objective of this research was to optimize the reaction conditions of the enzymatic PE degradation of the defatted Jatropha curcas seed cake (DJSC) using the acetone-dried lipase from the germinated Jatropha curcas seeds as a biocatalyst. Response Surface Methodology (RSM) using three-factors-three-levels Box-Behnken design was used to evaluate the effects of the reaction time, the ratio of buffer volume to DJSC, and the ratio of enzyme to DJSC on PE degradation. The results showed that the optimum conditions of PE degradation were 29.33 h, 51.11 : 6 (mL/g), and 30.10 : 5 (U/g cake) for the reaction time, the ratio of buffer volume to DJSC, and the ratio of enzyme to DJSC, respectively. The predicted degradation of PE was 98.96% and not significantly different with the validated data of PE degradation. PE content was 0.035 mg/g, in which it was lower than PE in non-toxic Jatropha seeds. The results indicated that enzymatic degradation of PE might be a promising method for degradation of PE. 
Surface Modification of Macroporous Matrix for Immobilization of Lipase for Fructose Oleic Ester Synthesis Hani Hilmanto; Chusnul Hidayat; Pudji Hastuti
Bulletin of Chemical Reaction Engineering & Catalysis 2016: BCREC Volume 11 Issue 3 Year 2016 (December 2016)
Publisher : Department of Chemical Engineering - Diponegoro University

Show Abstract | Download Original | Original Source | Check in Google Scholar | Full PDF (512.846 KB) | DOI: 10.9767/bcrec.11.3.573.339-345

Abstract

The objective of this research was to modify the matrix surfaces to obtain both hydrophobic matrix (HM) and hydrophilic-hydrophobic matrix (HHM) for enzymatic synthesis of fructose oleic ester (FOE). The modification was performed by the attachment of 2-phenylpropionaldehyde (PPA) and PPA followed by polyethyleneimine (PEI) for HM and HHM, respectively. The results from FT-IR analysis showed that the peak of stretching vibration of NH2 bond decreased and it was followed by an increase of the peak vibration of –C=N– bond at wave number 1667 cm-1. The peak of bending vibrations of the C=C bond also increased. It indicated that PPA was successfully attached on matrix. For HHM, an increase in the peak area of NH2 bond indicated that PEI was also successfully attached on the matrix. The optimum conditions of lipase adsorption were obtained at buffer pH 7 containing 0.5 M NaCl (9.27 mg protein/g matrix) and without NaCl (9.23 mg protein/g matrix) for HM and HHM, respectively. For FOE synthesis, the best immobilized lipase concentration was about 8% and 6% for HM and HHM, respectively. The optimum time of esterification was 24 h and 18 h for HM and HHM, respectively, in which the yields were 75.96% and 85.29%, respectively. The immobilized lipase could be used up to 3 cycles of esterification reaction. 
Surface Modification of Macroporous Matrix for Immobilization of Lipase for Fructose Oleic Ester Synthesis Hani Hilmanto; Chusnul Hidayat; Pudji Hastuti
Bulletin of Chemical Reaction Engineering & Catalysis 2016: BCREC Volume 11 Issue 3 Year 2016 (December 2016)
Publisher : Masyarakat Katalis Indonesia - Indonesian Catalyst Society (MKICS)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.9767/bcrec.11.3.573.339-345

Abstract

The objective of this research was to modify the matrix surfaces to obtain both hydrophobic matrix (HM) and hydrophilic-hydrophobic matrix (HHM) for enzymatic synthesis of fructose oleic ester (FOE). The modification was performed by the attachment of 2-phenylpropionaldehyde (PPA) and PPA followed by polyethyleneimine (PEI) for HM and HHM, respectively. The results from FT-IR analysis showed that the peak of stretching vibration of NH2 bond decreased and it was followed by an increase of the peak vibration of –C=N– bond at wave number 1667 cm-1. The peak of bending vibrations of the C=C bond also increased. It indicated that PPA was successfully attached on matrix. For HHM, an increase in the peak area of NH2 bond indicated that PEI was also successfully attached on the matrix. The optimum conditions of lipase adsorption were obtained at buffer pH 7 containing 0.5 M NaCl (9.27 mg protein/g matrix) and without NaCl (9.23 mg protein/g matrix) for HM and HHM, respectively. For FOE synthesis, the best immobilized lipase concentration was about 8% and 6% for HM and HHM, respectively. The optimum time of esterification was 24 h and 18 h for HM and HHM, respectively, in which the yields were 75.96% and 85.29%, respectively. The immobilized lipase could be used up to 3 cycles of esterification reaction. 
Enzymatic Phorbol Esters Degradation using the Germinated Jatropha Curcas Seed Lipase as Biocatalyst: Optimization Process Conditions by Response Surface Methodology Avita Kusuma Wardhani; Chusnul Hidayat; Pudji Hastuti
Bulletin of Chemical Reaction Engineering & Catalysis 2016: BCREC Volume 11 Issue 3 Year 2016 (December 2016)
Publisher : Masyarakat Katalis Indonesia - Indonesian Catalyst Society (MKICS)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.9767/bcrec.11.3.574.346-353

Abstract

Utilization of Jatropha curcas seed cake is limited by the presence of phorbol esters (PE), which are the main toxic compound and heat stable. The objective of this research was to optimize the reaction conditions of the enzymatic PE degradation of the defatted Jatropha curcas seed cake (DJSC) using the acetone-dried lipase from the germinated Jatropha curcas seeds as a biocatalyst. Response Surface Methodology (RSM) using three-factors-three-levels Box-Behnken design was used to evaluate the effects of the reaction time, the ratio of buffer volume to DJSC, and the ratio of enzyme to DJSC on PE degradation. The results showed that the optimum conditions of PE degradation were 29.33 h, 51.11 : 6 (mL/g), and 30.10 : 5 (U/g cake) for the reaction time, the ratio of buffer volume to DJSC, and the ratio of enzyme to DJSC, respectively. The predicted degradation of PE was 98.96% and not significantly different with the validated data of PE degradation. PE content was 0.035 mg/g, in which it was lower than PE in non-toxic Jatropha seeds. The results indicated that enzymatic degradation of PE might be a promising method for degradation of PE. 
Co-Authors Avita Kusuma Wardhani Hani Hilmanto Pudji Hastuti