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All Journal Chemistry Indonesian Journal of Chemical Research
Rusman, Hendra J.
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Biochemistry, Genetics & Molecular Biology Chemistry Engineering Environmental Science

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Produksi DAG Dari Virgin Coconut Oil (VCO) Melalui Reaksi Trans-Esterifikasi Menggunakan Enzim Lipase Dedak Padi (Oryza Sativa L.) Spesifik C18-20 Terimobilisasi Karbon Aktif Sebagai Biokatalis Dali, Seniwati; Firdaus, Firdaus; Rusman, Hendra J.
Indonesian Journal of Chemical Research Vol 5 No 1 (2017): Edisi Bulan Juli (Edition For July)
Publisher : Jurusan Kimia, Fakultas Sains dan Teknologi, Universitas Pattimura

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.30598/ijcr.2017.5-sen

Abstract

This research aims to produce DAG of the VCO through the substrate reaction of trans-esterification using lipase enzymes specifically C18-20 from rice bran (Oryza Sativa L.) immobiled of activated carbon as a catalyst. Phases of this research starts with the enzyme lipase do immobile using activated carbon; next enzymes of immobile used to produce DAG through the trans-esterification reaction using a VCO as a substrate and methanol as ko-substrate; DAG and methyl ester produced identified using FTIR instrument and GC-MS instruments. The results showed that there were three compounds DAG and three compound methyl ester produced trans-esterification reaction, namely (1) 1-laurin, 3-heksanoin esters of glycerol; (2) 2-laurin, 3-oktanoin esters of glycerol; (3) 1-laurin, 3-heksanoin esters of glycerol; (4) methyl ester oleic; (5) methyl ester stearic acids; and (6) methyl ester arachidat.
Imobilisasi Enzim Lipase Dedak Padi (Oryza Sativa L.) Pada Karbon Aktif: Karakterisasi, dan Uji Stabilitas Kerja Enzim Imobil Firdaus, Firdaus; Dali, Seniwati; Rusman, Hendra J.
Indonesian Journal of Chemical Research Vol 5 No 1 (2017): Edisi Bulan Juli (Edition For July)
Publisher : Jurusan Kimia, Fakultas Sains dan Teknologi, Universitas Pattimura

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.30598/ijcr.2017.5-fir

Abstract

This research aims to immobilization; characterize the enzyme of immobilized, test the effectiveness of the enzyme of immobilized. This research begins with the immobilization to process of enzyme lipase using activated carbon matrix, enzyme characterization covering of immobile determination of temperature and pH optimum of the enzyme of immobilized, as well as test the stability of work covering immobilized of enzyme the test thermal stability and repeated use. The results showed that the immobile of enzyme work optimally at 50oC of temperature and pH 6.5 with each activity 0.040 U/mL; research results also showed that the immobile of enzyme has higher thermal stability in comparison with the free enzyme: with the relative activity of 57.50% at the time of 45 minutes of exposure and the exposure time at 47.50% at 75-105 minutes and it can be used as many as six times with the relative activity of 52.5% in 6 times of use.
Co-Authors Firdaus Firdaus Seniwati Dali