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Judul Isolation and Characterization of Diamine Oxidase Enzyme from Mung Bean Sprouts (Vigna radiata L)
Pengarang Abdul Karim
Abd Rauf Patong
Abd Wahid Wahab
Indah Raya
EDISI American Journal of Biomedical and Life Sciences
Penerbitan 2018
Deskripsi Fisik 5 hlm.
Subjek Diamine Oxidase
Mung Bean
Fractionation
Ammonium Sulphate
Abstrak The diamine oxidase enzyme (DAO) can be isolated from mung bean sprouts (Vigna radiata L) through the process of extraction in phosphate buffer. Concentration and fractionation were performed by the addition of ammonium sulphate, (NH4)2SO4 saturation in stages and cold centrifuged at 10000 rpm. Enzyme activity of DAO crude and DAO fractionation results were tested using substrat histamin and measured with a spectrophotometer at a wavelength of 450 nm. This study revealed that the enzyme activity of the crude enzyme was1, 226 mU/mL, the fraction of 40-60% ammonium sulphate saturated had the highest activity which accounted for 3326 mU/mL and after gel filtration, the results for both activity and specific activity were 116 mU/mL and 185 mU/mg protein.
Bahasa Inggris
Bentuk Karya Bukan fiksi atau tidak didefinisikan
Target Pembaca Tidak diketahui / tidak ditentukan

 
No Barcode No. Panggil Akses Lokasi Ketersediaan
Tag Ind1 Ind2 Isi
001 INLIS000000000044806
005 20181204072442
007 ta
008 181204###########################0#eng##
035 # # $a 0010-1218000044
100 0 # $a Abdul Karim
245 1 # $a Isolation and Characterization of Diamine Oxidase Enzyme from Mung Bean Sprouts (Vigna radiata L)
250 # # $a American Journal of Biomedical and Life Sciences
260 # # ,$c 2018
300 # # $a 5 hlm.
520 # # $a The diamine oxidase enzyme (DAO) can be isolated from mung bean sprouts (Vigna radiata L) through the process of extraction in phosphate buffer. Concentration and fractionation were performed by the addition of ammonium sulphate, (NH4)2SO4 saturation in stages and cold centrifuged at 10000 rpm. Enzyme activity of DAO crude and DAO fractionation results were tested using substrat histamin and measured with a spectrophotometer at a wavelength of 450 nm. This study revealed that the enzyme activity of the crude enzyme was1, 226 mU/mL, the fraction of 40-60% ammonium sulphate saturated had the highest activity which accounted for 3326 mU/mL and after gel filtration, the results for both activity and specific activity were 116 mU/mL and 185 mU/mg protein.
650 # # $a Ammonium Sulphate
650 # # $a Diamine Oxidase
650 # # $a Fractionation
650 # # $a Mung Bean
700 0 # $a Abd Rauf Patong
700 0 # $a Abd Wahid Wahab
700 0 # $a Indah Raya
No Nama File Nama File Format Flash Format File Action
1 JURNAL ROMANIA.pdf pdf Baca Online
2 AJBLS-jurnal Abdul Karim- enzim DAO_001.pdf pdf Baca Online
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