Isolation and Characterization of Diamine Oxidase Enzyme from Mung Bean Sprouts (Vigna radiata L)

Abdul Karim; Abd Rauf Patong; Abd Wahid Wahab; Indah Raya

doi:doi:10.11648/j.ajbls.20150301.12

| Peer-Reviewed

Isolation and Characterization of Diamine Oxidase Enzyme from Mung Bean Sprouts (Vigna radiata L)

Abdul Karim, Abd Rauf Patong, Abd Wahid Wahab, Indah Raya

Published in American Journal of Biomedical and Life Sciences (Volume 3, Issue 1)

Received: 9 March 2015 Accepted: 22 March 2015 Published: 26 March 2015

Views: Downloads:

Download PDF

Share This Article

Twitter
Linked In
Facebook

Abstract

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.

Published in	American Journal of Biomedical and Life Sciences (Volume 3, Issue 1)
DOI	10.11648/j.ajbls.20150301.12
Page(s)	7-11
Creative Commons	This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.
Copyright	Copyright © The Author(s), 2015. Published by Science Publishing Group

Keywords

Diamine Oxidase, Mung Bean, Fractionation, Ammonium Sulphate

References

[1]	Chang, A., Scheer, M., Grote, A., Schomburg, I., Schomburg, D., 2008, Brenda, Amenda and Frenda the enzyme information system: new content and tools in 2009. Nucleic Acids Res. 37:588–592.
[2]	Choudhary, A., Singh, I. and Sigh, R. P., 1999, A thermostable Diamine Oxidase from Vignaradiata Seedlings. Phytochemistry. 52: 1-5.
[3]	Choudhary, A., Singh, R.P., 2013, Cadmium-induced Changes in Diamine Oxidase Activity and Polyamine Levels in VignaradiataWilczek Seedlings, Journal of Plant Physiology, 156: 704-710
[4]	Gaman, P.M and K.B. Sherrington.(1994). Ilmu Pangan, Pengantar Ilmu Pangan, Nutrisidan Mikrobiologi. Universitas Gadjah Mada press. Yogyakarta.
[5]	Lee, J. M. (1992). Biochemical Engineering.Prentice Hall Inc. New Jersey.
[6]	Medda, R., Padiglia, A. and Floris, G.,1995, Plant Copper amine Oxidases. Phytochemistry. 39: 1-9.
[7]	Mulchandani, A. and Rogers, R., 2001, Enzyme and Microbial Biosensors; Techniques and Protocols, Humana Press Inc., New Jersey
[8]	Mutiah, D., 2005, Ultrafiltrasi, Presipitasi Bertingkat dan Kromatografi Penukar Ion sebagai Tahapan Pemurnian Enzim Protease Bacillus megaterium MS-961, Fakultas Teknologi Pertanian Institut Pertanian Bogor.
[9]	Murray, R.K., Granner, D.K., and Victor, R.W., 2009, Biokimia Harper, EGC Penerbit Buku Kedokteran, Jakarta, 68-69
[10]	Padiglia, A., Cogoni, A.and Floris, G., 1991, Characterization of Amine Oxidases from Pisum, Lens, Lathyrus and Cicer. Phytochemistry. 30: 3895-3897
[11]	RINALDl, A., FLORIS, G.,and FINAZZI, A., 1982, Purification and Properties of Diamine Oxidase from Euphorbia latex, Eur. J. biochem, 127, 417-422
[12]	Suresh, M. R., Ramakrishna, S. and Adiga, P. R., 1976, Diamine Oxidase of Lathyrussativus Seddlings. Phytochemistry. 15: 483-485.
[13]	Wilflingseder, D. and Schwelberger, G., 2000, High Efficient Purification of Porcine Diamine Oxidase.Journal of Chromatography. 737:.161-166.
[14]	Whitaker, R.J., 1994, Principle of Enzymology for the Food Sciences, Mergel Dekker inc, New York.
[15]	Wimmerova. M. and Macholan, L., 1999, Sensitive Amperometric Biosensor for the Determination of Biogenic and Synthetic Amines Using Pea Seedlings Amine Oxidase: A Novel Approach for Enzyme Immobilization. Biosensor and Bioelectronics. 14: 695-702

Cite This Article

Plain Text BibTeX RIS

APA Style

Abdul Karim, Abd Rauf Patong, Abd Wahid Wahab, Indah Raya. (2015). Isolation and Characterization of Diamine Oxidase Enzyme from Mung Bean Sprouts (Vigna radiata L). American Journal of Biomedical and Life Sciences, 3(1), 7-11. https://doi.org/10.11648/j.ajbls.20150301.12

Copy | Download

ACS Style

Abdul Karim; Abd Rauf Patong; Abd Wahid Wahab; Indah Raya. Isolation and Characterization of Diamine Oxidase Enzyme from Mung Bean Sprouts (Vigna radiata L). Am. J. Biomed. Life Sci. 2015, 3(1), 7-11. doi: 10.11648/j.ajbls.20150301.12

Copy | Download

AMA Style

Abdul Karim, Abd Rauf Patong, Abd Wahid Wahab, Indah Raya. Isolation and Characterization of Diamine Oxidase Enzyme from Mung Bean Sprouts (Vigna radiata L). Am J Biomed Life Sci. 2015;3(1):7-11. doi: 10.11648/j.ajbls.20150301.12

Copy | Download

@article{10.11648/j.ajbls.20150301.12,
  author = {Abdul Karim and Abd Rauf Patong and Abd Wahid Wahab and Indah Raya},
  title = {Isolation and Characterization of Diamine Oxidase Enzyme from Mung Bean Sprouts (Vigna radiata L)},
  journal = {American Journal of Biomedical and Life Sciences},
  volume = {3},
  number = {1},
  pages = {7-11},
  doi = {10.11648/j.ajbls.20150301.12},
  url = {https://doi.org/10.11648/j.ajbls.20150301.12},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ajbls.20150301.12},
  abstract = {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.},
 year = {2015}
}

Copy | Download

TY  - JOUR
T1  - Isolation and Characterization of Diamine Oxidase Enzyme from Mung Bean Sprouts (Vigna radiata L)
AU  - Abdul Karim
AU  - Abd Rauf Patong
AU  - Abd Wahid Wahab
AU  - Indah Raya
Y1  - 2015/03/26
PY  - 2015
N1  - https://doi.org/10.11648/j.ajbls.20150301.12
DO  - 10.11648/j.ajbls.20150301.12
T2  - American Journal of Biomedical and Life Sciences
JF  - American Journal of Biomedical and Life Sciences
JO  - American Journal of Biomedical and Life Sciences
SP  - 7
EP  - 11
PB  - Science Publishing Group
SN  - 2330-880X
UR  - https://doi.org/10.11648/j.ajbls.20150301.12
AB  - 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.
VL  - 3
IS  - 1
ER  -

Copy | Download

Author Information

Abdul Karim

Laboratory of Biochemistry, Chemistry Department, Mathematic and Natural Science Faculty, Hasanuddin Univesity, Makassar, Indonesia
Abd Rauf Patong

Laboratory of Biochemistry, Chemistry Department, Mathematic and Natural Science Faculty, Hasanuddin Univesity, Makassar, Indonesia
Abd Wahid Wahab

Laboratory of Analytic chemistry, Chemistry Department, Mathematic and Natural Science Faculty, Hasanuddin Univesity, Makassar, Indonesia
Indah Raya

Laboratory of Inorganic chemistry, Chemistry Department, Mathematic and Natural Science Faculty, Hasanuddin Univesity, Makassar, Indonesia

Download PDF

Sections

Plain Text BibTeX RIS

APA Style

Abdul Karim, Abd Rauf Patong, Abd Wahid Wahab, Indah Raya. (2015). Isolation and Characterization of Diamine Oxidase Enzyme from Mung Bean Sprouts (Vigna radiata L). American Journal of Biomedical and Life Sciences, 3(1), 7-11. https://doi.org/10.11648/j.ajbls.20150301.12

Copy | Download

ACS Style

Abdul Karim; Abd Rauf Patong; Abd Wahid Wahab; Indah Raya. Isolation and Characterization of Diamine Oxidase Enzyme from Mung Bean Sprouts (Vigna radiata L). Am. J. Biomed. Life Sci. 2015, 3(1), 7-11. doi: 10.11648/j.ajbls.20150301.12

Copy | Download

AMA Style

Abdul Karim, Abd Rauf Patong, Abd Wahid Wahab, Indah Raya. Isolation and Characterization of Diamine Oxidase Enzyme from Mung Bean Sprouts (Vigna radiata L). Am J Biomed Life Sci. 2015;3(1):7-11. doi: 10.11648/j.ajbls.20150301.12

Copy | Download

@article{10.11648/j.ajbls.20150301.12,
  author = {Abdul Karim and Abd Rauf Patong and Abd Wahid Wahab and Indah Raya},
  title = {Isolation and Characterization of Diamine Oxidase Enzyme from Mung Bean Sprouts (Vigna radiata L)},
  journal = {American Journal of Biomedical and Life Sciences},
  volume = {3},
  number = {1},
  pages = {7-11},
  doi = {10.11648/j.ajbls.20150301.12},
  url = {https://doi.org/10.11648/j.ajbls.20150301.12},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ajbls.20150301.12},
  abstract = {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.},
 year = {2015}
}

Copy | Download

TY  - JOUR
T1  - Isolation and Characterization of Diamine Oxidase Enzyme from Mung Bean Sprouts (Vigna radiata L)
AU  - Abdul Karim
AU  - Abd Rauf Patong
AU  - Abd Wahid Wahab
AU  - Indah Raya
Y1  - 2015/03/26
PY  - 2015
N1  - https://doi.org/10.11648/j.ajbls.20150301.12
DO  - 10.11648/j.ajbls.20150301.12
T2  - American Journal of Biomedical and Life Sciences
JF  - American Journal of Biomedical and Life Sciences
JO  - American Journal of Biomedical and Life Sciences
SP  - 7
EP  - 11
PB  - Science Publishing Group
SN  - 2330-880X
UR  - https://doi.org/10.11648/j.ajbls.20150301.12
AB  - 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.
VL  - 3
IS  - 1
ER  -

Copy | Download