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Online Journal of Veterinary Research©

(Including Medical and Laboratory Research)

Established 1994
ISSN 1328-925X


Volume 27 (3): 146-155, 2023.

Cibacron nanoparticles for rumen fluid α–amylase.


Nosrat Allah Ghazvini1, Mohammad Chamani1, Homayon Ahmad Panahi2, Ali Asghar Sadeghi1 , Mehdi Aminafshar1


1Department(s) of Animal Science, 2Chemistry, Faculty of Agriculture and Natural Resources, Tehran Science and Research Branch, Islamic Azad University, Tehran, Iran.




Ghazvini NA, Chamani M, Panahi HA, Sadeghi AA,  Aminafshar M., Cibacron nanoparticles for rumen fluid α–amylase, Onl J Vet Res., 27 (3): 146-155, 2023. Clarified rumen fluid was utilized to obtain α-amylase by using magnetic nano-particles (MNPs) grafted with allyl 2,3epoxypropyl ether and Cibacron blue, a ligand for capturing the enzyme. Characteristics of particles were analyzed by thermogravy, transmission electron microscopy and Fourier transform infrared spectroscopy. Ruminal derived α-amylase was then adsorbed by modifying temperature, pH, and shaking. Transmission electron microscopy revealed spherical 20-80 nm diameter particle. By  Fourier transform in controls we detected peaks at 569 cm-1 due to Fe-O whereas in coated particles we found extra peaks at 2138, 1726, 1436, 1145, and 1240 cm-1 due to aliphatic C-H, C=O, CH2, Si-O, and C-O respectively. By thermography losses due to evaporation for controls reached 2.708% and coated particles 3.254% at 266°C. Compared with fresh amylase, we found no reduction after defrosting. Most retention occurred at pH 7, 24°C, and 10 min shaking whereas optimal desorption occurred in 0.5 M NaCl and 90min shaking (p<0.05). Purified enzymes had suitable activity.


Keywords: Amylase; magnetic nanoparticles; rumen fluid; adsorption; desorption.