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OJVRTM
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.
ABSTRACT
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 2,3–epoxypropyl 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.
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