Immobilization of Trichoderma harzianum α-amylase on PPyAgNp/Fe3O4-nanocomposite: chemical and physical properties

In this study, a new support has been developed by immobilization of α-amylase onto modified magnetic Fe 3 O 4 -nanoparticles. The characterization of soluble and immobilized α-amylases with regards to kinetic parameters, pH, thermal stability and reusability was studied. The effect of polypyrrole/s...

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Published inArtificial cells, nanomedicine, and biotechnology Vol. 46; no. sup2; pp. 201 - 206
Main Authors Mohamed, Saleh A., Al-Harbi, Majed H., Almulaiky, Yaaser Q., Ibrahim, Ibrahim H., Salah, Hala A., El-Badry, Mohamed O., Abdel-Aty, Azza M., Fahmy, Afaf S., El-Shishtawy, Reda M.
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LanguageEnglish
Published Abingdon Taylor & Francis 01.01.2018
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Abstract In this study, a new support has been developed by immobilization of α-amylase onto modified magnetic Fe 3 O 4 -nanoparticles. The characterization of soluble and immobilized α-amylases with regards to kinetic parameters, pH, thermal stability and reusability was studied. The effect of polypyrrole/silver nanocomposite (PPyAgNp) percentage on weight of Fe 3 O 4 and pH on the immobilization of α-amylase was studied. The highest immobilization efficiency (75%) was detected at 10% PPyAgNp/Fe 3 O 4 -nanocomposite and pH 7.0. Immobilization of α-amylase on PPyAgNp/Fe 3 O 4 -nanocomposite was characterized by FT-IR spectroscopy and scanning electron microscopy. The reusability of the immobilized enzyme activity was 80% of its initial activity after 10 reuses. The immobilized enzyme was more stable towards pH, temperature and metal ions compared with soluble enzyme. The kinetic study appeared higher affinity of immobilized enzyme (K m 2.5 mg starch) compared with soluble enzyme (K m 3.5 mg starch). In conclusion, the immobilization of α-amylase on PPyAgNp/Fe 3 O 4 -nanocomposite could successfully be used in industrial and medical applications.
AbstractList In this study, a new support has been developed by immobilization of α-amylase onto modified magnetic Fe3O4-nanoparticles. The characterization of soluble and immobilized α-amylases with regards to kinetic parameters, pH, thermal stability and reusability was studied. The effect of polypyrrole/silver nanocomposite (PPyAgNp) percentage on weight of Fe3O4 and pH on the immobilization of α-amylase was studied. The highest immobilization efficiency (75%) was detected at 10% PPyAgNp/Fe3O4-nanocomposite and pH 7.0. Immobilization of α-amylase on PPyAgNp/Fe3O4-nanocomposite was characterized by FT-IR spectroscopy and scanning electron microscopy. The reusability of the immobilized enzyme activity was 80% of its initial activity after 10 reuses. The immobilized enzyme was more stable towards pH, temperature and metal ions compared with soluble enzyme. The kinetic study appeared higher affinity of immobilized enzyme (Km 2.5 mg starch) compared with soluble enzyme (Km 3.5 mg starch). In conclusion, the immobilization of α-amylase on PPyAgNp/Fe3O4-nanocomposite could successfully be used in industrial and medical applications.
In this study, a new support has been developed by immobilization of α-amylase onto modified magnetic Fe 3 O 4 -nanoparticles. The characterization of soluble and immobilized α-amylases with regards to kinetic parameters, pH, thermal stability and reusability was studied. The effect of polypyrrole/silver nanocomposite (PPyAgNp) percentage on weight of Fe 3 O 4 and pH on the immobilization of α-amylase was studied. The highest immobilization efficiency (75%) was detected at 10% PPyAgNp/Fe 3 O 4 -nanocomposite and pH 7.0. Immobilization of α-amylase on PPyAgNp/Fe 3 O 4 -nanocomposite was characterized by FT-IR spectroscopy and scanning electron microscopy. The reusability of the immobilized enzyme activity was 80% of its initial activity after 10 reuses. The immobilized enzyme was more stable towards pH, temperature and metal ions compared with soluble enzyme. The kinetic study appeared higher affinity of immobilized enzyme (K m 2.5 mg starch) compared with soluble enzyme (K m 3.5 mg starch). In conclusion, the immobilization of α-amylase on PPyAgNp/Fe 3 O 4 -nanocomposite could successfully be used in industrial and medical applications.
Author Al-Harbi, Majed H.
Abdel-Aty, Azza M.
Ibrahim, Ibrahim H.
El-Badry, Mohamed O.
Fahmy, Afaf S.
Almulaiky, Yaaser Q.
Salah, Hala A.
Mohamed, Saleh A.
El-Shishtawy, Reda M.
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Snippet In this study, a new support has been developed by immobilization of α-amylase onto modified magnetic Fe 3 O 4 -nanoparticles. The characterization of soluble...
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SubjectTerms Amylases
Enzymatic activity
Enzyme activity
Enzymes
Fourier transforms
Fungi
Immobilization
Infrared spectroscopy
Iron oxides
Metal ions
nanocomposite
Nanocomposites
Nanoparticles
Organic chemistry
pH effects
Physical properties
Polypyrroles
PPyAgNp/Fe
Scanning electron microscopy
Silicon
Silver
Starch
Thermal stability
Trichoderma harzianum
Weight
α-Amylase
Title Immobilization of Trichoderma harzianum α-amylase on PPyAgNp/Fe3O4-nanocomposite: chemical and physical properties
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