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 in | Artificial cells, nanomedicine, and biotechnology Vol. 46; no. sup2; pp. 201 - 206 |
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Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Abingdon
Taylor & Francis
01.01.2018
Taylor & Francis Ltd |
Subjects | |
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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. |
Author_xml | – sequence: 1 givenname: Saleh A. surname: Mohamed fullname: Mohamed, Saleh A. email: saleh38@hotmail.com organization: Molecular Biology Department, National Research Centre – sequence: 2 givenname: Majed H. surname: Al-Harbi fullname: Al-Harbi, Majed H. organization: Biochemistry Department, Faculty of Science, King Abdulaziz University – sequence: 3 givenname: Yaaser Q. surname: Almulaiky fullname: Almulaiky, Yaaser Q. organization: Biochemistry Department, Faculty of Science, University of Jeddah – sequence: 4 givenname: Ibrahim H. surname: Ibrahim fullname: Ibrahim, Ibrahim H. organization: Biochemistry Department, Faculty of Science, King Abdulaziz University – sequence: 5 givenname: Hala A. surname: Salah fullname: Salah, Hala A. organization: Molecular Biology Department, National Research Centre – sequence: 6 givenname: Mohamed O. surname: El-Badry fullname: El-Badry, Mohamed O. organization: Molecular Biology Department, National Research Centre – sequence: 7 givenname: Azza M. surname: Abdel-Aty fullname: Abdel-Aty, Azza M. organization: Molecular Biology Department, National Research Centre – sequence: 8 givenname: Afaf S. surname: Fahmy fullname: Fahmy, Afaf S. organization: Molecular Biology Department, National Research Centre – sequence: 9 givenname: Reda M. surname: El-Shishtawy fullname: El-Shishtawy, Reda M. organization: Dyeing, Printing and Textile Auxiliaries Department, Textile Research Division, National Research Centre |
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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... In this study, a new support has been developed by immobilization of α-amylase onto modified magnetic Fe3O4-nanoparticles. The characterization of soluble and... |
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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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