Aspartic acid introduce the functional amine groups on the surface of superparamagnetic Fe(OH)3@Fe3O4 nanoparticles for efficient immobilization of Penaeus vannamei protease
In this study, we synthesized super magnetic Fe(OH)3@Fe3O4 nanoparticles (SPIONs) by the co-precipitation method and introduction of amine groups via chemisorption of l-aspartic acid (LAA) on the surface of SPIONs. Penaeus vannamei protease (PVP) was immobilized onto amine-functionalized supermagnetic nanoparticles (ASPIONs), and conditions affecting PVP immobilization were investigated. PVP immobilized onto ASPIONs exhibited shifts in both working optimum pH and temperature with an increase from pH 7 to pH 8, and increased optimum temperature by 10 °C compared to free enzyme. Similarly, the thermal, pH, and storage stabilities of the immobilized PVP were superior to those of free form of the enzyme. In comparison to the free enzyme, the immobilized enzyme was reusable for 15 cycles while retaining 73% of its initial activity. The Michaelis–Menten kinetic constant (Km) and maximum reaction velocity (Vmax) for free PVP were 2.3 µM and 88 µM min−1, respectively, whereas Km and Vmax values of immobilized enzyme were 2.5 µM and 85 µM min−1, respectively. These results indicated that immobilized PVP was efficient in terms of catalytic activity and can be applied to continuous casein processing applications in the different industries.
KeywordsSuperparamagnetic Fe(OH)3@Fe3O4 nanoparticles Aspartic acid Functional amine groups Penaeus vannamei protease
Authors are grateful to the University of Hormozgan for the financial support to this research.
Compliance with ethical standards
Conflict of interest
This work is free from any conflict of interest.
- 13.Shojaei F, Homaei A, Taherizadeh MR, Kamrani E (2017) Characterization of biosynthesized chitosan nanoparticles from Penaeus vannamei for the immobilization of P. vannamei protease: an eco-friendly nanobiocatalyst. Int J Food Prop 20:S1413–S1423Google Scholar
- 14.Dadshahi Z, Homaei A, Zeinali F et al (2016) Extraction and purification of a highly thermostable alkaline caseinolytic protease from wastes Litopenaeus vannamei suitable for food and detergent industries. Food Chem 202:110–115. https://doi.org/10.1016/j.foodchem.2016.01.104 CrossRefPubMedGoogle Scholar
- 23.Das A, Singh J, Yogalakshmi KN (2017) International biodeterioration and biodegradation laccase immobilized magnetic iron nanoparticles: fabrication and its performance evaluation in chlorpyrifos degradation. Int Biodeterior Biodegrad 117:183–189. https://doi.org/10.1016/j.ibiod.2017.01.007 CrossRefGoogle Scholar
- 25.Arrhenius S (1889) Uber die Reaktionsgeschwindigkeit bei der Inversion von Rohrzucker durch Säuren. Z Phys Chem 4:226Google Scholar
- 30.Tischer W, Kasche V (1999) Immobilized enzymes: crystals or carriers? 17:326–335Google Scholar
- 32.Palmer T (1995) Understanding enzymes. Prentice Hall/Ellis Horwood, Upper Saddle RiverGoogle Scholar
- 33.Jafary F, Panjehpour M, Varshosaz J, Yaghmaei P (2016) Stability improvement of immobilized alkaline phosphate using chitosan nanoparticles. Braz J Chem Eng 33:243–250. https://doi.org/10.1590/0104-6632.20160332s20140074 CrossRefGoogle Scholar
- 34.Samani NB, Nayeri H, Amiri G (2016) Effects of cadmium chloride as inhibitor on stability and kinetics of immobilized Lactoperoxidase (LPO) on silica-coated magnetite nanoparticles versus free LPO. 3:pp 230–239Google Scholar