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This enzyme from Aspergillus sp. is useful for a broad spectrum of reactions, such as enantioselective hydrolysis of amino acid esters and amides [161], regiose‐ lective alcoholysis of carboxylic acid esters [162–164], acylation of primary and secondary alcohols [165–168], and acylation of amines [165–169]. Immobilization of L‐aminoacylase from Aspergillus melleus using coaggregation with polyethyleneimine and subsequent cross‐linking with glutaraldehyde resulted in stable aminoacylase‐polyethyleneimine CLEAs (AP‐CLEA) with significantly higher temperature and storage stability of the enzyme without affecting its enantioselectivity [170].

This reaction is important in the food, cosmetic, and pharmaceutical industries, because trehalose is known to have high water‐holding activity and this characteristic makes it applicable to the develop‐ ment of additives, stabilizers, and sweeteners [188]. 4. Conclusion The stability of enzymes is important for biotechnological applications and can be achieved via immobilization methods. Large amounts of research have been devoted into exploring the synthesis and modification of magnetic nanoparticles.

Their inorganic magnetic core is usually surrounded by layers of functional coatings (Figure 1). Frequently used magnetic nanoparticles are also cobalt and nickel magnetic nanoparticles. Cobalt is a ferromagnetic element commonly used as an alloying element in permanent magnets. Nickel magnetic nanoparticles are of great interest due to their superparamagnetic and optical properties. There have been many protocols for the synthesis of cobalt or nickel magnetic nanoparticles, which include thermal decomposition, reverse micelles, chemical reduction, and polyol reduction, and for cobalt magnetic nanoparticles also sonochemical synthesis [54–62].

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