Development of protease nanobiocatalysts and their application in hydrolysis of sunflower meal protein isolate. (12th July 2021)

• Record Type: Journal Article
• Authors: Katić, Katarina; Banjanac, Katarina; Simović, Milica; Ćorović, Marija; Milivojević, Ana; Marinković, Aleksandar; Bezbradica, Dejan
• Is Part Of: International journal of food science & technology. Volume 56:Number 9(2021)
• Page Start: 4287
• Page End: 4297
• Publication Date: 2021-07-12
• Subjects: Alcalase -- covalent immobilisation -- Flavourzyme -- nanobiocatalyst -- protein hydrolysates -- sunflower meal; Food industry and trade -- Periodicals; 664
• DOI: 10.1111/ijfs.15189
• Languages: English
• ISSNs: 0950-5423

Abstract

Summary: In this study, the suitability of fumed silica nanoparticles (FNS) and its derivatives (amino‐modified FNS (AFNS), cyanuric chloride‐activated AFNS (CCAFNS) and epoxy‐modified FNS (GFNS)), for covalent immobilisation of two commercial protease preparations Alcalase ® and Flavourzyme ® was investigated. The highest hydrolytic activities of immobilised preparations were 25 IU g −1 support (Alcalase‐GFNS) and 2.95 IU g −1 support (Flavourzyme‐CCAFNS). Furthermore, the immobilised preparations showed 43% and 20% of initial specific activities of commercial protease preparations, respectively. Flavourzyme‐CCAFNS also exhibited the highest exopeptidase activity of 22.83 L‐ p NAU g −1 support. Finally, these two nanobiocatalysts were successfully applied for hydrolysis of sunflower meal protein isolate (SMPI), providing two times higher hydrolysis yields in comparison to free enzymes, justifying the applied immobilisation process. Namely, the highest hydrolysis yield (30%) was gained by the sequential hydrolysis with Alcalase‐GFNS and Flavourzyme‐CCAFNS, which resulted in the formation of small hydrophobic and hydrophilic peptides, ≤5 kDa, confirmed by HPLC analysis and electrophoretic separation. Abstract : The sequential hydrolysis of sunflower meal protein isolate (SMPI) with nanobiocatalysts Alcalase‐GFNS and Flavourzyme‐CCAFNS resulted in the formation of small hydrophobic and hydrophilic peptides which was confirmed by HPLC analysis.