数字农科院2.0

Extraction of proteins from streptomycin fermentation residue using aminosilane-modified magnetic Fe3O4 nanoparticles immobilized with neutral protease and lysozyme

文献类型： 外文期刊

作者： Li, Zaixing;Zhang, Wenjing;Gao, Wei;Liu, Rui;Shu, Shangyi;Xu, Bingbing;Qin, Xue;Hong, Chen;Wang, Nannan

作者机构：

关键词： Streptomycin fermentation residue;Protein extraction;Magnetic Fe 3 O 4 nanoparticles;Neutral protease;Lysozyme

期刊名称： PROCESS BIOCHEMISTRY

ISSN： 1359-5113

年卷期： 2025 年 160 卷

页码：

收录情况： SCIE（2025版） ; ; EI（2025版）

摘要： Streptomycin fermentation residues (SFR) are rich in protein, and enzyme hydrolysis is an efficient technique for recovering protein from these residues. This study explores the extraction of protein from SFR using immobilized enzyme technology, aiming to achieve efficient protein extraction and repeated enzyme reuse, thereby promoting the cost-effective and efficient recovery of proteins from antibiotic fermentation residues. In this experiment, we synthesized amino-silane modified magnetic Fe3O4 nanoparticles (Fe3O4@SiO2-NH2) and used them as carriers to immobilize lysozyme (Lys) and neutral protease (Neu) on the surface of Fe3O4@SiO2-NH2 (CE-Fe3O4@SiO2-NH2), successfully preparing a recyclable biocatalyst. This catalyst was then used for protein extraction from SFR. In a 20.0 % glutaraldehyde solution, the composite enzyme (CE) concentration was 0.6 mg center dot mL- 1, and the crosslinking time was 5 h, resulting in the highest immobilization efficiency (74.7 % f 0.48 %) and enzyme relative activity (89.2 % f 0.59 %). The CE-Fe3O4@SiO2-NH2 still exhibited superparamagnetic properties, with a saturation magnetization of 54 emu center dot g- 1. After 30 days of storage, the CEFe3O4@SiO2-NH2 retained 75.6 % f 1.12 % of its initial activity. Under extraction conditions of pH 6.0, 45 degrees C, and 3 h, CE-Fe3O4@SiO2-NH2 successfully extracted 59.3 % f 1.08 % of the protein from SFR. Furthermore, after five cycles of reuse, CE-Fe3O4@SiO2-NH2 maintained 30.8 % f 1.20 % of its protein extraction capacity. The catalyst demonstrated significant protein extraction efficiency from SFR and can be repeatedly recovered, improving processing efficiency, reducing costs, and enhancing the practical application value of the enzyme.

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