Investigation of the ELP-Mediated Silicification-Based Protein Self-Immobilization Using an Acidic Target Enzyme

Recently, we proposed a novel and effective strategy for enzyme immobilization, namely, as elastin-like polypeptide (ELP)-mediated silicification-based protein self-immobilization (ESPSI). Here, an enzyme with an acidic isoelectric point (pI) was chosen to further demonstrate the feasibility and gen...

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Published in:Industrial & engineering chemistry research 2020-11, Vol.59 (44), p.19829-19837
Main Authors: Lin, Yuanqing, Qiu, Yue, Cai, Lixi, Zhang, Guangya
Format: Article
Language:English
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Summary:Recently, we proposed a novel and effective strategy for enzyme immobilization, namely, as elastin-like polypeptide (ELP)-mediated silicification-based protein self-immobilization (ESPSI). Here, an enzyme with an acidic isoelectric point (pI) was chosen to further demonstrate the feasibility and generality of this method; pI is a critical factor in biosilicification. The lichenase (BglS) from Bacillus subtilis 168, with a theoretical pI of 5.77, was genetically fused to the cationic ELP. The recombinant chimera protein BglS-ELP (B-E) was purified through ELP-based nonchromatographic inverse transition cycling (ITC) method. B-E then was self-encapsulated within silica nanoparticle (NP) via ELP-mediated biomimetic silicification, producing the nanobiocatalyst B-E@silica. Excellent encapsulation efficiency (>85%) could be achieved within a short immobilization time (10 min). In addition, the encapsulation efficiency could be promoted through temperature-induced phase transition. Meanwhile, this method gave negligible protein leakage (
ISSN:0888-5885
1520-5045
DOI:10.1021/acs.iecr.0c03111