Engineered material-binding peptide empowers biocatalysis in stainless steel flow reactors for phosphate recovery

IF 19.6 1区 化学 Q1 CHEMISTRY, MULTIDISCIPLINARY Chem Pub Date : 2025-05-08 Epub Date: 2025-01-30 DOI:10.1016/j.chempr.2024.102395
Yi Lu , Florian Bourdeaux , Binbin Nian , Pirathiha Manimaran , Bhupesh Verma , Max Rommerskirchen , Sebastian Bold , Leilei Zhu , Yu Ji , Johannes Henrich Schleifenbaum , Ulrich Schwaneberg
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Abstract

Biocatalysis in stainless steel flow reactors is limited by inefficient enzyme immobilization on stainless steel surfaces. Herein, we report a universal and generally applicable strategy to achieve efficient enzyme immobilization in stainless steel flow reactors by utilizing an engineered material-binding peptide (MBP) with improved binding toward stainless steel. Through this method, phytase from Yersinia mollaretii (YmPh) was immobilized and showed high activity in hydrolyzing phytic acid to produce phosphate over multiple cycles. The MBP liquid chromatography peak I (LCI) was selected and engineered for improved stainless steel binding. The variant LCISS4 (LCI A14K/Y30R/D45R) showed an 8.2-fold improved binding to stainless steel compared with the LCI wild type. YmPh-LCISS4 immobilized in additively manufactured stainless steel flow reactors exhibited strong washing resistance and high reusability. The immobilization strategy presented here, based on LCISS4, enables robust and oriented enzyme immobilization on stainless steel, making it an appealing tool for industrial biocatalysis.

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工程材料结合肽授权生物催化在不锈钢流动反应器的磷酸盐回收
不锈钢流动反应器中的生物催化受到不锈钢表面酶固定效率低下的限制。在此,我们报告了一种通用且普遍适用的策略,通过利用改良的与不锈钢结合的工程材料结合肽(MBP),在不锈钢流动反应器中实现高效的酶固定化。该方法固定化了mollaretii耶尔森氏菌(Yersinia mollaretii, YmPh)植酸酶,该酶水解植酸生成磷酸盐的活性较高。选择并设计了MBP液相色谱峰I (LCI),用于改善不锈钢的结合。变体LCISS4 (LCI A14K/Y30R/D45R)与野生型LCI相比,与不锈钢的结合能力提高了8.2倍。在增材制造的不锈钢流动反应器中固定化YmPh-LCISS4具有较强的耐洗涤性和较高的可重复使用性。本文提出的基于LCISS4的固定化策略能够在不锈钢上实现稳健和定向的酶固定化,使其成为工业生物催化的一种有吸引力的工具。
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来源期刊
Chem
Chem Environmental Science-Environmental Chemistry
CiteScore
32.40
自引率
1.30%
发文量
281
期刊介绍: Chem, affiliated with Cell as its sister journal, serves as a platform for groundbreaking research and illustrates how fundamental inquiries in chemistry and its related fields can contribute to addressing future global challenges. It was established in 2016, and is currently edited by Robert Eagling.
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