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

IF 19.1 1区化学 Q1 CHEMISTRY, MULTIDISCIPLINARY Chem Pub 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 LCI_SS4 (LCI A14K/Y30R/D45R) showed an 8.2-fold improved binding to stainless steel compared with the LCI wild type. YmPh-LCI_SS4 immobilized in additively manufactured stainless steel flow reactors exhibited strong washing resistance and high reusability. The immobilization strategy presented here, based on LCI_SS4, enables robust and oriented enzyme immobilization on stainless steel, making it an appealing tool for industrial biocatalysis.

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来源期刊

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.