J Am Chem Soc. 2026 Aug 26;148(33):35941-35948. doi: 10.1021/jacs.6c09682. ABSTRACT Protein stabilizers and denaturants can be used to elucidate the fundamental principles of hydration, which is crucial for biological functions and biotechnology. Despite decades of work, existing molecular models of such stabilizers and denaturants have not yet been fully validated because few experimental methods can…

J Agric Food Chem. 2026 Aug 26;74(33):26498-26509. doi: 10.1021/acs.jafc.6c03912. ABSTRACT Biomass polysaccharides are explored as inexpensive raw materials for preparing value-added products, such as mannan oligosaccharides (MOS). However, the varied composition of MOS and the underlying mechanism have not been studied thoroughly yet. Here a β-mannanase from Paenibacillus sp. was engineered for hydrolyzing biomass polysaccharides…

J Agric Food Chem. 2026 Aug 26;74(33):26714-26734. doi: 10.1021/acs.jafc.6c06898. ABSTRACT Co-contamination of aflatoxin B1 (AFB1) and zearalenone (ZEN) poses a major food safety risk. In this study, the copper-containing nitrite reductase AfNiR was identified as a novel biocatalyst for AFB1 and ZEN degradation, achieving maximum efficiencies of 99.22% and 93.53%, respectively, under optimal conditions of…

J Agric Food Chem. 2026 Aug 26;74(33):26484-26497. doi: 10.1021/acs.jafc.6c03843. ABSTRACT Aflatoxins are major contaminants in raw food materials and their products. Developing enzymes that efficiently degrade multiple aflatoxins under acidic conditions has great practical value. In this study, the aflatoxin-degrading enzyme ADPPIII from Aspergillus terreus was systematically engineered. Substrate tunnel optimization obtained mutant F375L, which…

Chemphyschem. 2026 Sep 14;27(17):e70555. doi: 10.1002/cphc.70555. ABSTRACT The Kemp elimination reaction can be catalyzed by computationally designed enzymes. After undergoing directed evolution, changes to the positioning of active site residues in Kemp eliminases can alter electric fields (EFs) and improve catalytic efficiency. However, optimizing EFs during the enzyme design process remains a challenge. Here we…

Plant Commun. 2026 Aug 31:102088. doi: 10.1016/j.xplc.2026.102088. Online ahead of print. ABSTRACT Engineering enzymes with enhanced activity and stability is a central goal of biotechnology, yet the inherent trade-off between optimizing global protein fitness and specific substrate binding affinity poses a significant challenge. Here, we present ESM-FEP, a computational framework that synergistically integrates a fine-tuned…

ChemSusChem. 2026 Sep 14;19(17):e71038. doi: 10.1002/cssc.71038. ABSTRACT Living organisms have evolved multienzyme complexes to achieve efficient and spatially ordered metabolic reactions. Recently, liquid-liquid phase separation (LLPS) has emerged as a fundamental organizational principle underlying these natural networks, providing a versatile platform for constructing artificial multienzyme catalytic systems. Owing to their reversible self-assembly and programmable nature,…

Anal Chem. 2026 Aug 25;98(33):24379-24387. doi: 10.1021/acs.analchem.6c03212. ABSTRACT Enthalpy-driven catalytic hairpin assembly (CHA) suffers from an inherent trade-off, wherein enhanced reaction kinetics is inevitably accompanied by elevated nonspecific background. Catalytic hairpin assembly-and-cyclization (CHAC) integrates CHA with enzymatic ligation, allowing single-target-triggered multiple circularization events and thus bypassing the stoichiometric limitation of conventional padlock probe ligation. Nevertheless,…

J Chem Theory Comput. 2026 Aug 25;22(16):8595-8606. doi: 10.1021/acs.jctc.6c00761. ABSTRACT Predicting how mutations alter enzyme catalysis remains a central challenge in enzymology and enzyme engineering. Although quantum mechanics/molecular mechanics (QM/MM) simulations can in principle compute the activation free energy associated with enzymatic reactions, their high computational cost limits systematic studies across many variants. Here, we…

J Chem Theory Comput. 2026 Aug 25;22(16):8682-8699. doi: 10.1021/acs.jctc.6c01142. ABSTRACT Redox enzymes play an essential role in nature and in biotechnological applications such as (photo)biocatalysis and biosensing. Understanding how a protein’s sequence and structure tune its redox potential is very valuable for engineering proteins with tailored (photo)redox properties. Since protein redox potential measurements are laborious,…