Опубликована: Янв. 1, 2024
Язык: Английский
ACS Omega, Год журнала: 2024, Номер 9(47), С. 46698 - 46732
Опубликована: Ноя. 14, 2024
Immobilization of lipases by physical adsorption improves their stability, recovery, and reusability in biotechnological processes. The present review provides an advanced bibliometric analysis a comprehensive overview research progress this field. By searching Web Science, 39,575 publications were analyzed, 325 relevant articles selected. Key journals, countries, institutions, authors identified. most cited focus on biofuel production industrial applications. revealed four themes with the biofuel. method is effective when appropriate support used. Despite decrease patent applications, interest remains high. Future studies should optimizing materials exploring new applications technique. detailed understanding immobilization adsorption.
Язык: Английский
Процитировано
16
Journal of the American Chemical Society, Год журнала: 2024, Номер 146(28), С. 18817 - 18822
Опубликована: Июль 5, 2024
NAD(H)-dependent enzymes play a crucial role in the biosynthesis of pharmaceuticals and fine chemicals, but limited recyclability NAD(H) cofactor hinders its more general application. Here, we report generation mechano-responsive PEI-modified Cry3Aa protein crystals their use for NADH recycling over multiple reaction cycles. For demonstration practical utility, complementary particle containing genetically encoded co-immobilized formate dehydrogenase regeneration leucine catalyzing NADH-dependent l-tert-leucine (l-tert-Leu) has been produced. When combined with crystal, resultant system could be used efficient l-tert-Leu up to 21 days 10.5-fold improvement turnover number.
Язык: Английский
Процитировано
3
Protein Science, Год журнала: 2025, Номер 34(2)
Опубликована: Янв. 22, 2025
Abstract Enzyme immobilization is indispensable for enhancing enzyme performance in various industrial applications. Typically, enzymes require specific spatial arrangements optimal functionality, underscoring the importance of correct orientation. Despite well‐known N‐ or C‐terminus tailoring techniques, alternatives achieving orientation control are limited. Here, we propose a novel approach that tailors surface with engineered His‐rich loops. To aim, first solve X‐ray crystal structure hexameric alcohol dehydrogenase from Thermus thermophilus HB27 (TtHBDH) (PDB: 9FBD ). Guided by this 3D structure, engineer new loop enriched six His residues to Molecular dynamics simulations reveal loop's imidazole rings have greater solvent accessibility than those native residues, allowing more efficient on certain metal chelate‐functionalized carriers. Using carriers functionalized iron (III)‐catechol, apparent V max immobilized variant doubles His‐tagged one, and vice versa when both variants copper (II)‐imidodiacetic acid. loop‐engineered TtHBDH show high operational stability reaching 100% bioconversion after 10 reaction cycles, yet faster one.
Язык: Английский
Процитировано
0
Methods in enzymology on CD-ROM/Methods in enzymology, Год журнала: 2025, Номер unknown
Опубликована: Янв. 1, 2025
Язык: Английский
Процитировано
0
Topics in organometallic chemistry, Год журнала: 2025, Номер unknown
Опубликована: Янв. 1, 2025
Язык: Английский
Процитировано
0
Chem & Bio Engineering, Год журнала: 2025, Номер unknown
Опубликована: Март 17, 2025
The production of active pharmaceutical ingredients (APIs) requires enantiopure chiral amines, for which greener synthesis processes are needed. Transaminases (TAs) enzymes that catalyze the enantioselective amines from prochiral ketones through transamination under mild conditions. Yet, industrial applications biocatalytic remain currently hindered by limited stability soluble and unfavorable thermodynamic equilibrium targeted asymmetric reactions. Enzyme immobilization can be applied to address stability, recoverability, reusability issues. In perspective process intensification, we chose immobilize TAs on polymeric (polypropylene) membranes. (R)-2-fluoro-α-methylbenzylamine ((R)-FMBA), such membrane-immobilized exhibited superior specific activity compared with TAs; they also outperformed immobilized resins. reaction yield remained, however, thermodynamics. To further enhance yield, was coupled in situ crystallization (R)-FMBA 3,3-diphenylpropionic acid (DPPA). By doing so, theoretical conversion pushed ∼44% ∼83%. fact, a 72% overall recovery crystallized demonstrated. enantioselectivity mixture preserved. Importantly, purification greatly facilitated since target amine readily recovered as high-purity (R)-FMBA:DPPA crystals. membranes were found fully reusable, performing successive high-yield syntheses only minor deactivation. Overall, crystallization-assisted strategy proposed herein offers path valuable targets.
Язык: Английский
Процитировано
0
ACS Applied Materials & Interfaces, Год журнала: 2025, Номер unknown
Опубликована: Май 25, 2025
Additive manufacturing, commonly known as three-dimensional (3D) printing, transforms simple in silico designs into real objects with accessibility, reproducibility, and precision. By merging the versatility of 3D printing inherent advantages enzymatic processes, this technology opens up new possibilities for optimizing enzyme immobilization continuous flow reactors. Here, we systematically investigate various formulations to develop an optimal biocatalytic ink capable encapsulating enzymes cofactors within a hydrogel matrix. The ink, composed agarose polyethylenimine (PEI), printed porous monoliths, improved retention cofactor absorption through ionic interactions, outperforming alternative formulations. further integrating gold nanorods system, reaction substrates intermediates (i.e., NAD+, isopropanol) can be detected operando surface enhanced Raman scattering (SERS) sensing, serving complementary tool fluorescence microscopy. Using optimized fabricated 3D-printed reactors diverse architectures evaluate their efficiency reduction ethyl acetoacetate. Reactors cross-shaped design exhibit stable product yields minimize leaching during operation. Hence, formulate print self-sufficient sustaining activity immobilized dehydrogenases reactions without addition exogenous cofactors.
Язык: Английский
Процитировано
0
ACS Applied Nano Materials, Год журнала: 2025, Номер unknown
Опубликована: Май 30, 2025
Язык: Английский
Процитировано
0
Comptes Rendus Chimie, Год журнала: 2025, Номер 28(G1), С. 543 - 559
Опубликована: Июнь 4, 2025
Industrial biotechnology stands at a turning point. While enzymes have long promised green, efficient catalysis, their widespread adoption has been held back by practical limitations. In this work, we introduce an innovative family of sustainable carrier materials that redefine enzyme immobilization. These are synthesized via controlled solvothermal process, using renewable sources sugars and polyphenols to create interconnected porous structure with tunable surface chemistry. This design enables strong binding through mechanisms such as metal complexation, hydrophobic interactions, hydrogen bonding, offering high loading capacities exceptional operational stability. Developed sustainability core, these set new standards for both performance environmental responsibility, bridging the gap between laboratory research industrial applications in biocatalysis.
Язык: Английский
Процитировано
0
Bioresources and Bioprocessing, Год журнала: 2024, Номер 11(1)
Опубликована: Июль 18, 2024
Abstract Reductive amination by amine dehydrogenases is a green and sustainable process that produces only water as the by-product. In this study, continuous flow was designed utilizing packed bed reactor filled with co-immobilized dehydrogenase wh84 glucose for highly efficient biocatalytic synthesis of chiral amino alcohols. The immobilized exhibited better thermo-, pH solvent stability high activity recovery. ( S )-2-aminobutan-1-ol produced in up to 99% conversion ee processes, space-time yields were 124.5 g L -1 d . reactions also extended 48 h affording 91.8% average conversions. This study showcased important potential production alcohols processes.
Язык: Английский
Процитировано
2