Preparative Biochemistry & Biotechnology最新文献_第2页

Ultrasound-assisted extraction via RSM, phytochemical profiling and evaluation of TPC, TFC, α-glucosidase inhibitory & antioxidant activity of Crotalaria willdenowiana DC. Extracts. 超声辅助RSM提取、植物化学分析及对芥蓝TPC、TFC、α-葡萄糖苷酶抑制和抗氧化活性的评价。提取物。

IF 2.2 4区生物学

Preparative Biochemistry & Biotechnology Pub Date : 2026-10-04 DOI: 10.1080/10826068.2026.2734542

Charu Bhutani, Upasna Balyan, P Radha, C Udhayavani, Pankaj Khanna, Leena Khanna

{"title":"Ultrasound-assisted extraction via RSM, phytochemical profiling and evaluation of TPC, TFC, α-glucosidase inhibitory & antioxidant activity of Crotalaria willdenowiana DC. Extracts.","authors":"Charu Bhutani, Upasna Balyan, P Radha, C Udhayavani, Pankaj Khanna, Leena Khanna","doi":"10.1080/10826068.2026.2734542","DOIUrl":"https://doi.org/10.1080/10826068.2026.2734542","url":null,"abstract":"Crotalaria willdenowiana DC., an endemic and underexplored species from the wastelands and forested slopes of Tamil Nadu, was investigated for its phytochemical and biological potential using ultrasound-assisted extraction (UAE) optimized through Response Surface Methodology (RSM). Twenty methanolic root extracts were prepared under varying conditions of sample weight (0.15-1.841 g), extraction time (9.54-110.54 min), and temperature (26.5-68.5 °C). The optimized extract, obtained at 71.69 min, 57.27 °C, and a sample weight of 1.50 g, showed the maximum phytochemical yield, with TPC of 135.32 mg GAE/g, TFC of 122.85 mg QE/g, and an extraction yield of 24.13%. HPLC confirmed the presence of gallic acid and quercetin. Quantitative HPLC showed the presence of gallic acid (22.66 µg/mL) and quercetin (31.84 µg/mL), confirming the presence of some important phenolic and flavonoid components from the extract. In addition, NMR and FTIR studies confirmed the presence of signature functional groups and structural elements for these bioactive compounds. The extract exhibited 65% DPPH radical-scavenging activity and significant α-glucosidase inhibition (IC50 = 286.25 μg/mL). GC-MS analysis further identified 42 volatile constituents in the optimized extract.","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"1-21"},"PeriodicalIF":2.2,"publicationDate":"2026-10-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149113817","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Coated bacterial enzymes: a one-step approach for enzymatic purification and immobilization. 包膜细菌酶：一步法酶纯化和固定化。

IF 2.2 4区生物学

Preparative Biochemistry & Biotechnology Pub Date : 2026-10-01 DOI: 10.1080/10826068.2026.2736623

Inés Harguindeguy, Melisa S Homse, Andrea C Ramírez, Alan E Sabetta, Sebastián F Cavalitto, Gastón E Ortiz

{"title":"Coated bacterial enzymes: a one-step approach for enzymatic purification and immobilization.","authors":"Inés Harguindeguy, Melisa S Homse, Andrea C Ramírez, Alan E Sabetta, Sebastián F Cavalitto, Gastón E Ortiz","doi":"10.1080/10826068.2026.2736623","DOIUrl":"https://doi.org/10.1080/10826068.2026.2736623","url":null,"abstract":"The purification of industrial enzymes typically relies on costly, multi‑step chromatographic protocols. To address this, we developed a novel platform termed Coated Bacterial Enzymes (CBEs), which enables one‑step purification and immobilization of recombinant proteins fused to the SlpA cell wall binding domain. As a proof of concept, we used a β‑galactosidase from Bifidobacterium bifidum of dairy relevance. The chimeric enzyme BbgII‑SlpA was expressed in Escherichia coli and captured from crude lysate onto glutaraldehyde‑inactivated Bacillus subtilis cells via SlpA domain. Binding was characterized by a dissociation constant (Kd) of 16.2 μM and maximum binding capacity (Bmax) of 144 μmol/g. The resulting CBEs biocatalyst exhibited optimal activity at pH 6.0 for ONPG and lactose, with a broader pH profile than the free enzyme. Optimal temperatures were 60 °C for ONPG and 50 °C for lactose, and CBEs retained >80% activity after 390 min at 45 °C, compared to 20% for the free enzyme. Catalytic efficiencies (kcat/Km) were 2.62 × 106 M-1·s-1 for ONPG and 4.40 × 102 M-1·s-1 for lactose. Moreover, CBEs showed improved tolerance to cations such as Ca2+ and Fe2+. Furthermore, at 7 °C in skim milk, the CBEs achieved approximately 53% lactose hydrolysis within 20 h and retained 35-45% of its initial activity after five reuse cycles.","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"1-13"},"PeriodicalIF":2.2,"publicationDate":"2026-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149113795","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Valorization of banana flower waste for biopolymer coatings to enhance post-harvest quality of black grapes. 香蕉花废弃物制备生物聚合物涂层以提高黑葡萄采后品质。

IF 2.2 4区生物学

Preparative Biochemistry & Biotechnology Pub Date : 2026-09-28 DOI: 10.1080/10826068.2026.2737344

Adhithya Sankar Santhosh, Suzaine Roy Zachariah, Rita Rose Chacko, Mridul Umesh

{"title":"Valorization of banana flower waste for biopolymer coatings to enhance post-harvest quality of black grapes.","authors":"Adhithya Sankar Santhosh, Suzaine Roy Zachariah, Rita Rose Chacko, Mridul Umesh","doi":"10.1080/10826068.2026.2737344","DOIUrl":"https://doi.org/10.1080/10826068.2026.2737344","url":null,"abstract":"Banana is one of the most consumed fruits globally, but only a part of it is consumed and the rest of the plant is disposed of which generates a large amount of waste. This paper focuses on how banana waste (Banana flowers) can be utilized for the isolation of cellulose. The effective isolation of cellulose from banana flowers is examined in this work as a potential sustainable and profitable source. The cellulose extraction from banana flowers was done using combination of solvent extraction, alkali treatment and bleaching and the yield obtained from the banana flower was 58.37 ± 0.03% (w/w). The purity and structural characteristics of the isolated cellulose are characterized by using FTIR, XRD, SEM, TEM, DSC, and TGA. The isolated cellulose was subjected to shelf-life extension property study using black grapes. The shelf-life extension was most significant for black grapes coated with 1% cellulose with a significant reduction of weight loss (75.40 ± 1.40%) as compared to the uncoated grapes (14.40 ± 0.18%) when maintained at room temperature for 10 days. The results demonstrated the viability of using banana flowers, an underutilized and renewable resource for cellulose isolation, advancing the development of environmentally friendly substitutes in the material industry.","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"1-13"},"PeriodicalIF":2.2,"publicationDate":"2026-09-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149075796","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

PEG-directed structural modulation of short hexagonal Co-nanozyme: enhanced aqueous stability, high peroxidase activity and colorimetric detection of H₂O₂ and dopamine. 短六方共纳米酶的peg定向结构调节：增强水稳定性，高过氧化物酶活性和H2O2和多巴胺的比色检测。

IF 2.2 4区生物学

Preparative Biochemistry & Biotechnology Pub Date : 2026-09-28 DOI: 10.1080/10826068.2026.2693867

Santosh Sethi, Virendra Kisan Rathod

{"title":"PEG-directed structural modulation of short hexagonal Co-nanozyme: enhanced aqueous stability, high peroxidase activity and colorimetric detection of H2O2 and dopamine.","authors":"Santosh Sethi, Virendra Kisan Rathod","doi":"10.1080/10826068.2026.2693867","DOIUrl":"https://doi.org/10.1080/10826068.2026.2693867","url":null,"abstract":"Nanozyme offers promising alternatives to natural enzymes, but has poor aqueous stability and aggregation, which limit their practical applications. In this work, a polyethylene glycol (PEG)-modulated short hexagonal-Co-nanozyme was synthesized via co-precipitation methods to address these limitations. Different PEG molecular weights (2000-8000) were evaluated, and scanning electron microscope (SEM) imaging and dynamic light scattering (DLS) results confirmed that PEG 6000 at 10% w/w produced uniform hexagonal particles, non-aggregates, well-dispersed with an excellent particle size distribution (PSD), and aqueous stability. The morphological, crystallographic, and phase structure analysis supported by SEM, PSD, transmission electron microscopy (TEM), seleced area electron diffraction (SAED), and XRD. Surface area, porosity, and chemical composition by AFM, BET, and FTIR. Additionally, the surface state, surface charge and colloidal stability by X-ray photoelectron spectroscopy (XPS) and zetapotential by DLS. The optimized nanozyme exhibited strong peroxidase activity with a low Km = 20.77 µM (Vmax = 0.046 µM/s). Under the optimized conditions of TMB, nanozyme (pH 4.0, 55 °C) and 10 min reaction time, the system enabled sensitive colorimetric detection of H2O2 (limit of detection [LOD] = 0.79 µM, limit of quantification [LOQ] = 2.4 µM, linear range 1-20 µM) and dopamine (LOD = 0.86 µM, LOQ = 2.63 µM, linear range 2.5-25 µM). The interference studies confirmed high selectivity, while spiked assays achieved recoveries between 105 to 116% with RSD % below 5%. These findings establish PEG-modulated Co-MOF as a stable, sensitive, and versatile platform for next-generation sensing.","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"1-17"},"PeriodicalIF":2.2,"publicationDate":"2026-09-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149075660","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Sinapic acid-mediated green synthesis of silver nanoparticles: characterization, antioxidant capacity and antidiabetic enzyme inhibition. 辛酸介导的纳米银绿色合成：表征、抗氧化能力和抗糖尿病酶抑制。

IF 2.2 4区生物学

Preparative Biochemistry & Biotechnology Pub Date : 2026-09-28 DOI: 10.1080/10826068.2026.2736619

Nadia Murshed Abed, Emel Ekinci, Zeyad Adil Hameed Hameed, Şevki Adem

{"title":"Sinapic acid-mediated green synthesis of silver nanoparticles: characterization, antioxidant capacity and antidiabetic enzyme inhibition.","authors":"Nadia Murshed Abed, Emel Ekinci, Zeyad Adil Hameed Hameed, Şevki Adem","doi":"10.1080/10826068.2026.2736619","DOIUrl":"https://doi.org/10.1080/10826068.2026.2736619","url":null,"abstract":"Green synthesis using chemically defined natural phenolic compounds offers a reproducible route to biofunctional nanomaterials. Here, sinapic acid-mediated silver nanoparticles (Sin-AgNPs) were prepared and evaluated for physicochemical characteristics, antioxidant capacity, and inhibition of carbohydrate-hydrolyzing enzymes. Condition screening selected pH 10, 50 °C, a 1:1 sinapic acid/silver nitrate volume ratio, and 8 mM silver nitrate. Ultraviolet-visible spectroscopy showed a surface plasmon resonance band at 400-450 nm. Scanning electron microscopy indicated predominantly spherical particles with dry diameters of approximately 31-96 nm, whereas dynamic light scattering gave a Z-average hydrodynamic diameter of approximately 96-97 nm. The zeta potential was -30.9 mV. Fourier transform infrared spectroscopy detected oxygen-containing bands consistent with sinapic acid-derived species associated with the recovered material, although these data alone do not prove a capping mechanism. In cell-free assays, Sin-AgNPs inhibited α-amylase and α-glucosidase, with IC50 values of 2.01 ± 0.17 and 5.89 ± 0.43 µg/mL, respectively. Under the same assay conditions, acarbose gave IC50 values of 18.55 ± 1.40 and 253.40 ± 5.14 µg/mL, respectively. Sin-AgNPs also produced measurable responses in 2,2-diphenyl-1-picrylhydrazyl (DPPH), 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), and ferrous-ion-chelation assays. Because residual free sinapic acid was not quantified, silver nitrate and free sinapic acid were not tested as direct controls, and cytotoxicity, long-term stability, and in vivo efficacy were not evaluated, the results support only preliminary antioxidant and diabetes-related enzyme-inhibition activity and warrant further controlled investigation.","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"1-9"},"PeriodicalIF":2.2,"publicationDate":"2026-09-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149075764","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Garlic processing for bioactive transformation and recovery: aging, emerging technologies, extraction, isolation, and functional applications. 大蒜的生物活性转化和恢复：老化，新兴技术，提取，分离和功能应用。

IF 2.2 4区生物学

Preparative Biochemistry & Biotechnology Pub Date : 2026-09-26 DOI: 10.1080/10826068.2026.2736618

Ajay Kumar Shakya, Kosei Yamauchi, Chandan Das

{"title":"Garlic processing for bioactive transformation and recovery: aging, emerging technologies, extraction, isolation, and functional applications.","authors":"Ajay Kumar Shakya, Kosei Yamauchi, Chandan Das","doi":"10.1080/10826068.2026.2736618","DOIUrl":"https://doi.org/10.1080/10826068.2026.2736618","url":null,"abstract":"The health-promoting potential of garlic stems largely from organosulfur compounds (OSCs), phenolics, and flavonoids that drive its antioxidant, anti-inflammatory, and antimicrobial activities. However, key bioactive precursors such as alliin and allicin are chemically unstable, limiting the direct use of fresh garlic in functional food and nutraceutical development. To overcome this, various aging and processing techniques, most notably those used to produce black garlic, have been developed to convert these labile compounds into more stable, bioavailable derivatives, creating value-added products with enhanced functional properties. This review synthesizes current research on the biochemical transformations that occur during garlic aging and treatment, emphasizing the way different processing technologies influence the extent of compound conversion while preserving bioactivity. It critically examines extraction and purification strategies to maximize the recovery of bioactive compounds from aged or treated garlic, as well as recent advances in the extraction, isolation, and analytical characterization of these phytochemicals. Furthermore, previous studies demonstrated that garlic processing alters its phytochemical composition, with higher levels of certain compounds (such as SAC, phenolics, and flavonoids) and lower levels of other unstable compounds (such as alliin and thiosulfinates). The changes are influenced by the type of garlic, heat, pH, moisture, and processing time. While the application of conventional and emerging extraction methods can enhance bioactive recovery, limited kinetic studies, process standardization, and solvent usage remain important challenges. Future studies are needed to investigate time-dependent studies, process standardization, green extraction, bioaccessibility, pilot-scale validation, techno-economic analysis, and environmental assessment for the development of functional and nutraceutical products from garlic.","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"1-24"},"PeriodicalIF":2.2,"publicationDate":"2026-09-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149064091","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Production and applications of a microbial protease for silver biostripping and biorefining slaughterhouse by-products. 一种用于银生物剥离和生物精制屠宰场副产品的微生物蛋白酶的生产和应用。

IF 2.2 4区生物学

Preparative Biochemistry & Biotechnology Pub Date : 2026-09-22 DOI: 10.1080/10826068.2026.2736614

Rodrigo Almeida de Lima, Juliano Backes Scherer, Bruna Willig Kopplin, Rafael Franco Pires, Daniel Joner Daroit

{"title":"Production and applications of a microbial protease for silver biostripping and biorefining slaughterhouse by-products.","authors":"Rodrigo Almeida de Lima, Juliano Backes Scherer, Bruna Willig Kopplin, Rafael Franco Pires, Daniel Joner Daroit","doi":"10.1080/10826068.2026.2736614","DOIUrl":"https://doi.org/10.1080/10826068.2026.2736614","url":null,"abstract":"Waste radiographic films are hazardous materials, and methods for recycling the silver contained therein raise environmental concerns. Concurrently, slaughterhouse by-products remain underutilized, causing ecological impacts upon inadequate disposal. Therefore, a crude protease from Bacillus pumilus CL33A was evaluated for recovering silver from X-ray films and generating bioactive hydrolysates from slaughterhouse by-products. Protease was obtained via a 4-day submerged fermentation using chicken viscera meal (VM) as non-conventional substrate, and culture supernatants also showed enhanced antioxidant activities. The crude protease (0-80% dilutions) stripped the gelatin-silver emulsion from X-ray films in 4.3-9.4 min (55 °C), while chemical removal took 8.7 min. Enzyme preparations remained effective for three removal cycles (6.4-12.5 min), and biostripped silver formed colloidal suspensions. Furthermore, the crude protease hydrolyzed porcine liver, kidneys, lungs, spleen, VM, and blood meal (4 h; 55 °C), significantly increasing radical-scavenging (1.3- to 4.2-fold), Fe2+-chelating (1.2- to 1.5-fold), and reducing power (1.4- to 4.9-fold) abilities compared to non-hydrolyzed controls. Time-course monitoring demonstrated that a 3-h hydrolysis period sufficed to obtain VM hydrolysates with maximal antioxidant activities. Thus, bacterial processing of a low-cost biomass yields a multi-purpose protease (and antioxidants as co-products), whose applications offer cleaner, sustainable opportunities to advance bio-based frameworks for material and nutrient recycling.","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"1-9"},"PeriodicalIF":2.2,"publicationDate":"2026-09-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149025952","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Microbial proteases for sustainable protein-waste valorization and circular bioeconomy. 微生物蛋白酶在蛋白质废物可持续增值和循环生物经济中的应用。

IF 2.2 4区生物学

Preparative Biochemistry & Biotechnology Pub Date : 2026-09-21 DOI: 10.1080/10826068.2026.2734549

Nazneen Nasir, Kratika Naik, Melvin Vincent Dsouza, Sahar Banu Soudagar, Manjunath P Eelager, Suneel Dodamani, M Parthasarathy, Nagarjuna Prakash Dalbanjan

{"title":"Microbial proteases for sustainable protein-waste valorization and circular bioeconomy.","authors":"Nazneen Nasir, Kratika Naik, Melvin Vincent Dsouza, Sahar Banu Soudagar, Manjunath P Eelager, Suneel Dodamani, M Parthasarathy, Nagarjuna Prakash Dalbanjan","doi":"10.1080/10826068.2026.2734549","DOIUrl":"https://doi.org/10.1080/10826068.2026.2734549","url":null,"abstract":"Microbial proteases are among the most commercially important enzyme groups, contributing approximately 20% of the global industrial enzyme market because of their broad substrate specificity, operational robustness, and cost-effectiveness. These enzymes catalyze peptide bond hydrolysis under mild and environmentally benign conditions, supporting cleaner manufacturing and circular bioeconomy strategies. This review focuses on the production, engineering, and industrial application of microbial proteases, with particular emphasis on the valorization of protein-rich agro-industrial, food, and animal-processing residues generated in multi-million-ton quantities annually. The review adopts a circular bioprocessing perspective that links protease performance with waste-stream conversion, process integration, and resource-efficiency outcomes. Applications in food and feed processing, detergent formulations, leather processing, and protein hydrolysate production are critically discussed in the context of sustainable industrial processing. Advances in enzyme engineering, secretion and production optimization, and integrated bioprocess design are examined alongside key technical and economic constraints. Future progress will depend on the development of robust proteases, intensified and continuous processing platforms, and decentralized waste-to-value systems supported by improved process monitoring and standardized product characterization.","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"1-26"},"PeriodicalIF":2.2,"publicationDate":"2026-09-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149017451","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Immobilized enzymes in continuous biotransformations: advances, challenges, and engineering perspectives for scalable biocatalytic processes. 固定化酶在连续生物转化：进展，挑战，和工程前景的可扩展的生物催化过程。

IF 2.2 4区生物学

Preparative Biochemistry & Biotechnology Pub Date : 2026-09-16 DOI: 10.1080/10826068.2026.2726322

Ruby Mishra, Dayalan J, Sathish S, Ranjeet Kumar, Aravindan Munusamy Kalidhas, Shilpa Ashutosh Pathak, Subhaprada Dash, Aseel Smerat, Kamakshi Priya Kumar

{"title":"Immobilized enzymes in continuous biotransformations: advances, challenges, and engineering perspectives for scalable biocatalytic processes.","authors":"Ruby Mishra, Dayalan J, Sathish S, Ranjeet Kumar, Aravindan Munusamy Kalidhas, Shilpa Ashutosh Pathak, Subhaprada Dash, Aseel Smerat, Kamakshi Priya Kumar","doi":"10.1080/10826068.2026.2726322","DOIUrl":"https://doi.org/10.1080/10826068.2026.2726322","url":null,"abstract":"Immobilized enzymes have become central to continuous biotransformations by enabling catalyst recovery, repeated utilization, simplified product separation, and stable long-term reactor operation. This study critically evaluates how immobilization strategies, support architectures, reactor configurations, and reaction media collectively govern enzyme stability, mass transfer, catalytic efficiency, and process productivity in continuous biocatalytic systems. Recent advances in adsorption, covalent immobilization, entrapment, encapsulation, cross-linked enzyme aggregates (CLEAs), membrane reactors, packed-bed reactors, monolithic reactors, and structured flow platforms are systematically assessed with emphasis on industrially relevant performance metrics. The analysis demonstrates that although immobilization substantially enhances operational stability and catalyst lifetime, overall process performance is dictated by the interplay between enzyme orientation, support microstructure, pore diffusion, substrate and product transport, water activity, cofactor availability, product inhibition, enzyme leaching, fouling, and hydrodynamic limitations. Despite significant progress, meaningful comparison across studies remains constrained by inconsistent reporting of key process parameters, including enzyme loading, immobilization efficiency, residence time, space-time yield (STY), turnover number (TON), operational half-life, catalyst productivity, pressure drop, and time-on-stream stability. The study identifies critical knowledge gaps in mechanistic understanding, standardized performance evaluation, and long-duration continuous operation. It proposes an integrated framework that combines rational immobilization design with transport modeling, in situ reaction diagnostics, and cofactor engineering.","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"1-19"},"PeriodicalIF":2.2,"publicationDate":"2026-09-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148983505","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Green and sustainable enzyme-assisted extraction of antidiabetic phytochemicals: current trends and future prospects. 绿色可持续的酶辅助提取抗糖尿病植物化学物质：现状和前景。

IF 2.2 4区生物学

Preparative Biochemistry & Biotechnology Pub Date : 2026-09-15 DOI: 10.1080/10826068.2026.2716078

Deepak Kumar Verma, Pawan Prabhakar, Basant Kumar Dadrwal, Smita Singh, Alok Kumar Gupta, Ami R Patel, Prem Prakash Srivastav, Cristobal Noe Aguilar

{"title":"Green and sustainable enzyme-assisted extraction of antidiabetic phytochemicals: current trends and future prospects.","authors":"Deepak Kumar Verma, Pawan Prabhakar, Basant Kumar Dadrwal, Smita Singh, Alok Kumar Gupta, Ami R Patel, Prem Prakash Srivastav, Cristobal Noe Aguilar","doi":"10.1080/10826068.2026.2716078","DOIUrl":"https://doi.org/10.1080/10826068.2026.2716078","url":null,"abstract":"Diabetes mellitus is a critical global metabolic disorder that leads to serious complications and increasingly burdens healthcare systems. While people widely use traditional antidiabetic medications, long-term use often results in side effects, drug resistance, and increased costs. As a result, medicinal plants rich in bioactive phytochemicals such as alkaloids, phenolics, terpenoids, phytosterols, and cardiac glycosides are being explored as safer, more effective alternatives. These compounds offer diverse pharmacological benefits, including inhibition of α-amylase and α-glucosidase, stimulation of insulin secretion, regeneration of β-cells, antioxidant effects, and improvement of diabetes-related complications. However, efficient extraction of these bioactives remains challenging due to the use of toxic solvents, high temperatures, and poor selectivity in conventional methods. Enzyme-assisted extraction (EAE) has emerged as an eco-friendly, cost-effective, and efficient technique. EAE employs hydrolytic enzymes like cellulase, pectinase, and hemicellulose to break down plant cell walls, leading to greater phytochemical release. Benefits include higher yields, reduced solvent and energy use, shorter extraction times, and improved extract quality. This review critically examines antidiabetic phytochemicals, the mechanisms and key operational parameters of EAE, the specific roles of hydrolytic enzymes, recent experimental advances, industrial scalability challenges, and sustainability considerations, thereby outlining current trends and future prospects for the green, large-scale production of herbal antidiabetic agents.","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"1-24"},"PeriodicalIF":2.2,"publicationDate":"2026-09-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148970625","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0