Biotechnology and applied biochemistry最新文献

{"title":"Development and Validation of an ELISA Method for Quantification of HuB01 in Fermentation Products.","authors":"Yuying Liu, Yao Zhang, Ling Li, Dan Chen, Zengmin Yang, Yun Liu, Xinyu Yu, Yongjiang Liu, Haijiang Zhang","doi":"10.1002/bab.70183","DOIUrl":"10.1002/bab.70183","url":null,"abstract":"<p><strong>Background: </strong>The antibodies (including 7C4, 8D1) are neutralizing antibodies specifically targeting the protein RBD, a key core of the combination with angiotensin-converting enzyme 2 (ACE2). In order to measure HuB01 in fermentation products accurately, a bioanalytical method was needed, which should have high selectivity and be free from interference by 501Y.V2.</p><p><strong>Methods and results: </strong>To quantify HuB01 in fermentation products, an indirect ELISA was developed and validated, utilizing anti-idiotypic monoclonal antibodies for both capture and detection. The assay demonstrates high sensitivity, with a lower limit of quantification set at 3.906 ng/mL, a wide dynamic range spanning 3906-125 ng/mL for HuB01, and outstanding precision and accuracy.</p><p><strong>Conclusion: </strong>A sensitive and selective method for measuring HuB01 in fermentation products has been developed and validated by us. Currently, this assay is applied in the quality control of the production process.</p>","PeriodicalId":9274,"journal":{"name":"Biotechnology and applied biochemistry","volume":" ","pages":"2433-2440"},"PeriodicalIF":2.5,"publicationDate":"2026-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148238856","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}

{"title":"A Biologically Active Yellow Pigment From Micrococcus luteus (PX673990), Production, Extraction, Purification, Characterization, and Application in Textile and Paper Dyeing.","authors":"Minakshi Chakraborty, Royee Santra, Jayati Bhowal","doi":"10.1002/bab.70186","DOIUrl":"10.1002/bab.70186","url":null,"abstract":"<p><p>Microbes are a potential source of bio-pigments, offering safe and cost-effective alternatives to synthetic dyes. This study demonstrates the utilization of orange peel waste as a cost-effective substrate for pigment production by Micrococcus luteus. The nucleotide sequence of M. luteus, with 99.9% similarity, was deposited in GenBank under the accession number PX673990. The microbial pigment was further partially purified, yielding 14.94 ± 0.09 µg/mL of crude pigment under optimized conditions and 2.4 mg/L at partially purified conditions. High-performance liquid chromatography (HPLC) analysis demonstrated two prominent, broad peaks at 2.060 and 2.423 min, suggesting the presence of an oxygenated carotenoid-like compound. Furthermore, Fourier transform infrared (FTIR) and combined ¹H and ¹³C nuclear magnetic resonance spectra have suggested that the pigment is similar to a glycosylated carotenoid-like compound with esterified fatty acids. The x-ray diffraction (XRD) patterns exhibit sharp peaks between 17° and 28°, indicating the high crystallinity of the purified pigment. Furthermore, the partially purified pigment can scavenge 42.44% ± 0.03% of 1,1-diphenyl-2-picrylhydrazyl (DPPH) and 37.245% ± 0.05% of ABTS. This partially purified yellow pigment has been applied to various textiles and paper for dyeing. Different fastness properties, resistance to rubbing, washing, light, and temperature, were also evaluated. This study suggests that the bio-pigment obtained from the M. luteus strain PPIOR 1 (PX673990) exhibits effective dyeing properties. It also suggests that this pigment could be used as a sustainable, bio-based dye for the textile and paper industries in the near future. Further, its ability to produce at low cost and its various substrate affinities effectively substitute the synthetic dyes.</p>","PeriodicalId":9274,"journal":{"name":"Biotechnology and applied biochemistry","volume":" ","pages":"2482-2495"},"PeriodicalIF":2.5,"publicationDate":"2026-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148435195","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}

{"title":"Inducer Optimization Enhances Rhodotorula mucilaginosa Lipase for Biodetergent Application.","authors":"Ika Rahmatul Layly, Catur Sriherwanto, Siswa Setyahadi, Edi Wahjono, Dewi Nandyawati, Kharis Yohan Abidin, Erma Widyasti, Muhammad Irfan","doi":"10.1002/bab.70211","DOIUrl":"https://doi.org/10.1002/bab.70211","url":null,"abstract":"<p><p>Biodetergents represent sustainable alternatives to conventional chemical detergents, with lipases playing a key role in the removal of lipid-based stains. This study aimed to optimize inducer conditions for enhanced lipase production by Rhodotorula mucilaginosa and to evaluate the enzyme's suitability for biodetergent applications. Lipase production was carried out in Yeast Nitrogen Base Broth supplemented with 1% (v/v) different oil inducers under varying pH, temperature, and incubation time conditions. The highest lipase activity during production was achieved using olive oil and used cooking oil as inducers, reaching 3.80 and 3.75 U/mL, respectively, at 72 h, pH 6, and 30°C. Biochemical characterization showed that the lipase exhibited optimal activity at pH 8 and 42°C, with a maximum activity of 3.25 U/mL, and retained substantial stability under detergent-relevant conditions. Enzyme activity was enhanced in the presence of Mg²⁺, reaching 4.67 U/mL, whereas Zn²⁺ and Ba²⁺ strongly inhibited activity. In washing performance tests, R. mucilaginosa lipase achieved 29.40% oil removal, compared to 9.90% in the control and 54.53% for commercial Thermomyces lanuginosus lipase. These results demonstrate that inducer optimization significantly improves lipase production and highlight the potential of R. mucilaginosa lipase for biodetergent applications.</p>","PeriodicalId":9274,"journal":{"name":"Biotechnology and applied biochemistry","volume":" ","pages":""},"PeriodicalIF":2.5,"publicationDate":"2026-09-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149036316","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}

{"title":"Stabilization by Crosslinking of β-Galactosidase Immobilized by Adsorption for Application in a Continuous Lactose Removal Process.","authors":"Aliou Toro Lafia, Adrielle Aparecia Paulista Ribeiro, Larissa Nayhara Soares Santana Falleiros, Carla Zanella Guidini","doi":"10.1002/bab.70214","DOIUrl":"https://doi.org/10.1002/bab.70214","url":null,"abstract":"<p><p>Adsorption is the simplest method of enzyme immobilization, but it often requires additional treatments to improve stability. These treatments, however, may impact enzymatic activity. This study investigated the effect of crosslinking on the stability of β-galactosidase immobilized by adsorption on A-568 resin and its implications for enzymatic activity. The immobilized enzyme was crosslinked with different concentrations of glutaraldehyde (0.50% to 0.80% v/v). Parameters such as thermal stability (30°C to 60°C), stability during consecutive reuse, and storage stability for 90 days at different pH values (3-8) were evaluated. The feasibility of using the immobilized enzyme in an industrial process was also evaluated, an aspect that is not usually addressed. The conversion capacity was evaluated in a continuous reactor at different feed flow rates (4-10 mL/min). The results showed that crosslinking with glutaraldehyde (0.50%) provided greater stability for the enzyme adsorbed on the resin, which retained more than 90% of its initial activity at the end of the consecutive use cycle. Crosslinking improved the thermal stability of the enzyme, and its half-life was more than doubled at all temperatures. Storage conditions affected the non-crosslinked enzyme more, which showed intolerance to pH extremes, losing more than 60% of its initial activity at pH 3, 7, and 8, while the crosslinked enzyme retained more than 70% of its initial activity at all pH values after 90 days. Both enzymes showed great potential for industrial use in continuous processes. Although the cross-Linked enzyme showed high operational stability, its lactose conversion was low.</p>","PeriodicalId":9274,"journal":{"name":"Biotechnology and applied biochemistry","volume":" ","pages":""},"PeriodicalIF":2.5,"publicationDate":"2026-09-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149029847","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}

{"title":"Investigation of the Tyrosine Phosphatase Activity of Cps2D From Streptococcus suis Serotype 2.","authors":"Jiawen Ping, Bingbing Lu, Jingwen Liu, Li Zhang, Chengliang Tang, Yutao Wang, Xiuzhen Pan, Feng Zheng, Hua Ni","doi":"10.1002/bab.70213","DOIUrl":"https://doi.org/10.1002/bab.70213","url":null,"abstract":"<p><p>Streptococcus suis serotype 2 (S. suis 2) is an important zoonotic pathogen, with its capsular polysaccharide (CPS) serving as a key virulence factor. However, the regulatory mechanisms of CPS biosynthesis remain unclear. This study aimed to prepare and characterize the capsular synthesis regulatory factor Cps2D from S. suis 2 and investigate its enzymatic activity. Bioinformatics analysis using ProtParam and Alpha Fold revealed Cps2D as a hydrophilic, stable protein of 242 amino acids, with a molecular weight of 28 kDa and a pI of 8.69. It was annotated as a tyrosine protein phosphatase, primarily composed of α-helices and random coils, and structurally homologous to the protein model 3qy8.1.A, suggesting potential interactions with glycosyltransferases involved in capsule synthesis. The cps2D gene was amplified from S. suis 2 strain 05ZYH33 and cloned into the pET30a vector, and the recombinant protein was successfully purified via Ni²⁺-NTA affinity chromatography and confirmed by SDS-PAGE and Western blot. Enzymatic characterization using p-nitrophenyl phosphate as a substrate showed that purified Cps2D exhibited phosphatase activity of 81.64 ± 0.72 U/L. The enzyme showed maximal activity at pH 10.0 and 37°C. Among the divalent metal ions tested, Mg² ⁺ produced the strongest stimulatory effect, with 5 mM Mg² ⁺ yielding the highest activity. Kinetic analysis under optimized conditions gave a K_m of 1.367 mM, V_max of 1.012 × 10^- ² mM min^- ¹, K_cat of 0.4819 min^- ¹, and K_cat/K_m of 0.3525 min^- ¹ mM^- ¹. These results establish a soluble prokaryotic expression and purification strategy for Cps2D and provide the first biochemical evidence supporting its phosphatase activity in vitro. The purified recombinant protein will facilitate future structural and mechanistic studies of phosphorylation-dependent regulation of capsule-associated proteins in S. suis serotype 2.</p>","PeriodicalId":9274,"journal":{"name":"Biotechnology and applied biochemistry","volume":" ","pages":""},"PeriodicalIF":2.5,"publicationDate":"2026-09-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149015751","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}

{"title":"Biobased Sunflower Stalk Matrix for Lipase Stabilization via Physical Adsorption.","authors":"Jaci L Vilanova Neta, Larissa O Jesus, Sande A S Costa, Edélvio B Gomes, Rita C M Miranda, Daniel P Silva, Denise S Ruzene, Cleide M F Soares, Álvaro S Lima","doi":"10.1002/bab.70209","DOIUrl":"https://doi.org/10.1002/bab.70209","url":null,"abstract":"<p><p>The search for sustainable, cost-effective biocatalytic processes has driven efforts to develop low-cost supports for enzyme immobilization. Lignocellulosic residues have received particular attention due to their abundance, renewability, and structural properties. Despite the growing interest in lignocellulosic residues as enzyme supports, sunflower stalks remain largely unexplored for lipase immobilization. This study aims to evaluate the use of sunflower stalks (Helianthus annuus L.), in natura and after alkaline and hydrothermal pretreatments, as supports for the immobilization of Burkholderia cepacia lipase by physical adsorption. Pretreatment improved enzyme performance, increasing thermal stability by up to 4.28-fold compared to the free enzyme. The biocatalysts prepared using alkaline-treated, hydrothermal-treated, in natura supports, and free enzyme showed half-life values of 19.95, 16.86, 10.25, and 4.66 h, respectively. Immobilization also enhanced enzyme reusability, particularly for the alkaline-treated support, which maintained activity for up to six operational cycles. Kinetic analysis of the immobilized enzyme showed reduced V_max and apparent K_m values, suggesting changes in enzyme-substrate interactions and possible diffusion limitations. These results indicate that pretreatment plays an important role in modifying the physicochemical properties of sunflower stalks, directly affecting the stability and reusability of the biocatalyst. Overall, this study highlights the potential of sunflower stalk residues as a low-cost and effective support with improved catalytic performance and operational stability.</p>","PeriodicalId":9274,"journal":{"name":"Biotechnology and applied biochemistry","volume":" ","pages":""},"PeriodicalIF":2.5,"publicationDate":"2026-09-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149015750","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}

{"title":"Enhanced and Optimized Production of Cellulase Using Trichoderma harzianum through the Utilization of Pretreated Lignocellulosic Wastes: Purification, Characterization, and Industrial Applications.","authors":"Hifza Rahat, Ieshmal M Hashmi, Sarwat Ismail, Duaa Qaiser, Sibtain Ahmed, Tahir Mehmood","doi":"10.1002/bab.70207","DOIUrl":"https://doi.org/10.1002/bab.70207","url":null,"abstract":"<p><p>In the current study, various Aspergillus and Trichoderma strains were explored to produce cellulase using a variety of agricultural wastes as cheaper substrates. Among the tested strains, Trichoderma harzianum exhibited the highest enzyme activity (84.0 FPU/mL) when grown on alkali-pretreated sugarcane bagasse after purification. Out of three substrates, pretreated sugarcane bagasse consistently resulted in higher cellulase activity (42.05 FPU/mL) as compared to wheat straw (26.5 FPU/mL) and wheat bran (16.7 FPU/mL) across all tested strains due to its high cellulose/hemicellulose content and low lignin levels in proximate analysis. Central Composite Design Response Surface Methodology was employed in Minitab software to optimize solid-state fermentation parameters, achieving 76.2 FPU/mL activity in T. harzianum at pH 5.5, 28°C, 68% moisture, 0.5 mL inoculum, 5 g substrate with 5 days' incubation time as compared to Aspergillus fumigatus (57.2 FPU/mL). Stepwise ammonium sulfate precipitation (60%-80%) followed by dialysis and gel chromatography increased specific activity to 84.00 FPU/mg, with a purification fold of 5.51 and a 22.0% yield, whereas SDS-PAGE further confirmed enzyme homogeneity. The purified cellulase exhibited maximum relative activity at 50°C and pH 4 in the characterization study. The activity was strongly inhibited by Hg² ⁺, while the activity loss was very small in the presence of Ca² ⁺ and Mg² ⁺. The enzyme kinetic resulted in a <math><msub><mi>V</mi> <mi>max</mi></msub> </math> of 103.89 U/mL and a <math><msub><mi>K</mi> <mi>m</mi></msub> </math> of 3.71 mg/mL by nonlinear Michaelis-Menten regression. First-order thermal inactivation showed k_d value increasing from 0.000250 to 0.002900 min^- ¹, E_d (72.5 kJ/mol), and z (28.3°C). These results indicated that the optimized and purified enzyme still had high catalytic activity toward carboxymethyl cellulose (CMC). Industrial applicability was demonstrated through bio-polishing of cotton fabric, resulting in improved surface smoothness and a 3.8% weight loss, comparable to that of standard cellulase. Compatibility with various commercial detergents showed the highest level of activity, increasing from 69% to 97% in Surf Excel. This finding offers a cost-effective design for enzyme production using large amounts of lignocellulose byproducts, which can meet industry needs while also managing the disposal of agricultural wastes, etc.</p>","PeriodicalId":9274,"journal":{"name":"Biotechnology and applied biochemistry","volume":" ","pages":""},"PeriodicalIF":2.5,"publicationDate":"2026-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148988106","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}

{"title":"Novel Ferulic Acid Esterase From Human Gut Microbiome: Cloning and Application in Crop Residue Valorization.","authors":"Saarika Pothuvan Kunnummal, Aneesha Abdulla, Mahejibin Khan","doi":"10.1002/bab.70208","DOIUrl":"https://doi.org/10.1002/bab.70208","url":null,"abstract":"<p><p>Ferulic acid esterases (FAEs) are enzymes that interact with esterified components of plant cell walls, facilitating the release of free ferulic acid (FA) from plant materials. Therefore, they hold significant importance across multiple industries, including pharma, food, and cosmetics. This investigation involved the cloning, expression, and characterization of FAE from the human fecal metagenome. Sequence analysis revealed that the cloned gene was approximately 750 bp in length and contained an open reading frame encoding a protein of 252 amino acids. The resulting recombinant protein displayed a molecular weight of 28 kDa and 49.7% identity with the chlorogenic acid esterase from Lactobacillus helveticus. The hydrolytic activity of the recombinant FAE was validated using p-nitrophenyl-ferulate (pNPF) as the substrate, with optimal activity at a pH of 7 and a temperature of 35°C. The enzyme showed stability within a pH range of 5.0-7.0 and temperatures from 5°C to 35°C. High-performance liquid chromatography (HPLC) results indicated that the FAE enzyme could release up to 49.7% of total alkali-extractable FA from dehydrated rice bran, followed by wheat bran and sugarcane bagasse. The total phenolic content of sugarcane bagasse increased by approximately 100% after in situ enzymatic fermentation compared with the chemically extracted fraction. These results indicate that cloned FAE can be used as a potential biocatalyst in industrial applications.</p>","PeriodicalId":9274,"journal":{"name":"Biotechnology and applied biochemistry","volume":" ","pages":""},"PeriodicalIF":2.5,"publicationDate":"2026-09-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148975940","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}

{"title":"Integrated Algal Biorefineries for Biofuel and Bioplastic Co-Production: Process Performance, Circularity, and Scale-Up.","authors":"Senthil Kumar S, Bharani Kumar S, Srinivas J, Ashok Kumar R, Ravikumar Jayabal, Prajith Prabhakar","doi":"10.1002/bab.70210","DOIUrl":"https://doi.org/10.1002/bab.70210","url":null,"abstract":"<p><p>Algal biorefineries provide a platform for producing fuels, biodegradable materials, and higher-value co-products from the same biomass resource. This review examines integrated pathways that connect microalgal and macroalgal cultivation with biodiesel production, hydrothermal liquefaction (HTL), anaerobic digestion (AD), polysaccharide extraction, and bioplastic manufacture. Microalgal lipid contents of 40%-70% of dry biomass can support biodiesel production, whereas hydrothermal processing of wet biomass has produced bio-crude yields of 30-50 wt% with energy densities of approximately 35-40 MJ/kg. Macroalgal polysaccharides, including alginate, agar, and carrageenan, can be processed into films, blends, and composites with reported tensile strengths of 18-45 MPa. However, the environmental and economic performance of these routes depends on cultivation configuration, dewatering requirements, product recovery, allocation method, and system boundary. Published techno-economic estimates place stand-alone algal biodiesel production at approximately USD 4-7 gal^-1. In contrast, integrated scenarios can approach USD 2.50 gal^-1 when favorable biomass productivity and co-product credits are assumed. Machine-learning (ML) methods have mainly been applied to laboratory data analysis and process prediction, while evidence of commercial real-time control remains limited. The review identifies mass-balance reporting, long-duration outdoor cultivation, standardized biodegradation testing, and harmonized techno-economic and life-cycle assessment as priorities for scale-up.</p>","PeriodicalId":9274,"journal":{"name":"Biotechnology and applied biochemistry","volume":" ","pages":""},"PeriodicalIF":2.5,"publicationDate":"2026-09-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148929040","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}

{"title":"Valorization of Textile Waste: Enzymatic Upcycling of Terephthalic Acid Toward a Sustainable PET Value Chain.","authors":"Fares Al-Ostoot, Loredano Pollegioni, Elena Rosini","doi":"10.1002/bab.70205","DOIUrl":"https://doi.org/10.1002/bab.70205","url":null,"abstract":"<p><p>The rapid expansion of the global textile industry, driven by the fast-fashion paradigm, which is characterized by low-cost, short-lived garments made from inexpensive synthetic fibers, has intensified environmental pressures through increased waste generation, resource depletion, microplastic pollution, and greenhouse gas emissions. Conventional polyethylene terephthalate (PET) recycling remains limited by high energy demands, harsh processing conditions, and the generation of low-value products. This review examines emerging upcycling strategies targeting PET-derived monomers, including terephthalic acid (TPA) and ethylene glycol, with particular emphasis on converting TPA into high-value chemicals, functional materials, and specialty polymers. By integrating biological and materials engineering approaches, these strategies offer a transformative pathway for converting textile waste into value-added products, thereby supporting the development of a circular and sustainable PET economy. Unlike previous surveys, this work focuses on the upcycling of TPA, providing a critical evaluation of how advanced protein engineering is driving improvements in enzymatic depolymerization and bioconversion pathways toward high-value products, thereby filling a key gap in existing research, which is predominantly centered on primary recycling approaches.</p>","PeriodicalId":9274,"journal":{"name":"Biotechnology and applied biochemistry","volume":" ","pages":""},"PeriodicalIF":2.5,"publicationDate":"2026-09-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148891023","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}