{"title":"Corrigendum to \"Effects of overexpression of the human intestinal alkaline phosphatase gene on the expression of related genes in intestinal epithelium-like cells\" [Enzyme Microb. Technol. 195 (2026) 110807].","authors":"Seiko Noda, Shiho Ishii, Asako Yamada, Sadako Matsui, Hideo Orimo, Masae Goseki-Sone","doi":"10.1016/j.enzmictec.2026.110820","DOIUrl":"10.1016/j.enzmictec.2026.110820","url":null,"abstract":"","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":" ","pages":"110820"},"PeriodicalIF":3.7,"publicationDate":"2026-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146044006","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-01-30DOI: 10.1016/j.enzmictec.2026.110822
Huanhuan Li, Yao Wang, Kun Wang, Li Xu, Wenyue Liu, Lingfang Gu, Xiaoman Xie, Yunjun Yan
Poor thermal stability of Rhizopus oryzae lipase (ROL) has long limited its industrial applicability. In this study, we systematically investigated the underlying mechanism for its inactivation and correspondingly developed an effective stabilization strategy. Kinetic analyses revealed that ROL thermal inactivation process followed a two-step model, demonstrating its inactivation proceeds a distinct intermediate state. Various spectroscopic characterizations further suggested that activity loss was closely associated with the progressive unfolding of the enzyme, as evidenced by the disruption of secondary structures and a pronounced increase in fluorescence intensity resulting from the exposure of hydrophobic clusters. To enhance its thermostability, based on the above-discovered mechanism, a compound stabilizer system was developed and further optimized via a combination of Plackett-Burman design and response surface methodology. The obtained optimal formula comprised of 35.94 % (m/v) glucose, 34.82 % (m/v) sorbitol, and 2.50 mol/L NaCl, which could effectively preserve 97.7 % of the initial activity after 3 h of incubation at 60 °C, in contrast to only 29.5 % residual activity of the control. Thus, this study elucidated the underlying thermal inactivation mechanism for ROL and developed a practical and efficient stabilization strategy with potential prospect for industrial application.
{"title":"The underlying thermal inactivation mechanism and corresponding effective stabilization strategy for Rhizopus oryzae lipase.","authors":"Huanhuan Li, Yao Wang, Kun Wang, Li Xu, Wenyue Liu, Lingfang Gu, Xiaoman Xie, Yunjun Yan","doi":"10.1016/j.enzmictec.2026.110822","DOIUrl":"https://doi.org/10.1016/j.enzmictec.2026.110822","url":null,"abstract":"<p><p>Poor thermal stability of Rhizopus oryzae lipase (ROL) has long limited its industrial applicability. In this study, we systematically investigated the underlying mechanism for its inactivation and correspondingly developed an effective stabilization strategy. Kinetic analyses revealed that ROL thermal inactivation process followed a two-step model, demonstrating its inactivation proceeds a distinct intermediate state. Various spectroscopic characterizations further suggested that activity loss was closely associated with the progressive unfolding of the enzyme, as evidenced by the disruption of secondary structures and a pronounced increase in fluorescence intensity resulting from the exposure of hydrophobic clusters. To enhance its thermostability, based on the above-discovered mechanism, a compound stabilizer system was developed and further optimized via a combination of Plackett-Burman design and response surface methodology. The obtained optimal formula comprised of 35.94 % (m/v) glucose, 34.82 % (m/v) sorbitol, and 2.50 mol/L NaCl, which could effectively preserve 97.7 % of the initial activity after 3 h of incubation at 60 °C, in contrast to only 29.5 % residual activity of the control. Thus, this study elucidated the underlying thermal inactivation mechanism for ROL and developed a practical and efficient stabilization strategy with potential prospect for industrial application.</p>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"196 ","pages":"110822"},"PeriodicalIF":3.7,"publicationDate":"2026-01-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146112385","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
In the present study, the combinatory role of beta-cryptoxanthin (β-CRX) and novel biosurfactant (BS) produced by Kocuria marina DAGII was explored. Spectral analysis of biosurfactant showed a strong peak at 265 nm. Characterization of biosurfactant was performed using CHNSO (carbon, hydrogen, nitrogen, sulphur, and oxygen) and MALDI-TOF (matrix-assisted laser desorption ionization-time of flight) analysis. MALDI-TOF spectra showed an intense peak at 379.7 m/z, indicating the presence of structural components like sugars, lipids, and clusters of fragment ions closely related to rhamnolipid (glycolipid) like biosurfactant. CHNSO analysis of partially purified biosurfactant revealed the presence of nitrogen (4.675 %), carbon (30.815 %), hydrogen (7.417 %), and oxygen (25.428 %). A combination of BS and β-CRX demonstrated higher antioxidant activity compared to BS alone. The highest inhibition against Staphylococcus epidermidis MTCC 3615 and Pseudomonas aeruginosa MTCC 741 was observed for the combined effect of BS (32 mg/ml) and β-CRX (0.1 mg/ml). However, the lowest antibacterial activity was observed against Staphylococcus aureus MTCC 96 (0.3 ± 0.041 cm), likely due to its strong biofilm formation. Membrane integrity and permeability assays revealed enhanced activity against Gram-positive Staphylococcus epidermidis having OD260 value 1.23 ± 0.060 and OD420value 0.157 ± 0.01. The increased outer membrane permeability was assessed through the NPN uptake assay in Pseudomonas aeruginosa. Antibiofilm assay showed good antibiofilm activity (66.14 ± 0.13 %) against Staphylococcus epidermidis for combined effect of BS (32 mg/ml) and β-CRX (0.1 mg/ml). Overall, the study suggests that a combination of BS and β-CRX has promising potential as a dual antioxidant and antibacterial agent, particularly effective against these tested opportunistic skin pathogens.
{"title":"Dual antioxidant and antibacterial potential of β-cryptoxanthin and a novel biosurfactant from Kocuria marina DAGII","authors":"Daiji Brahma , Anwesha Mahanty , Prity Chatterjee , Riya Dey , Abheerup Sarker , Sagnik Kulavi , Debjani Dutta","doi":"10.1016/j.enzmictec.2026.110821","DOIUrl":"10.1016/j.enzmictec.2026.110821","url":null,"abstract":"<div><div>In the present study, the combinatory role of beta-cryptoxanthin (β-CRX) and novel biosurfactant (BS) produced by <em>Kocuria marina</em> DAGII was explored. Spectral analysis of biosurfactant showed <em>a</em> strong peak at 265 nm. Characterization of biosurfactant was performed using CHNSO (carbon, hydrogen, nitrogen, sulphur, and oxygen) and MALDI-TOF (matrix-assisted laser desorption ionization-time of flight) analysis. MALDI-TOF spectra showed an intense peak at 379.7 <em>m/z</em>, indicating the presence of structural components like sugars, lipids, and clusters of fragment ions closely related to rhamnolipid (glycolipid) like biosurfactant. CHNSO analysis of partially purified biosurfactant revealed the presence of nitrogen (4.675 %), carbon (30.815 %), hydrogen (7.417 %), and oxygen (25.428 %). A combination of BS and β-CRX demonstrated higher antioxidant activity compared to BS alone. The highest inhibition against <em>Staphylococcus epidermidis</em> MTCC 3615 and <em>Pseudomonas aeruginosa</em> MTCC 741 was observed for the combined effect of BS (32 mg/ml) and β-CRX (0.1 mg/ml). However, the lowest antibacterial activity was observed against <em>Staphylococcus aureus</em> MTCC 96 (0.3 ± 0.041 cm), likely due to its strong biofilm formation. Membrane integrity and permeability assays revealed enhanced activity against Gram-positive <em>Staphylococcus epidermidis</em> having OD<sub>260</sub> value 1.23 ± 0.060 and OD<sub>420</sub>value 0.157 ± 0.01. The increased outer membrane permeability was assessed through the NPN uptake assay in <em>Pseudomonas aeruginosa</em>. Antibiofilm assay showed good antibiofilm activity (66.14 ± 0.13 %) against <em>Staphylococcus epidermidis</em> for combined effect of BS (32 mg/ml) and β-CRX (0.1 mg/ml). Overall, the study suggests that a combination of BS and β-CRX has promising potential as a dual antioxidant and antibacterial agent, particularly effective against these tested opportunistic skin pathogens.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"196 ","pages":"Article 110821"},"PeriodicalIF":3.7,"publicationDate":"2026-01-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146071142","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Macroalgae are a sustainable, non-terrestrial biomass resource critical for the emerging blue economy. They play a crucial role in marine ecosystems, including the natural sequestration of carbon, which grounds the entire value chain in sustainable CO2 removal. This review presents how enzyme and microbial biotechnology drive the techno-economic feasibility of macroalgal processing within a circular biorefinery framework. We detail how tailored enzymatic cocktails enable the selective, mild-condition extraction and modification of high-value, mainstream products, such as hydrocolloids and nutraceuticals like omega-3 lipids, from the three major macroalgal groups. Concurrently, microbial bioconversion is crucial for transforming macroalgal components, including polysaccharides, proteins, and lipids, into byproducts such as biofuels and biofertilizers, thereby ensuring resource efficiency and minimizing waste. The application of molecular omics technologies (genomics, transcriptomics, proteomics, and metabolomics) is shown to underpin the macroalgal biology and optimize bioprocesses by identifying novel microbial strains, enzymes and engineering metabolic pathways of microbial strains to enhance yields and specificity. The study addresses technological, economic, and environmental difficulties. This integrated, cascading approach is necessary to transition macroalgae valorization from single-product extraction to a profitable, multi-product industry, balancing economic growth with environmental preservation. Critical assessment of the framework's overall environmental viability relies on life cycle analysis (LCA). This review contributes an essential methodological synthesis to guide future studies, ensuring consistent sustainability assessment of the macroalgal biorefinery.
{"title":"Harnessing enzyme and microbial biotechnology for macroalgae valorization: A circular economy approach with implications for carbon sequestration","authors":"Bharmjeet Singh , Mahesh Vemula , Abeba Haile Mariamenatu , Abdalah Makaranga , Asha Arumugam Nesamma , Pannaga Pavan Jutur","doi":"10.1016/j.enzmictec.2026.110819","DOIUrl":"10.1016/j.enzmictec.2026.110819","url":null,"abstract":"<div><div>Macroalgae are a sustainable, non-terrestrial biomass resource critical for the emerging blue economy. They play a crucial role in marine ecosystems, including the natural sequestration of carbon, which grounds the entire value chain in sustainable CO<sub>2</sub> removal. This review presents how enzyme and microbial biotechnology drive the techno-economic feasibility of macroalgal processing within a circular biorefinery framework. We detail how tailored enzymatic cocktails enable the selective, mild-condition extraction and modification of high-value, mainstream products, such as hydrocolloids and nutraceuticals like omega-3 lipids, from the three major macroalgal groups. Concurrently, microbial bioconversion is crucial for transforming macroalgal components, including polysaccharides, proteins, and lipids, into byproducts such as biofuels and biofertilizers, thereby ensuring resource efficiency and minimizing waste. The application of molecular omics technologies (genomics, transcriptomics, proteomics, and metabolomics) is shown to underpin the macroalgal biology and optimize bioprocesses by identifying novel microbial strains, enzymes and engineering metabolic pathways of microbial strains to enhance yields and specificity. The study addresses technological, economic, and environmental difficulties. This integrated, cascading approach is necessary to transition macroalgae valorization from single-product extraction to a profitable, multi-product industry, balancing economic growth with environmental preservation. Critical assessment of the framework's overall environmental viability relies on life cycle analysis (LCA). This review contributes an essential methodological synthesis to guide future studies, ensuring consistent sustainability assessment of the macroalgal biorefinery.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"195 ","pages":"Article 110819"},"PeriodicalIF":3.7,"publicationDate":"2026-01-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146009097","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
α-Glucosidase is in high demand for applications involving the digestion of α-configured glycoside and saccharide substrates. Areas of application include industrial processing in food/feed and chemistry, as well as medicine and analytics. With an analytical application for assaying α-amylase in mind, we conducted a study on the immobilization of α-glucosidases from Bacillus stearothermophilus and Saccharomyces cerevisiae on support materials based on polystyrene and polymethacrylate. The carriers had nine different surface functional groups: none (plain material), carboxylate, sulfate, thiol, hydroxy, amine, sulfonyl chloride, epoxy, and PEG300. Based on preliminary results obtained with polymer beads, we selected the α-glucosidase from B. stearothermophilus and polystyrene plates with surface functional groups for detailed studies on enzyme immobilization. Carrier activity (Ac), immobilized enzyme effectiveness (ƞ), and reusability were evaluated depending on protein loading. Sulfonyl chloride (-SO2Cl) showed efficient and stable immobilization (Ac up to 279 U/m2 carrier; ƞ 58 %; Ac after 6 uses, 171 U/m2 carrier). The α-glucosidase immobilized onto sulfonyl chloride-polystyrene carrier was used in an assay of α-amylase activity as a representative analytical application. 4-Nitrophenyl 4,6-ethylidene-α-D-maltoheptaoside was used as the chromogenic substrate in the α-amylase assay. The results indicated that the immobilized α-glucosidase was suitable for detecting α-amylase concentrations ranging from 0.1 µg/mL to 0.5 µg/mL (0.3 – 1.3 U/L as observed activities). Additionally, the results can be readily applied in a microtiter plate-based assay. Collectively, our results reveal the basic requirements for immobilizing α-glucosidase on polystyrene for the advancement of analytical assays.
{"title":"Immobilization of α-glucosidase on polystyrene plates: A practical application to α-amylase detection","authors":"Jihye Jung , Verónica Mora-Sanz , Nerea Briz , Bernd Nidetzky","doi":"10.1016/j.enzmictec.2026.110818","DOIUrl":"10.1016/j.enzmictec.2026.110818","url":null,"abstract":"<div><div>α-Glucosidase is in high demand for applications involving the digestion of α-configured glycoside and saccharide substrates. Areas of application include industrial processing in food/feed and chemistry, as well as medicine and analytics. With an analytical application for assaying α-amylase in mind, we conducted a study on the immobilization of α-glucosidases from <em>Bacillus stearothermophilus</em> and <em>Saccharomyces cerevisiae</em> on support materials based on polystyrene and polymethacrylate. The carriers had nine different surface functional groups: none (plain material), carboxylate, sulfate, thiol, hydroxy, amine, sulfonyl chloride, epoxy, and PEG300. Based on preliminary results obtained with polymer beads, we selected the α-glucosidase from <em>B. stearothermophilus</em> and polystyrene plates with surface functional groups for detailed studies on enzyme immobilization. Carrier activity (<em>A</em><sub>c</sub>), immobilized enzyme effectiveness (ƞ), and reusability were evaluated depending on protein loading. Sulfonyl chloride (-SO<sub>2</sub>Cl) showed efficient and stable immobilization (<em>A</em><sub>c</sub> up to 279 U/m<sup>2</sup> carrier; ƞ 58 %; <em>A</em><sub>c</sub> after 6 uses, 171 U/m<sup>2</sup> carrier). The α-glucosidase immobilized onto sulfonyl chloride-polystyrene carrier was used in an assay of α-amylase activity as a representative analytical application. 4-Nitrophenyl 4,6-ethylidene-α-<span>D</span>-maltoheptaoside was used as the chromogenic substrate in the α-amylase assay. The results indicated that the immobilized α-glucosidase was suitable for detecting α-amylase concentrations ranging from 0.1 µg/mL to 0.5 µg/mL (0.3 – 1.3 U/L as observed activities). Additionally, the results can be readily applied in a microtiter plate-based assay. Collectively, our results reveal the basic requirements for immobilizing α-glucosidase on polystyrene for the advancement of analytical assays.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"195 ","pages":"Article 110818"},"PeriodicalIF":3.7,"publicationDate":"2026-01-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145972933","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Alkaline phosphatase is an enzyme that hydrolyzes phosphate monoesters. Intestinal-type ALP (IAP), which localizes to the small intestine, is closely associated with dietary factors; however, its physiological functions remain largely unclear. Therefore, we herein hypothesized that the transient overexpression of the human Intestinal Alkaline Phosphatase (ALPI) gene, which encodes IAP, may suggest its effects on the expression of other related genes. Human intestinal epithelium-like Caco-2 cells were transfected with an IAP expression vector or a Mock control to induce transient overexpression. Three days later, Caco-2 cells were harvested and RNA was extracted. Using purified RNA, a comprehensive gene expression analysis was performed by RNA sequencing with next-generation sequencing technology. In comparisons with the Mock control, 1036 differentially expressed genes (DEGs) were identified in Caco-2 cells transfected with the human IAP expression vector. The expression of 79 of these genes was more than two-fold higher, while that of 74 of these genes was more than two-fold lower. The GO analysis of the 79 up-regulated genes demonstrated that seven genes were enriched in “nervous system development” and three genes in “negative chemotaxis”. In contrast, the GO analysis of the 74 down-regulated genes demonstrated that two genes were enriched in “membrane repolarization during atrial cardiac muscle cell action potential”, four genes in “cell surface receptor signaling pathway”, five genes were enriched in “neuron projection”, and three genes in “perikaryon”. Further studies are warranted to investigate the relationships between DEGs and the regulation of ALPI gene expression in more detail.
{"title":"Effects of overexpression of the human intestinal alkaline phosphatase gene on the expression of related genes in intestinal epithelium-like cells","authors":"Seiko Noda , Shiho Ishii , Asako Yamada , Sadako Matsui , Hideo Orimo , Masae Goseki-Sone","doi":"10.1016/j.enzmictec.2025.110807","DOIUrl":"10.1016/j.enzmictec.2025.110807","url":null,"abstract":"<div><div>Alkaline phosphatase is an enzyme that hydrolyzes phosphate monoesters. Intestinal-type ALP (IAP), which localizes to the small intestine, is closely associated with dietary factors; however, its physiological functions remain largely unclear. Therefore, we herein hypothesized that the transient overexpression of the human <em>Intestinal Alkaline Phosphatase</em> (<em>ALPI</em>) gene, which encodes IAP, may suggest its effects on the expression of other related genes. Human intestinal epithelium-like Caco-2 cells were transfected with an IAP expression vector or a Mock control to induce transient overexpression. Three days later, Caco-2 cells were harvested and RNA was extracted. Using purified RNA, a comprehensive gene expression analysis was performed by RNA sequencing with next-generation sequencing technology. In comparisons with the Mock control, 1036 differentially expressed genes (DEGs) were identified in Caco-2 cells transfected with the human IAP expression vector. The expression of 79 of these genes was more than two-fold higher, while that of 74 of these genes was more than two-fold lower. The GO analysis of the 79 up-regulated genes demonstrated that seven genes were enriched in “nervous system development” and three genes in “negative chemotaxis”. In contrast, the GO analysis of the 74 down-regulated genes demonstrated that two genes were enriched in “membrane repolarization during atrial cardiac muscle cell action potential”, four genes in “cell surface receptor signaling pathway”, five genes were enriched in “neuron projection”, and three genes in “perikaryon”. Further studies are warranted to investigate the relationships between DEGs and the regulation of <em>ALPI</em> gene expression in more detail.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"195 ","pages":"Article 110807"},"PeriodicalIF":3.7,"publicationDate":"2025-12-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145881449","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-12-31DOI: 10.1016/j.enzmictec.2025.110810
Tahseen Hameed Khlaif
This study presents a novel, synergistic bioremediation platform for petroleum-contaminated produced water, utilizing Alcanivorax borkumensis in conjunction with a hybrid nanocomposite of graphene quantum dots (GQDs), zinc oxide (ZnO), and lanthanum oxide (La₂O₃). The nanocomposite was synthesized via ultrasonic-assisted co-precipitation and hydrothermal methods, exhibiting high surface area and photocatalytic potential. The bacterium was isolated from oil-field equipment and identified based on 16S rRNA sequencing, showing selective affinity for hydrocarbons in saline conditions. Integrated systems were optimized by evaluating nanocomposite dose, contact time, and light intensity. Results revealed a clear synergy: GQDs enhanced bacterial adhesion and minimized cytotoxicity, while ZnO/La₂O₃ contributed to robust radical formation under light exposure. Combined systems achieved over 98 % total petroleum hydrocarbon (TPH) and 99 % polycyclic aromatic hydrocarbon (PAH) removal, outperforming individual components. Material characterizations (BET, FTIR, XRD, SEM) confirmed the composite’s stability and biointerface compatibility. Comparative trials across bacteria-only, nanomaterial-only, and hybrid systems validated the superiority of the bio-nanocomposite configuration. The approach merges enzymatic and photocatalytic degradation in a biologically resilient matrix, providing a scalable, environmentally sound strategy for industrial water treatment. These findings offer a comprehensive framework for future application of microbe–nanomaterial hybrids in complex pollutant removal.
{"title":"Integrated bio-nano remediation of produced water using Alcanivorax borkumensis and GQDs-modified ZnO/La₂O₃ nanocomposites","authors":"Tahseen Hameed Khlaif","doi":"10.1016/j.enzmictec.2025.110810","DOIUrl":"10.1016/j.enzmictec.2025.110810","url":null,"abstract":"<div><div>This study presents a novel, synergistic bioremediation platform for petroleum-contaminated produced water, utilizing <em>Alcanivorax borkumensis</em> in conjunction with a hybrid nanocomposite of graphene quantum dots (GQDs), zinc oxide (ZnO), and lanthanum oxide (La₂O₃). The nanocomposite was synthesized via ultrasonic-assisted co-precipitation and hydrothermal methods, exhibiting high surface area and photocatalytic potential. The bacterium was isolated from oil-field equipment and identified based on 16S rRNA sequencing, showing selective affinity for hydrocarbons in saline conditions. Integrated systems were optimized by evaluating nanocomposite dose, contact time, and light intensity. Results revealed a clear synergy: GQDs enhanced bacterial adhesion and minimized cytotoxicity, while ZnO/La₂O₃ contributed to robust radical formation under light exposure. Combined systems achieved over 98 % total petroleum hydrocarbon (TPH) and 99 % polycyclic aromatic hydrocarbon (PAH) removal, outperforming individual components. Material characterizations (BET, FTIR, XRD, SEM) confirmed the composite’s stability and biointerface compatibility. Comparative trials across bacteria-only, nanomaterial-only, and hybrid systems validated the superiority of the bio-nanocomposite configuration. The approach merges enzymatic and photocatalytic degradation in a biologically resilient matrix, providing a scalable, environmentally sound strategy for industrial water treatment. These findings offer a comprehensive framework for future application of microbe–nanomaterial hybrids in complex pollutant removal.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"195 ","pages":"Article 110810"},"PeriodicalIF":3.7,"publicationDate":"2025-12-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145881384","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-12-27DOI: 10.1016/j.enzmictec.2025.110808
Nidhi S. Hallikeri , Deepak A. Yaraguppi , Bhavya S. Gangadharappa , Nitin Mantri
Naringinase is a bifunctional enzyme exhibiting both α-L-rhamnosidase and β-D-glucosidase activity, primarily utilized for the hydrolysis of bitter compounds like naringin in citrus products. This enzymatic action yields naringenin, a bioactive flavonoid known for its significant antioxidant, anti-inflammatory, and cardioprotective properties. Given its dual enzymatic function and substrate specificity, naringinase has garnered substantial interest across the food, pharmaceutical, and broader biotechnological sectors. This comprehensive review critically examines recent advancements concerning naringinase, focusing on its microbial production, optimization strategies in fermentation, purification methods, and various immobilization technologies. Aspergillus niger and Penicillium decumbens are identified as the predominant microbial sources for naringinase production, with solid-state fermentation demonstrating economic and cost-effectiveness over submerged fermentation. The application of diverse immobilization techniques, including adsorption, covalent binding, and encapsulation, has been shown to significantly enhance the enzyme's catalytic stability, reusability, and overall efficiency in applications such as juice debittering and the development of functional foods. While advanced biocatalysis approaches like recombinant expression and enzyme engineering offer promising improvements in catalytic properties, the persistent challenges related to production scalability and purification costs warrant further assessment. The integration of sustainable solid-state fermentation with cutting-edge nanomaterials holds considerable promise, opening new avenues for naringinase applications in environmental biotechnology and personalized medicine.
柚皮苷酶是一种具有α- l -鼠李糖苷酶和β- d -葡萄糖苷酶活性的双功能酶，主要用于柑橘产品中柚皮苷等苦味化合物的水解。这种酶的作用产生柚皮素，一种具有生物活性的类黄酮，以其显著的抗氧化、抗炎和心脏保护特性而闻名。鉴于其双重酶功能和底物特异性，柚皮苷酶在食品、制药和更广泛的生物技术领域获得了极大的兴趣。本文综述了柚皮苷酶的最新进展，重点介绍了柚皮苷酶的微生物生产、发酵优化策略、纯化方法和各种固定化技术。黑曲霉和躺倒青霉被认为是柚皮苷酶生产的主要微生物来源，固态发酵比水下发酵更经济、更经济。各种固定技术的应用，包括吸附、共价结合和包封，已被证明可以显著提高酶的催化稳定性、可重复使用性和整体效率，如果汁脱脂和功能食品的开发。虽然重组表达和酶工程等先进的生物催化方法有望改善催化性能，但与生产可扩展性和纯化成本相关的持续挑战需要进一步评估。可持续固态发酵与尖端纳米材料的结合具有相当大的前景，为柚皮苷酶在环境生物技术和个性化医疗中的应用开辟了新的途径。
{"title":"Naringinase: A comprehensive review on its characteristics, production, and biotechnological applications","authors":"Nidhi S. Hallikeri , Deepak A. Yaraguppi , Bhavya S. Gangadharappa , Nitin Mantri","doi":"10.1016/j.enzmictec.2025.110808","DOIUrl":"10.1016/j.enzmictec.2025.110808","url":null,"abstract":"<div><div>Naringinase is a bifunctional enzyme exhibiting both α-<span>L</span>-rhamnosidase and β-<span>D</span>-glucosidase activity, primarily utilized for the hydrolysis of bitter compounds like naringin in citrus products. This enzymatic action yields naringenin, a bioactive flavonoid known for its significant antioxidant, anti-inflammatory, and cardioprotective properties. Given its dual enzymatic function and substrate specificity, naringinase has garnered substantial interest across the food, pharmaceutical, and broader biotechnological sectors. This comprehensive review critically examines recent advancements concerning naringinase, focusing on its microbial production, optimization strategies in fermentation, purification methods, and various immobilization technologies. <em>Aspergillus niger</em> and <em>Penicillium decumbens</em> are identified as the predominant microbial sources for naringinase production, with solid-state fermentation demonstrating economic and cost-effectiveness over submerged fermentation. The application of diverse immobilization techniques, including adsorption, covalent binding, and encapsulation, has been shown to significantly enhance the enzyme's catalytic stability, reusability, and overall efficiency in applications such as juice debittering and the development of functional foods. While advanced biocatalysis approaches like recombinant expression and enzyme engineering offer promising improvements in catalytic properties, the persistent challenges related to production scalability and purification costs warrant further assessment. The integration of sustainable solid-state fermentation with cutting-edge nanomaterials holds considerable promise, opening new avenues for naringinase applications in environmental biotechnology and personalized medicine.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"195 ","pages":"Article 110808"},"PeriodicalIF":3.7,"publicationDate":"2025-12-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145877903","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-12-27DOI: 10.1016/j.enzmictec.2025.110809
Xiaotong Kang , Hang Yuan , Weimeng Li, Yun Hu, Fubao Sun
Thermophilic endoglucanases are of big promise in enzymatic degradation of lignocellulosic substrate, yet their limited catalytic efficiency remains a major barrier to industrial application. This study focused on the improvement of activity and stability of thermostable endoglucanase DtCelA from Dictyoglomus turgidum with a three-stage cascade engineering strategy that integrated model-guided site-directed mutagenesis, disulfide bond introduction, and carbohydrate-binding module (CBM) fusion. Among the variants, the triple mutant S25D/T265C/A305C fused with CBM2 (S25D/T265C/A305C-A-CBM2) exhibited a 90.56 % increase in specific activity toward CMC relative to the wild type, together with a 2.97-fold longer half-life at 75 °C and a 5.3-fold longer at 80 °C. This mutant also displayed 3.0- and 5.4-fold higher hydrolytic activity against Avicel and konjac glucomannan, respectively. On natural lignocellulosic substrates including filter paper, sugarcane bagasse, and corn stover, the mutant also showed potential application. The mutated endoglucanase DtCelA was powerful with enhanced catalytic performance and thermostability after multicascade engineering, which can provide a robust framework for the rational design of cellulases that are optimized for high-temperature biorefinery process.
嗜热性内切葡聚糖酶在木质纤维素底物的酶解中具有很大的前景，但其有限的催化效率仍然是工业应用的主要障碍。本研究采用三级级联工程策略，将模型引导的位点定向诱变、二硫键引入和碳水化合物结合模块（CBM）融合结合在一起，重点研究了从瘤胃Dictyoglomus turgidum中提高热稳定型内切葡聚糖酶DtCelA的活性和稳定性。其中，与CBM2融合的三突变体S25D/T265C/A305C- a -CBM2 （S25D/T265C/A305C- a -CBM2）对CMC的比活性比野生型提高了90.56 %，75℃时半衰期延长了2.97倍，80℃时半衰期延长了5.3倍。该突变体对Avicel和魔芋葡甘露聚糖的水解活性分别提高了3.0倍和5.4倍。在包括滤纸、甘蔗渣和玉米秸秆在内的天然木质纤维素基质上，该突变体也显示出潜在的应用前景。突变后的内切葡聚糖酶DtCelA具有较强的催化性能和热稳定性，可为优化高温生物炼制工艺的纤维素酶的合理设计提供坚实的框架。
{"title":"Enhanced activity and stability of thermostable endoglucanase Dictyoglomus turgidum DtCelA with multiple strategies","authors":"Xiaotong Kang , Hang Yuan , Weimeng Li, Yun Hu, Fubao Sun","doi":"10.1016/j.enzmictec.2025.110809","DOIUrl":"10.1016/j.enzmictec.2025.110809","url":null,"abstract":"<div><div>Thermophilic endoglucanases are of big promise in enzymatic degradation of lignocellulosic substrate, yet their limited catalytic efficiency remains a major barrier to industrial application. This study focused on the improvement of activity and stability of thermostable endoglucanase <em>Dt</em>CelA from <em>Dictyoglomus turgidum</em> with a three-stage cascade engineering strategy that integrated model-guided site-directed mutagenesis, disulfide bond introduction, and carbohydrate-binding module (CBM) fusion. Among the variants, the triple mutant S25D/T265C/A305C fused with CBM2 (S25D/T265C/A305C-A-CBM2) exhibited a 90.56 % increase in specific activity toward CMC relative to the wild type, together with a 2.97-fold longer half-life at 75 °C and a 5.3-fold longer at 80 °C. This mutant also displayed 3.0- and 5.4-fold higher hydrolytic activity against Avicel and konjac glucomannan, respectively. On natural lignocellulosic substrates including filter paper, sugarcane bagasse, and corn stover, the mutant also showed potential application. The mutated endoglucanase <em>Dt</em>CelA was powerful with enhanced catalytic performance and thermostability after multicascade engineering, which can provide a robust framework for the rational design of cellulases that are optimized for high-temperature biorefinery process.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"195 ","pages":"Article 110809"},"PeriodicalIF":3.7,"publicationDate":"2025-12-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145862488","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-12-26DOI: 10.1016/j.enzmictec.2025.110806
Lei Zhao , Jinghui Lai , Shenghui Zhang , Mengqi Dai , Enxiang Zong , Youqiang Xu , Xiuting Li
As an eco-friendly and non-toxic nonionic surfactant, enzymatically synthesized sucrose esters (SEs) are increasingly valued across the food, cosmetic, and pharmaceutical industries due to their environmentally benign production characteristics. However, current enzymatic synthesis faces several fundamental constraints, like limited diversity of enzyme resources restricting process versatility, insufficient catalytic activity and thermostability of enzymes leading to suboptimal reaction efficiency, and prohibitive enzyme production costs hindering industrial scalability. To address these critical challenges, this review presents a systematic summarize of SEs synthetic technologies and their emerging applications, with particular emphasis on elucidating enzymatic synthetic mechanisms. Due to limited enzyme resources, we innovatively propose a high-throughput bioinformatics-driven enzyme mining platform that employs SEs synthase sequences as molecular probes for screening the SEs synthases, identifying previously uncharacterized enzyme candidates with potentially enhanced catalytic efficiencies. Through systematic bottleneck analysis and a forward-looking perspective, our work establishes a theoretical foundation for developing cost-effective enzymatic processes while providing a valuable repository of potential enzyme candidates for the first time. These findings offer useful guidelines for promoting enzymatic SEs production.
{"title":"Enzymatic synthesis of sucrose esters: Advances and challenges in high-efficiency and regioselective catalysis","authors":"Lei Zhao , Jinghui Lai , Shenghui Zhang , Mengqi Dai , Enxiang Zong , Youqiang Xu , Xiuting Li","doi":"10.1016/j.enzmictec.2025.110806","DOIUrl":"10.1016/j.enzmictec.2025.110806","url":null,"abstract":"<div><div>As an eco-friendly and non-toxic nonionic surfactant, enzymatically synthesized sucrose esters (SEs) are increasingly valued across the food, cosmetic, and pharmaceutical industries due to their environmentally benign production characteristics. However, current enzymatic synthesis faces several fundamental constraints, like limited diversity of enzyme resources restricting process versatility, insufficient catalytic activity and thermostability of enzymes leading to suboptimal reaction efficiency, and prohibitive enzyme production costs hindering industrial scalability. To address these critical challenges, this review presents a systematic summarize of SEs synthetic technologies and their emerging applications, with particular emphasis on elucidating enzymatic synthetic mechanisms. Due to limited enzyme resources, we innovatively propose a high-throughput bioinformatics-driven enzyme mining platform that employs SEs synthase sequences as molecular probes for screening the SEs synthases, identifying previously uncharacterized enzyme candidates with potentially enhanced catalytic efficiencies. Through systematic bottleneck analysis and a forward-looking perspective, our work establishes a theoretical foundation for developing cost-effective enzymatic processes while providing a valuable repository of potential enzyme candidates for the first time. These findings offer useful guidelines for promoting enzymatic SEs production.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"195 ","pages":"Article 110806"},"PeriodicalIF":3.7,"publicationDate":"2025-12-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145881383","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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