Enzyme and Microbial Technology最新文献

Synergy between processive cellulases in Ruminoccocus albus

IF 3.4 3区生物学

Enzyme and Microbial Technology Pub Date : 2025-02-18 DOI: 10.1016/j.enzmictec.2025.110610

Alem Storani , Alberto A. Iglesias, Sergio A. Guerrero

{"title":"Synergy between processive cellulases in Ruminoccocus albus","authors":"Alem Storani , Alberto A. Iglesias, Sergio A. Guerrero","doi":"10.1016/j.enzmictec.2025.110610","DOIUrl":"10.1016/j.enzmictec.2025.110610","url":null,"abstract":"<div><div>Endoglucanases (EGs), cellobiohydrolases (CBHs), and β-glucosidases are essential components in enzymatic degradation of cellulose. We analyzed the glycosyl hydrolases from families GH5 and GH48 from <em>Ruminococcus albus</em> 8 (<em>Ral</em>Cel5G and <em>Ral</em>Cel48A). Both enzymes feature a catalytic motif and a carbohydrate binding domain from family 37 (CBM37). <em>Ral</em>Cel5G also exhibited a second CBM37 with lower similarity. As a result, <em>Ral</em>Cel5G showed higher binding affinity toward insoluble substrates and broader recognition capacity. Kinetic characterization using different cellulosic substrates and reaction product analysis confirmed <em>Ral</em>Cel5G as a processive EG while <em>Ral</em>Cel48A is a CBH. Interestingly, we found a synergistic effect on their activity at a low EG to CBH ratio, despite the processive activity of <em>Ral</em>Cel5G. Furthermore, the lignocellulose degradation capacity was improved by supplementing the cellulases with hemicellulase <em>Ral</em>Xyn10A. These results provide valuable information about the interaction between processive EG and conventional CBH, necessary for the rational design of enzyme cocktails for optimized biomass processing.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"186 ","pages":"Article 110610"},"PeriodicalIF":3.4,"publicationDate":"2025-02-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143455005","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}

引用次数: 0

Characterization of keratinase from Chryseobacterium camelliae Dolsongi-HT1 and efficacy on skin exfoliation

IF 3.4 3区生物学

Enzyme and Microbial Technology Pub Date : 2025-02-17 DOI: 10.1016/j.enzmictec.2025.110605

Eun-Mi Kim, Soojung Oh, Hyeongwon Choi, Won-Seok Park

{"title":"Characterization of keratinase from Chryseobacterium camelliae Dolsongi-HT1 and efficacy on skin exfoliation","authors":"Eun-Mi Kim, Soojung Oh, Hyeongwon Choi, Won-Seok Park","doi":"10.1016/j.enzmictec.2025.110605","DOIUrl":"10.1016/j.enzmictec.2025.110605","url":null,"abstract":"<div><div>Keratin is the outermost layer that protects our skin and has an appropriate turnover cycle. With age, the keratin turnover cycle begins to dysfunction. To overcome this issue, we artificially remove dead skin cells. In this study, we attempted to screen enzymes that could be useful in the cosmetics industry to develop enzymes suitable for the enzyme-based method, a mild exfoliation method that does not damage the skin. <em>Chryseobacterium camelliae</em> Dolsongi-HT1 with keratinolytic activity was isolated from green tea leaves (sourced from the Dolsongi tea garden, Jeju Island). The keratinolytic activity of <em>C. camelliae</em> Dolsongi-HT1 was detected in the culture media, indicating that the target keratinolytic enzyme is a secreted protein. Keratinolytic activity was demonstrated using forearm skin keratin and reconstituted human skin models. The enzyme from <em>C. camelliae</em> Dolsng-HT1 (HT1) could efficiently decompose human skin keratin. Moreover, experiments using the reconstituted human skin model demonstrated that HT1 is efficient in exfoliating the outermost stratum corneum. Compared with the popularly used chemical exfoliation method, enzymatic exfoliation using HT1 was less abrasive and did not damage the epidermal layer. Keratinolytic enzyme was identified using protein purification and mass spectrometry. The identified enzyme (iHT1) was expressed in the <em>Bacillus subtilis</em> RIK 1285 secretory protein expression system. The iHT1 enzyme showed high activity over a wide temperature range (30–60 °C), with the highest activity at 30 °C. The optimum pH for the activity of iHT was pH8.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"186 ","pages":"Article 110605"},"PeriodicalIF":3.4,"publicationDate":"2025-02-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143429904","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}

引用次数: 0

Enzymatic production of chitooligosaccharides with high degree of polymerisations and their potential application to soy sauce preservation 高聚合度壳寡糖的酶法生产及其在酱油保鲜中的潜在应用

IF 3.4 3区生物学

Enzyme and Microbial Technology Pub Date : 2025-02-17 DOI: 10.1016/j.enzmictec.2025.110608

Yihao Liu , Guangru Sun , Yimeng Lou , Peng Cheng , Qian Song , Wen Lv , Chunling Wang

{"title":"Enzymatic production of chitooligosaccharides with high degree of polymerisations and their potential application to soy sauce preservation","authors":"Yihao Liu , Guangru Sun , Yimeng Lou , Peng Cheng , Qian Song , Wen Lv , Chunling Wang","doi":"10.1016/j.enzmictec.2025.110608","DOIUrl":"10.1016/j.enzmictec.2025.110608","url":null,"abstract":"<div><div>Chitooligosaccharides (COSs) with a high degree of polymerisation (DP 5–10) have been reported to possess diverse bioactivities. Thus, the development of novel methods for the acquisition of high-DP COSs has become increasingly significant. In the study, a novel GH family 46 chitosanase gene (<em>ThCsn46</em>) was expressed and characterized. ThCsn46 was further applied to COSs production, and the highest yield of 95.7 % (143.6 g/L) was obtained using 15 % (w/v) of chitosan as the substrate. The proportion of high-DP COSs occupied 40.6 % of the total COSs. Moreover, the high (GlcN)<sub>6</sub> content was achieved. The total viable count (TVC) and amino acid nitrogen (AAN) of soy sauce incorporated with 0.1 % (w/v) of COSs were better than that of the negative control. The potential of ThCsn46 for application in the production of COSs and the preservation of soy sauce is significant. The green and efficient bioproduction process represents a promising way for further research.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"186 ","pages":"Article 110608"},"PeriodicalIF":3.4,"publicationDate":"2025-02-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143429810","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}

引用次数: 0

Screening and characterization of thermostable xylose isomerase from Rhodothermus marinus for erythrose production from one-carbon source 筛选和鉴定海红藻中的可热稳定木糖异构酶，以利用单碳源生产赤藓糖

IF 3.4 3区生物学

Enzyme and Microbial Technology Pub Date : 2025-02-17 DOI: 10.1016/j.enzmictec.2025.110607

Yanfei Wang , Wenwen Li , Dandan Wang , Yan Zeng , Ming Li , Yuanxia Sun , Jiangang Yang

{"title":"Screening and characterization of thermostable xylose isomerase from Rhodothermus marinus for erythrose production from one-carbon source","authors":"Yanfei Wang , Wenwen Li , Dandan Wang , Yan Zeng , Ming Li , Yuanxia Sun , Jiangang Yang","doi":"10.1016/j.enzmictec.2025.110607","DOIUrl":"10.1016/j.enzmictec.2025.110607","url":null,"abstract":"<div><div>Four-carbon (C4) sugars, which rarely exist in nature, usually have various biological functions and serve as building units for pharmaceutical agents. For example, erythrose possesses various pharmacological activities. Although several iso/epimerases have a catalytic function on C5/C6 sugars, only a few studies have demonstrated the enzymatic iso/epimerization of C4 sugars. In this work, we presented a xylose isomerase from <em>Rhodothermus marinus</em> possessing isomerization activity toward C4 <span>l</span>-erythrulose. This enzyme showed higher affinity and catalytic efficiency toward <span>l</span>-erythrulose than <span>d</span>-fructose and <span>d</span>-xylulose. Its specific activity reached 24.2 U/mg under optimal reaction conditions, and its half-life was over 8 days at 50 ℃. Demonstration of this enzyme under 833 mM of L-erythrulose gave 130 mM L-erythrose with a conversion yield of 15.6 %. On the basis of this beneficial enzyme, we further designed a multienzyme system and presented a one-pot cascade process for the synthesis of <span>l</span>-erythrose from low-cost, one-carbon formaldehyde (FALD) as the sole feedstock. Given that FALD can be derived from CO<sub>2</sub> electrocatalysis or methanol oxidization, <span>l</span>-erythrose synthesis can be realized from methanol and even CO<sub>2</sub>. <span>l</span>-erythrose can further function as feedstock for synthesizing other high-carbon sugars by coupling enzymatic aldol condensation and reduction reactions.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"186 ","pages":"Article 110607"},"PeriodicalIF":3.4,"publicationDate":"2025-02-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143429811","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}

引用次数: 0

Processivity and enzymatic mechanism of a non-modular family 5 endoglucanase from Sporocytophaga sp. CX11 with potential applications in cellulose saccharification

IF 3.4 3区生物学

Enzyme and Microbial Technology Pub Date : 2025-02-15 DOI: 10.1016/j.enzmictec.2025.110609

Xiaoyi Chen , Zilong Gao , Shang Wang, Fan Yang

{"title":"Processivity and enzymatic mechanism of a non-modular family 5 endoglucanase from Sporocytophaga sp. CX11 with potential applications in cellulose saccharification","authors":"Xiaoyi Chen , Zilong Gao , Shang Wang, Fan Yang","doi":"10.1016/j.enzmictec.2025.110609","DOIUrl":"10.1016/j.enzmictec.2025.110609","url":null,"abstract":"<div><div>In this study, a novel GH5 processive endoglucanase <em>Sm</em>Cel5A from <em>Sporocytophaga</em> sp. CX11 was functionally expressed in <em>E. coli.</em> It could rapidly decrease the viscosity of carboxymethyl cellulose (CMC-Na) solution by nearly 50 % within the initial 8 min of incubation and exhibited a significantly high specific activity towards CMC-Na of 9940 U/µmol. <em>Sm</em>Cel5A could also hydrolyze other cellulosic substrates such as RAC, Avicel, filter paper, β-glucan and the chromogenic substrate <em>p</em>NPC. When hydrolyzing filter paper, about 89.1 % of soluble reducing sugars were generated after 180 min of incubation, and the main products were cellobiose followed by cellotriose and glucose. The processive ratio of <em>Sm</em>Cel5A increased from 2.32 to 11.22 as the reaction time was extended from 5 min to 180 min, which is significantly higher than those of other known processive endoglucanases. Moreover, <em>Sm</em>Cel5A could hydrolyze cellodextrins with the degree of polymerization (DP) ≥ 3, but it was not active on cellobiose. In combination reaction with β-glucosidase, the maximum substrate conversion rate reached 73.2 %, showing that the synergistic reaction of the two enzymes could efficiently reduce the accumulation of cellobiose and greatly improve the hydrolysis efficiency of cellulose. The three-dimensional structure of <em>Sm</em>Cel5A was predicted by AlphaFold2 and showed to feature a classic GH5 family (β/α)<sub>8</sub>-barrel structure, with a deep substrate-binding cleft formed by the amino acids at the C-terminus. Molecular docking results indicated that when hydrolyzing cellulosic substrates, <em>Sm</em>Cel5A exhibits a preference for the exo-type mechanism of action over the endo-type mechanism of action.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"185 ","pages":"Article 110609"},"PeriodicalIF":3.4,"publicationDate":"2025-02-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143429162","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}

引用次数: 0

Engineering the D-lactic acid responsive promoter/repressor system as dynamic metabolic engineering tool in Lactobacillus delbrueckii subsp. bulgaricus for controlled D-lactic acid biosynthesis

IF 3.4 3区生物学

Enzyme and Microbial Technology Pub Date : 2025-02-07 DOI: 10.1016/j.enzmictec.2025.110606

Payal Mukherjee , Senthilkumar Sivaprakasam

{"title":"Engineering the D-lactic acid responsive promoter/repressor system as dynamic metabolic engineering tool in Lactobacillus delbrueckii subsp. bulgaricus for controlled D-lactic acid biosynthesis","authors":"Payal Mukherjee , Senthilkumar Sivaprakasam","doi":"10.1016/j.enzmictec.2025.110606","DOIUrl":"10.1016/j.enzmictec.2025.110606","url":null,"abstract":"<div><div>Dynamic metabolic engineering integrates synthetic logic circuits into cellular systems, optimizing metabolic fluxes and augmenting biosynthesis of target metabolites. This study evaluated a D-lactic acid (DLA)-responsive promoter-repressor system from <em>Pseudomonas fluorescens</em> A506, re-engineered for heightened sensitivity and functional efficacy in <em>Lactobacillus delbrueckii</em> subsp. <em>bulgaricus</em> VI104. The codon-optimized regulatory architecture exhibited peak performance at DLA inducer concentration range of 60–100 mM, validated by fluorometry and microscopy. As an application, overexpression of D-lactate dehydrogenase (<em>dldh</em>) downstream of the engineered promoter repressor system enabled finely tuned modulation of DLA biosynthesis, autonomously regulating the transition between growth and production phases, thereby attenuating overall metabolic load. Cross-species compatibility was confirmed by excising regulatory elements from the promoter-repressor system and functionally assessing them in recombinant <em>L. bulgaricus</em>. Molecular docking elucidated critical noncovalent interactions between D-<em>LldR</em> repressor and operator nucleotide sequence in absence of inducer DLA. The engineered promoter construct with high efficiency effectively elevated DLA biosynthesis by 2.15-folds and expanded the overall fermentation time relative to constitutive systems, attaining maximum DLA titre of 9.02 g L⁻<sup>1</sup> in bioreactor setup. These results substantially broaden the molecular cloning toolkit available for <em>L. bulgaricus</em>, fostering potential future applications in biotherapeutics and probiotics.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"185 ","pages":"Article 110606"},"PeriodicalIF":3.4,"publicationDate":"2025-02-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143377871","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}

引用次数: 0

Identification of 2’-deoxyguanosine for an α-amylase inhibitor in the extracts of the earthworm Eisenia fetida and characterization of its inhibitory activity against porcine pancreatic α-amylase

IF 3.4 3区生物学

Enzyme and Microbial Technology Pub Date : 2025-02-04 DOI: 10.1016/j.enzmictec.2025.110604

Masako Ogasawara , Katsuhiro Yoshii , Jun Wada , Yoshihiro Yamamoto , Kuniyo Inouye

{"title":"Identification of 2’-deoxyguanosine for an α-amylase inhibitor in the extracts of the earthworm Eisenia fetida and characterization of its inhibitory activity against porcine pancreatic α-amylase","authors":"Masako Ogasawara , Katsuhiro Yoshii , Jun Wada , Yoshihiro Yamamoto , Kuniyo Inouye","doi":"10.1016/j.enzmictec.2025.110604","DOIUrl":"10.1016/j.enzmictec.2025.110604","url":null,"abstract":"<div><div>Inhibitory activity (IA) against porcine pancreatic α-amylase (PPA) has been found in the water extract of <em>Eisenia fetida</em>. IA is recovered mostly in a fraction (U3EE) containing compounds of low molecular mass under 3 kDa. U3EE is treated with 85 % ethanol (EtOH) and the obtained EtOH extract is applied to the solid-phase extraction (SPE) system. An IA fraction named AI is separated from SPE by elution with water, and then a fraction AI* has been obtained by elution with 5 % EtOH. In the previous study, PPA inhibitors of guanine (Gua), guanosine (Guo), and inosine (Ino) have been isolated from AI. In the present study, IA of AI* was examined and a new inhibitor 2’-deoxyguanosine (2’-dGuo) was isolated by RP-HPLC. It was a mixed-type inhibitor showing IC<sub>50</sub> of 0.7 ± 0.1 mM and inhibitor constants <em>K</em><sub>i</sub> and <em>K</em><sub>i</sub>’ of 2.0 ± 0.5 and 0.9 ± 0.2 mM, respectively, at pH 6 and at 37 °C. PPA inhibitors of U3EE were arranged in the order according to the inhibitory efficiency as Gua> 2’-dGuo> Guo> Ino. This study reports that compounds related to nucleic acids could be PPA inhibitors. These inhibitors as well as U3EE might be suitable for functional foods to prevent obesity and type 2 diabetes.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"185 ","pages":"Article 110604"},"PeriodicalIF":3.4,"publicationDate":"2025-02-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143350651","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}

引用次数: 0

Development of an enzymatic aptasensor for monitoring recombinant His-tagged proteins in microbial biotechnology

IF 3.4 3区生物学

Enzyme and Microbial Technology Pub Date : 2025-02-03 DOI: 10.1016/j.enzmictec.2025.110603

Mohammad Javad Jadidi , Rahman Emamzadeh , Mahboobeh Nazari , Sayed Rasoul Zaker

引用次数: 0

An all-in-one strategy for the simultaneous production of bioplastics and degrading enzymes in engineered Escherichia coli

IF 3.4 3区生物学

Enzyme and Microbial Technology Pub Date : 2025-01-31 DOI: 10.1016/j.enzmictec.2025.110593

Suwon Kim , Yebin Han , Gaeun Lim , See-Hyoung Park , Kyungmoon Park , Shashi Kant Bhatia , Yung-Hun Yang

{"title":"An all-in-one strategy for the simultaneous production of bioplastics and degrading enzymes in engineered Escherichia coli","authors":"Suwon Kim , Yebin Han , Gaeun Lim , See-Hyoung Park , Kyungmoon Park , Shashi Kant Bhatia , Yung-Hun Yang","doi":"10.1016/j.enzmictec.2025.110593","DOIUrl":"10.1016/j.enzmictec.2025.110593","url":null,"abstract":"<div><div>Bioplastics are promising alternatives for traditional plastics, which contribute significantly to environmental pollution and have a detrimental impact on ecosystems. To advance their use, further research into bioplastic biodegradation is essential. In this study, we propose a novel approach for simultaneous polyhydroxybutyrate (PHB) and degrading enzyme production in a single-cell system using engineered <em>Escherichia coli</em>. Typically, PHB depolymerases, such as PhaZ, disrupt bioplastic synthesis in cells, leading to a self-defeating cycle of production and degradation. To counter this, we introduced synthetic PHB production genes and triacylglycerol lipase (TGL) from <em>Bacillus</em> sp. JY35, along with a native signal peptide for secretion. This enabled PHB accumulation inside the cells while TGL was secreted into the supernatant. The concentrations of PHB produced with and without TGL were similar (31.44 % PHB with TGL and 32.12 % PHB without TGL). TGL was efficiently secreted in <em>E. coli</em>, achieving specific esterase activities of 7.1 U/mg and 15.7 U/mg for p-Nitrophenyl butyrate and p-nitrophenyl octanoate, respectively, and degraded PHB film by 30.1 % over 14 d. Moreover, TGL retained 86 % and 91 % of its activities for the C4 and C8 substrates, respectively, after 30 d of storage at room temperature, suggesting potential use PHB degradation after use. Our study demonstrates a straightforward one-month circular cycle for bioplastic production and degradation by a single producer.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"185 ","pages":"Article 110593"},"PeriodicalIF":3.4,"publicationDate":"2025-01-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143103487","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}

引用次数: 0

Development of an enzymatic method for efficient production of DHA-enriched phospholipids through immobilized phospholipase A1 in AOT-water reverse micelles

IF 3.4 3区生物学

Enzyme and Microbial Technology Pub Date : 2025-01-30 DOI: 10.1016/j.enzmictec.2025.110600

Qin Gao , Xiaolin Yu , Jianming Wei , Xuechao Hu , Lujing Ren

{"title":"Development of an enzymatic method for efficient production of DHA-enriched phospholipids through immobilized phospholipase A1 in AOT-water reverse micelles","authors":"Qin Gao , Xiaolin Yu , Jianming Wei , Xuechao Hu , Lujing Ren","doi":"10.1016/j.enzmictec.2025.110600","DOIUrl":"10.1016/j.enzmictec.2025.110600","url":null,"abstract":"<div><div>The demand for omega-3 polyunsaturated fatty acids (PUFAs), particularly docosahexaenoic acid (DHA), has been steadily increasing due to their significant health benefits. Traditional methods for producing DHA-enriched phospholipids often suffer from low efficiency and high costs. In this study, we developed an efficient enzymatic process to prepare phospholipid-DHA, which used immobilized phospholipase A1 to catalyze transesterification in AOT-water reverse micelle systems. Initially, high concentrations of free fatty acids were produced via acid hydrolysis of algae oil followed by crystallization. Among six evaluated reverse micelle systems, one was selected for further optimization. The substrate/enzyme ratio, temperature, reaction time, and water content were optimized using single-factor experiments and response surface methodology. To enhance cost-efficiency and eco-friendly practices, substrate recycling was implemented to maximize substrate utilization. This study established a comprehensive process chain for the preparation of phospholipid-DHA, promoting its industrial production and providing a reference for the production of other phospholipid products.</div></div>","PeriodicalId":11770,"journal":{"name":"Enzyme and Microbial Technology","volume":"185 ","pages":"Article 110600"},"PeriodicalIF":3.4,"publicationDate":"2025-01-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143074292","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}

引用次数: 0