Preparative Biochemistry & Biotechnology最新文献

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Isolation, purification, and physio-chemical characterization of melanin pigment from nigerseed hulls (Guizotia abyssinica). 从黑木耳(Guizotia abysinica)中分离、提纯和鉴定黑色素。
IF 2 4区 生物学
Preparative Biochemistry & Biotechnology Pub Date : 2025-02-01 Epub Date: 2024-07-12 DOI: 10.1080/10826068.2024.2376579
Sunil Kumar B T, Umesh H Hebbar, Sridevi Annapurna Singh
{"title":"Isolation, purification, and physio-chemical characterization of melanin pigment from nigerseed hulls (<i>Guizotia abyssinica</i>).","authors":"Sunil Kumar B T, Umesh H Hebbar, Sridevi Annapurna Singh","doi":"10.1080/10826068.2024.2376579","DOIUrl":"10.1080/10826068.2024.2376579","url":null,"abstract":"<p><p>Plant melanin, a natural pigment, has gained significant attention recently due to its potential therapeutic and industrial applications. In this study, melanin pigments were extracted from Nigerseed hulls (NH) <i>via</i> alkali and acid extraction methods, followed by acid hydrolysis, organic solvent treatment, and repeated precipitation. The solubility of NH melanin was assessed, revealing solubility in alkali and dimethyl sulfoxide (DMSO) but insolubility in other common organic solvents. High-performance liquid chromatography (HPLC) was employed to measure the purity of NH melanin in comparison to standard melanin, while elemental analysis indicated a similarity between melanin extracted from nigerseed hulls and the standard counterpart. LC-MS data revealed a molecular weight of NH melanin. Furthermore, the stability of melanin was evaluated under varying conditions including temperature, oxidants, reducing agents, light exposure, and metal ion presence. Results demonstrated significant effects of Mg<sup>2+</sup>, Cu<sup>2+</sup>, and Fe<sup>2+</sup> metal ions on melanin stability, with a minor effect observed for Ca<sup>2+</sup>, while sodium hyposulfite was found to destabilize the pigments. Our findings suggest that nigerseed hulls hold promise as a novel source for efficient melanin production, with potential applications in the food sector, food packaging, and biomedical fields.</p>","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"141-149"},"PeriodicalIF":2.0,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141601363","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
Advanced temperature control in ethanol fermentation using a PSO-PID controller with split-range control strategy. 采用分程控制策略的 PSO-PID 控制器在乙醇发酵过程中实现先进的温度控制。
IF 2 4区 生物学
Preparative Biochemistry & Biotechnology Pub Date : 2025-02-01 Epub Date: 2024-08-03 DOI: 10.1080/10826068.2024.2381761
Raju Yerolla, Suhailam P, Chandra Shekar Besta
{"title":"Advanced temperature control in ethanol fermentation using a PSO-PID controller with split-range control strategy.","authors":"Raju Yerolla, Suhailam P, Chandra Shekar Besta","doi":"10.1080/10826068.2024.2381761","DOIUrl":"10.1080/10826068.2024.2381761","url":null,"abstract":"<p><p>Global energy demand is experiencing a notable surge due to growing energy security. Renewable energy sources, like ethanol, are becoming more viable. In the present study, the application of a PSO-PID (Particle Swarm Optimization - Proportional Integral Derivative) controller with a split-range control strategy was suggested for the regulation of temperature within the fermentation system. To optimize performance, a POS-PID controller with a split-range arrangement utilizing two control valves for hot and cold utilities was constructed. The study began by examining the open-loop dynamic response of the system to inlet temperature and concentration disturbances during ethanol production fermentation. Subsequently, a transfer function model was developed through linearization at the steady-state operating point. The split-range controller structure, implemented by optimizing the PSO-PID controller parameters using PSO, effectively demonstrated temperature control in simulations of a nonlinear model. In this investigation, the ethanol fermentation system was modeled as a CSTR using a modified Monod equation for microbial growth kinetics. Various dynamic behavioral disturbances were explored and verified in the model with plant data in this study. The simulation model results were validated through plant data. The proposed method showed superior closed-loop performance with respect to errors, with the actuators proving to be effective than other reported methods for temperature control.</p>","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"196-209"},"PeriodicalIF":2.0,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141889947","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
Ultrasonic/microwave-assisted extraction and properties of polysaccharides from Elaeagnus angustifolia.
IF 2 4区 生物学
Preparative Biochemistry & Biotechnology Pub Date : 2025-01-31 DOI: 10.1080/10826068.2025.2457539
Jin-Feng Li, Yan Chen, Qi Yan, Chen-Yang Li, Yu-Han Yao, Jun Zhao
{"title":"Ultrasonic/microwave-assisted extraction and properties of polysaccharides from <i>Elaeagnus angustifolia</i>.","authors":"Jin-Feng Li, Yan Chen, Qi Yan, Chen-Yang Li, Yu-Han Yao, Jun Zhao","doi":"10.1080/10826068.2025.2457539","DOIUrl":"https://doi.org/10.1080/10826068.2025.2457539","url":null,"abstract":"<p><p>This study aimed to optimize the ultrasonic/microwave-assisted extraction (UAME) technique of <i>Elaeagnus angustifolia</i> polysaccharides (EAP-UM) by response surface methodology (RSM). The optimum conditions include: solid-liquid ratio of 1:23 g/mL, ultrasonic power of 252 W, microwave power of 417 W, and extraction time of 11 min. Under these conditions, the yield of polysaccharides reached 7.87%, superior to ultrasound-assisted extraction (UAE, 5.74%), microwave-assisted extraction (MAE, 6.86%), and hot water extraction (HWE, 4.91%). UAME could also result in higher carbohydrate, protein, and uronic acid contents compared to other methods. The properties of EAP-UM were further analyzed by infrared spectra (IR) and scanning electron microscopy (SEM). Moreover, EAP-UM exhibited a remarkable free radical scavenging ability (DPPH, IC<sub>50,</sub> 79 µg/mL) and reduced power. EAP-UM also showed α-amylase inhibiting activity (IC<sub>50</sub>, 2.826 mg/mL). UAME has the advantage of high extraction rate and short extraction time, and the obtained polysaccharide EAP-UM had better properties. These findings may serve as a reference for the development and application of <i>E. angustifolia</i>.</p>","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"1-11"},"PeriodicalIF":2.0,"publicationDate":"2025-01-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143067648","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
Improving soluble recombinant SARS-CoV-2 papain-like protease production in Escherichia coli through chaperonin and maltose-binding protein tag: purification and kinetic characterization.
IF 2 4区 生物学
Preparative Biochemistry & Biotechnology Pub Date : 2025-01-31 DOI: 10.1080/10826068.2025.2456940
Riswanto Napitupulu, Maimunah, Amarila Malik, Is Helianti
{"title":"Improving soluble recombinant SARS-CoV-2 papain-like protease production in <i>Escherichia coli</i> through chaperonin and maltose-binding protein tag: purification and kinetic characterization.","authors":"Riswanto Napitupulu, Maimunah, Amarila Malik, Is Helianti","doi":"10.1080/10826068.2025.2456940","DOIUrl":"https://doi.org/10.1080/10826068.2025.2456940","url":null,"abstract":"<p><p>Although COVID-19 is now becoming endemic, SARS-CoV-2 persists potential jeopardy to clinically vulnerable populations. Hence, further study is still necessary to discover novel antiviral agents against SARS-CoV-2 for proactive preparedness. SARS-CoV-2 papain-like protease (PL Pro) is a target enzyme for searching anti-Covid candidates. Our prior study revealed the major formation of inclusion bodies during PL Pro expression in <i>E. coli</i> RIPL. In this study, we tried using chaperonin in the <i>E. coli</i> Arctic Express system and both codon optimization and maltose-binding protein (MBP) fusion protein to make PL Pro more soluble. Recombinant PL Pro encoded on the pET21d(+) plasmid was expressed in <i>E. coli</i> Arctic express. However, the soluble protein yield remained low and unstable due to suboptimal codon usage in the insert gene. Whereas, fusion of the MBP protein with optimized codon of PL Pro enhanced the enzyme expression and solubility. Recombinant PL Pro cleaved the linker between MBP and PL Pro, which served as a cleavage site recognized by PL Pro (LKGG↓A). The purified enzyme from a 200-mL culture generated 1 mL of pure PL Pro enzyme at a 1.913 mg/mL concentration. It exhibited favorable activity against the Z-RLRGG-AMC substrate, with a Km value of 33.40 μM and a Vmax of 5.10 RFU/min.</p>","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"1-10"},"PeriodicalIF":2.0,"publicationDate":"2025-01-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143075302","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
The potential of Streptococcus pyogenes and Escherichia coli bacteriocins in synergistic control of Staphylococcus aureus.
IF 2 4区 生物学
Preparative Biochemistry & Biotechnology Pub Date : 2025-01-28 DOI: 10.1080/10826068.2025.2457556
Gideon Sadikiel Mmbando, Musa Wilson Salaja
{"title":"The potential of <i>Streptococcus pyogenes</i> and <i>Escherichia coli</i> bacteriocins in synergistic control of <i>Staphylococcus aureus</i>.","authors":"Gideon Sadikiel Mmbando, Musa Wilson Salaja","doi":"10.1080/10826068.2025.2457556","DOIUrl":"https://doi.org/10.1080/10826068.2025.2457556","url":null,"abstract":"<p><p><i>Staphylococcus aureus</i> has developed resistance to most conventional antibiotics and is a causative agent of serious infections. Alternative therapies are urgently needed. Bacteriocins are ribosomally synthesized antimicrobial peptides produced by bacteria, including <i>Escherichia coli</i> (<i>E. coli</i>) and <i>Streptococcus pyogenes</i> (<i>S. pyogenes</i>), and represent a potential solution. While several bacteriocins have shown promise, their synergy with bacteriocins from other bacterial species remains largely unexplored. This work used agar diffusion on Muller-Hinton Agar (MHA) with <i>S. aureus</i> as a test bacterium to evaluate <i>E. coli</i>, <i>S. pyogenes</i> and their combined bacteriocins. The bacteriocins of <i>S. pyogenes</i> showed the maximum antimicrobial activity of zone of inhibition (ZOI), 24.93 mm, compared to that of <i>E. coli</i> bacteriocin, which was 19.28 mm, and that of the combined ones at 100% concentration, 22.6 mm. The combined bacteriocins at 50% concentration showed a reduced activity of 18.35 mm. These observations suggest that the bacteriocins produced by <i>S. pyogenes</i> have higher specificity and activity against <i>S. aureus</i>, making them effective therapeutic agents in the fight against multidrug-resistant infections.</p>","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"1-9"},"PeriodicalIF":2.0,"publicationDate":"2025-01-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143053322","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
Bioconversion of mustard oil cake for production of lipase, optimization and direct immobilization from solid-state fermentation extract. 芥子油饼生物转化生产脂肪酶、优化和直接固定固态发酵提取物。
IF 2 4区 生物学
Preparative Biochemistry & Biotechnology Pub Date : 2025-01-28 DOI: 10.1080/10826068.2025.2453729
Bhim Singh, Asim Kumar Jana, Mithu Maiti Jana
{"title":"Bioconversion of mustard oil cake for production of lipase, optimization and direct immobilization from solid-state fermentation extract.","authors":"Bhim Singh, Asim Kumar Jana, Mithu Maiti Jana","doi":"10.1080/10826068.2025.2453729","DOIUrl":"https://doi.org/10.1080/10826068.2025.2453729","url":null,"abstract":"<p><p>Fungal lipases are the leading industrial biocatalyst due to their broad applications, but high cost limits their commercial usage. The low-cost agri-residues substrates can reduce the cost of lipase production. However, the compatibility of agri-residue with fungal species, recovery process of lipase and stability of the enzyme are crucial steps. The aim of the present work was optimization of lipase production from a suitable combination of fungal culture with a locally available vegetable oilseed cake (mustard/groundnut/almond/cottonseed) in solid-state fermentation process and its direct immobilization. The enzyme produced using selected combination of <i>Rhizopus oryzae</i> and mustard oilseed cake was optimized by Plackett-Burman design, one-factor-at-a-time and central composite design (CCD). The highest enzyme activity of 25.08 U/gds was obtained by CCD at urea 2.11% w/w, inoculum size 1.18% v/w, and moisture content 69.99% w/w. The crude enzyme from the extract was immobilized on functionalized magnetic nanoparticles with the results of protein loading 68.88 ± 3.54 µg/mg of MNPs and activity recovery of 60.33 ± 3.03%. This study can be helpful to explore the suitability of locally available agri-residue for production of lipase and utilization of enzyme in different industrial applications.</p>","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"1-14"},"PeriodicalIF":2.0,"publicationDate":"2025-01-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143053320","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
Review on up and downstream processing of L-asparaginase.
IF 2 4区 生物学
Preparative Biochemistry & Biotechnology Pub Date : 2025-01-24 DOI: 10.1080/10826068.2024.2449139
Kamran Hosseini, Tayebeh Zivari-Ghader, Azita Dilmaghani, Parvin Akbarzadehlaleh, Elnaz-Alsadat Jafarzadeh-Chehraghi
{"title":"Review on up and downstream processing of L-asparaginase.","authors":"Kamran Hosseini, Tayebeh Zivari-Ghader, Azita Dilmaghani, Parvin Akbarzadehlaleh, Elnaz-Alsadat Jafarzadeh-Chehraghi","doi":"10.1080/10826068.2024.2449139","DOIUrl":"https://doi.org/10.1080/10826068.2024.2449139","url":null,"abstract":"<p><p>L-asparaginase (asparagine amidohydrolase) contributes to 40% of the total enzyme demands worldwide and is one-third of the global requirement as an anti-cancerous drug in treating acute lymphocytic leukemia (ALL), a type of leukemia. This protein breaks down L-asparagine into aspartic acid and ammonia those involved in ALL, rely on for growth and survival. Both non-recombinant and recombinant L-asparaginase can be produced by bacteria when a suitable substrate and method (solid-state fermentation (SSF) or submerged fermentation (SmF) which are techniques to grow microorganisms under controlled conditions), is provided. Between both L-asparaginase's isozymes, asparaginase type II displays higher specific action against L-asparagine and precisely shows antitumor activity. The applied methods in purification of L-asparaginase in the frame of three phases of protein purification strategy known as CIPP (including capture, intermediate purification, and polishing phase) are discussed in this review. Depending on whether the production of the enzyme is intracellular or extracellular, various steps in each phase, like removal of insoluble material, extraction, concentration, and purification, must followed. In this review, authors summarize the upstream processes in L-asparaginase production and the various applied chromatographic and non-chromatographic methods in each step of CIPP, in downstream processes.</p>","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"1-9"},"PeriodicalIF":2.0,"publicationDate":"2025-01-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143033809","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
Cellulase from Halomonas elongata for biofuel application: enzymatic characterization and inhibition tolerance investigation. 用于生物燃料的长形盐单胞菌纤维素酶:酶学表征和抑制耐受性研究。
IF 2 4区 生物学
Preparative Biochemistry & Biotechnology Pub Date : 2025-01-21 DOI: 10.1080/10826068.2025.2453727
Aathimoolam Narayanan, Kanimozhi Jeyaram, Ashish A Prabhu, Sundar Krishnan, Selvaraj Kunjiappan, Nareshkumar Baskaran, Dharanidharan Murugan
{"title":"Cellulase from <i>Halomonas elongata</i> for biofuel application: enzymatic characterization and inhibition tolerance investigation.","authors":"Aathimoolam Narayanan, Kanimozhi Jeyaram, Ashish A Prabhu, Sundar Krishnan, Selvaraj Kunjiappan, Nareshkumar Baskaran, Dharanidharan Murugan","doi":"10.1080/10826068.2025.2453727","DOIUrl":"https://doi.org/10.1080/10826068.2025.2453727","url":null,"abstract":"<p><p>Halophilic bacteria are promising candidates for biofuel production because of their efficient cellulose degradation. Their cellulases exhibit high activity, even in the presence of inhibitors and under extreme conditions, making them ideal for biorefinery applications. In this study, we isolated a strain of <i>Halomonas elongata</i> (Kadal6) from decomposed cotton cloth on a Rameshwaram seashore. Morphological, biochemical, and 16S rRNA analyses revealed that Kadal6 was 99.93% similar to the cellulase-producing strain, <i>H. elongata</i> MH25661. The tolerance of the cellulase to inhibitors was assessed through molecular docking with a cellulase model of MH25661 generated by I-TASSER and experimentally using response surface methodology (RSM) with Kadal6. A molecular docking study indicated a high inhibition constant for ethanol, hydroxymethylfurfural (HMF), and furfural. Cellulase from <i>H. elongata</i> Kadal6 (CellHe) showed a maximum inhibition rate of 44.27% at 55 °C, 15% ethanol, and 6.5 g/L furfural and HMF. The enzyme retained 50% of its activity in the presence of these inhibitors, and remained unaffected at 1 g/L furfural and HMF, although inhibition occurred at 3 g/L. <i>H. elongata</i> cellulase demonstrated significant tolerance to inhibition both in vitro (RSM) and in silico, indicating its potential for biorefinery applications in harsh environments.</p>","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"1-18"},"PeriodicalIF":2.0,"publicationDate":"2025-01-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143010499","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
Development of an attenuated glutamine synthetase (GS) selection system for the stable expression of tissue plasminogen activator in CHO-K1 cells. 在CHO-K1细胞中稳定表达组织纤溶酶原激活物的减毒谷氨酰胺合成酶(GS)选择系统的建立。
IF 2 4区 生物学
Preparative Biochemistry & Biotechnology Pub Date : 2025-01-21 DOI: 10.1080/10826068.2025.2454335
Mozhgan Raigani, Pegah Namdar, Farzaneh Barkhordari, Sima Sadat Seyedjavadi, Azam Rahimpour, Ahmad Adeli
{"title":"Development of an attenuated glutamine synthetase (GS) selection system for the stable expression of tissue plasminogen activator in CHO-K1 cells.","authors":"Mozhgan Raigani, Pegah Namdar, Farzaneh Barkhordari, Sima Sadat Seyedjavadi, Azam Rahimpour, Ahmad Adeli","doi":"10.1080/10826068.2025.2454335","DOIUrl":"https://doi.org/10.1080/10826068.2025.2454335","url":null,"abstract":"<p><p>Chinese hamster ovary (CHO) cells represent the most common host system for the expression of high-quality recombinant proteins. The development of stable CHO cell lines used in industrial recombinant protein production often relies on dihydrofolate reductase (DHFR) and glutamine synthetase (GS) amplification systems. Conventional approaches to develop stable cell lines lead to heterogeneous cell populations. Consequently, it is desirable to adopt innovative strategies to increase the efficiency of clone selection to reduce the time and effort invested in the cell line development process. Attenuating the selection marker gene is an effective strategy for isolating high-producing cells. In this study, we evaluated the efficiency of an attenuated glutamine synthetase selection system for the expression of human tissue plasminogen activator (t-PA) in CHO cells. We introduced an AU-rich element (ARE) at the 3'UTR of the glutamine synthetase coding sequence and employed a weak promoter (mSV40) for the expression of this gene. Subsequently, we analyzed the effect of ARE on the GS RNA levels, and recombinant t-PA expression. Our results demonstrate that the use of ARE significantly enhances the detection of high expressing cells compared to the control. Additionally, the t-PA expression level in GS-ARE clones was approximately 900-fold greater than those without the ARE.</p>","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"1-7"},"PeriodicalIF":2.0,"publicationDate":"2025-01-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143010503","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
Pea whey wastewater as a medium additive for the production of docosahexaenoic acid (C22:6 n3). 豌豆乳清废水作为生产二十二碳六烯酸(C22:6 n3)的介质添加剂。
IF 2 4区 生物学
Preparative Biochemistry & Biotechnology Pub Date : 2025-01-19 DOI: 10.1080/10826068.2025.2453833
Xinyu Wang, Xiangying Zhao, Ruiguo Li, Jiaxiang Zhang, Xia Li, Liping Liu
{"title":"Pea whey wastewater as a medium additive for the production of docosahexaenoic acid (C22:6 n3).","authors":"Xinyu Wang, Xiangying Zhao, Ruiguo Li, Jiaxiang Zhang, Xia Li, Liping Liu","doi":"10.1080/10826068.2025.2453833","DOIUrl":"https://doi.org/10.1080/10826068.2025.2453833","url":null,"abstract":"<p><p>In this study, the potential of pea whey wastewater (PWW) as a substrate for the biosynthesis of docosahexaenoic acid (DHA) was investigated by culturing the strain Aurantiochytrium limacinum SFD-1502. The results showed that culturing SFD-1502 in PWW alone resulted in poor growth, possibly due to an insufficient carbon source. The addition of glucose and monosodium glutamate to PWW resulted in a significant improvement in cell growth, and the dry weight of the cells reaching 43.45 ± 0.39 g/L g/L, comparable to that of the control (using artificial seawater fermentation medium), despite the lipid content in the cells and the DHA proportion in the lipids were slightly lower than those of the control. Subsequent studies demonstrated that the presence of raffinose family oligosaccharides, a higher concentration of arginine, and a lower concentration of Na<sup>+</sup> relative to artificial seawater in PWW resulted in the reduction of cellular lipids and the proportion of DHA. Furthermore, the chemical oxygen demand (COD) of PWW was reduced by approximately 60% during the fermentation. Consequently, the utilization of PWW in A. limacinum culture for DHA production is a viable and cost-effective strategy.</p>","PeriodicalId":20401,"journal":{"name":"Preparative Biochemistry & Biotechnology","volume":" ","pages":"1-8"},"PeriodicalIF":2.0,"publicationDate":"2025-01-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143010510","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
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