Applied Biochemistry and Microbiology最新文献

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How Does Curtobacterium Produce a Bright Flash-Yellow Color? 弯曲杆菌如何产生明亮的闪光黄色?
IF 1 4区 生物学
Applied Biochemistry and Microbiology Pub Date : 2024-03-27 DOI: 10.1134/S0003683823602895
T. Kawamura, S. Takanawa, H. Ashida, S. Muranaka, A. Murota, S. Kota, A. Maeda, R. Hashimoto, E. Matsui, K. Takayama
{"title":"How Does Curtobacterium Produce a Bright Flash-Yellow Color?","authors":"T. Kawamura,&nbsp;S. Takanawa,&nbsp;H. Ashida,&nbsp;S. Muranaka,&nbsp;A. Murota,&nbsp;S. Kota,&nbsp;A. Maeda,&nbsp;R. Hashimoto,&nbsp;E. Matsui,&nbsp;K. Takayama","doi":"10.1134/S0003683823602895","DOIUrl":"10.1134/S0003683823602895","url":null,"abstract":"<p><i>Curtobacterium</i>, a bright flash-yellow color-producing bacterium, has been isolated from the body fluid of the pupae of <i>Graphium sarpedon</i>. Several experiments were conducted to identify three mechanisms by which this bacterium expresses a vibrant color. The first is caused by yellow pigmentation; the second is due to a substance that absorbs blue light and emits green fluorescence; and the third is a process that excludes brownish colors by inhibiting melanin synthesis. In particular, we focused on melanin synthesis inhibition and used the water-soluble fraction of <i>Curtobacterium</i> and the melanin synthase in vitro human tyrosinase activity assay to examine its inhibitory effects on monophenolase activity, which converts Tyr to L-3,4-dihydroxyphenylalanine (L-DOPA), and diphenolase activity, which uses L-DOPA as a substrate to produce L-dopaquinone. The results demonstrated that the water-soluble fraction of bacterial secretion inhibited monophenolase activity but not diphenolase activity. Additionally, we discovered a compound with the molecular weight of approximately 379.2 Da and the tyrosinase inhibitory effect in which two protons were bound in the absence of copper ions and copper ions were bound instead when they were present in the water-soluble fraction of the bacterial secretion. Since the enzymatic activity of tyrosinase is copper ion-dependent, <i>Curtobacterium</i> may be able to suppress the browning caused by the copper-binding compound-induced oxidation of phenols, such as Tyr, allowing it to express a bright flash-yellow color.</p>","PeriodicalId":466,"journal":{"name":"Applied Biochemistry and Microbiology","volume":null,"pages":null},"PeriodicalIF":1.0,"publicationDate":"2024-03-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140315642","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
A Review on Microbial Alkaline Proteases: Optimization of Submerged Fermentative Production, Properties, and Industrial Applications 微生物碱性蛋白酶综述:优化浸没式发酵生产、特性和工业应用
IF 1 4区 生物学
Applied Biochemistry and Microbiology Pub Date : 2024-03-27 DOI: 10.1134/S0003683823602767
S. Mrudula
{"title":"A Review on Microbial Alkaline Proteases: Optimization of Submerged Fermentative Production, Properties, and Industrial Applications","authors":"S. Mrudula","doi":"10.1134/S0003683823602767","DOIUrl":"10.1134/S0003683823602767","url":null,"abstract":"<div><p>Due to the growing need for alkaline proteases in various industrial applications, the preference for microbial sources, such as bacteria and fungi, has surged in comparison to plant and animal-derived alternatives. These microorganisms which can be isolated from natural alkaline habitats have emerged as promising candidates for large-scale industrial production. To meet this demand, greater attention is being given to improving the enzyme yields by optimizing culture conditions employing various approaches, viz., optimization of environmental and nutritional factors, statistical methodologies for screening, strain improvement, etc. Although acidic and neutral proteases are currently in industrial use, this review focuses on alkaline proteases from various sources because of their catalytic abilities at extreme pH values. While acidic proteases do possess distinctive and valuable catalytic capabilities at extreme pH values, they are predominantly utilized in the food industry for specific applications and are primarily produced by fungi, in contrast to alkaline proteases. Considering this, the present review focuses extensively on various environmental and nutritional factors affecting alkaline protease production in submerged fermentation. Additionally, the purification methodologies adopted, and properties of alkaline proteases obtained from different sources are discussed, and the industrial applications of alkaline proteases are also highlighted.</p></div>","PeriodicalId":466,"journal":{"name":"Applied Biochemistry and Microbiology","volume":null,"pages":null},"PeriodicalIF":1.0,"publicationDate":"2024-03-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140315634","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
Shaking Hands with Streptococcal Antibody-Degrading Enzymes for Clinical Use (Review) 与临床使用的链球菌抗体降解酶握手(综述)
IF 1 4区 生物学
Applied Biochemistry and Microbiology Pub Date : 2024-03-27 DOI: 10.1134/S0003683823602871
S. Jain, S. Srivastava, I. Gulati, K. Bhandari
{"title":"Shaking Hands with Streptococcal Antibody-Degrading Enzymes for Clinical Use (Review)","authors":"S. Jain,&nbsp;S. Srivastava,&nbsp;I. Gulati,&nbsp;K. Bhandari","doi":"10.1134/S0003683823602871","DOIUrl":"10.1134/S0003683823602871","url":null,"abstract":"<p>Antibody-degrading enzymes are one among crucial virulence factors of pathogenic bacteria and parasites for they help the inhabitant evade the attacks of the host immune system. IdeS and EndoS are two such well-characterised enzymes of <i>Streptococcus pyogenes</i> that have the ability to cleave specific peptide bonds within the hinge region of the antibody and deglycosylate the molecule leading to loss of its effector functions, including activation of complement cascade by classical pathway and bridgement of cytotoxic cells. This forms the basis for development of enzyme-based interventions for antibody-mediated clinical conditions including various autoimmune disorders, organ rejection during transplantations, and therapeutic viral vector destruction. The specificity of these enzymes is exploited in efficient proteolytic processing of anti-cancer monoclonal antibodies for their characterization and production of clinically-important fragments. Use of antibody-degrading enzymes in clinical settings comes with some unmet challenges in terms of safe application, economical production, efficient immobilization, patient-friendly delivery, and limited scope.</p>","PeriodicalId":466,"journal":{"name":"Applied Biochemistry and Microbiology","volume":null,"pages":null},"PeriodicalIF":1.0,"publicationDate":"2024-03-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140315540","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 Expression of Recombinant Human Hepatocyte Growth Factor in Pichia pastoris 重组人肝细胞生长因子在 Pichia pastoris 中的表达
IF 1 4区 生物学
Applied Biochemistry and Microbiology Pub Date : 2024-03-27 DOI: 10.1134/S0003683823602391
X.-F. Song, N. Zhao, Y.-H. Dong
{"title":"The Expression of Recombinant Human Hepatocyte Growth Factor in Pichia pastoris","authors":"X.-F. Song,&nbsp;N. Zhao,&nbsp;Y.-H. Dong","doi":"10.1134/S0003683823602391","DOIUrl":"10.1134/S0003683823602391","url":null,"abstract":"<p>The aim of this study was to construct a stable and efficient eukaryotic expression system for the secretion of biologically active recombinant human hepatocyte growth factor (rhHGF). The eukaryotic expression vector pGAPZα A was chosen to express rhHGF. To ensure the presence of the secondary structure, we inserted the enterokinase sequence between Arg494 and Val495. After digesting the rhHGF and pGAPZα A plasmid with Xho I and Xba I, we connected and transformed them into <i>E. coli</i> Trans10 competent cells. This resulted in the successful construction of the shuttle plasmid, pGAPZα A-rhHGF. After sequencing, we transformed the linearized pGAPZα A-rhHGF plasmid into <i>Pichia pastoris</i> GS115 using electroporation for subsequent protein expression. The expressed rhHGF samples were collected at 0, 24, 48, 72 and 96 h, purified by affinity chromatography, and tested using Western blotting. As a result, the pGAPZα A-rhHGF shuttle plasmid was constructed successfully. A positive band of approximately 80 kDa was observed in the Western blotting indicating successful expression of rhHGF. The highest expression abundance of rhHGF protein was observed at 48 h. Furthermore, we isolated and cultured primary rat hepatocytes, the harvested rhHGF protein exhibited high biological activity. This research provides experimental evidence for the eukaryotic expression of rhHGF protein and theoretical support for large-scale manufacturing.</p>","PeriodicalId":466,"journal":{"name":"Applied Biochemistry and Microbiology","volume":null,"pages":null},"PeriodicalIF":1.0,"publicationDate":"2024-03-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140315530","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
Agonists and Antagonists of GIP and GLP-1 Receptors: Recombinant Species-Specific Variants and Mutual Neutralization of Activity GIP 和 GLP-1 受体的激动剂和拮抗剂:重组物种特异性变体和活性相互中和
IF 1 4区 生物学
Applied Biochemistry and Microbiology Pub Date : 2024-01-12 DOI: 10.1134/S0003683823090065
M. Yu. Kopaeva, E. P. Sannikova, E. S. Bobrov, I. I. Gubaidullin, N. V. Bulushova, D. G. Kozlov
{"title":"Agonists and Antagonists of GIP and GLP-1 Receptors: Recombinant Species-Specific Variants and Mutual Neutralization of Activity","authors":"M. Yu. Kopaeva,&nbsp;E. P. Sannikova,&nbsp;E. S. Bobrov,&nbsp;I. I. Gubaidullin,&nbsp;N. V. Bulushova,&nbsp;D. G. Kozlov","doi":"10.1134/S0003683823090065","DOIUrl":"10.1134/S0003683823090065","url":null,"abstract":"<div><p>The development of recombinant modified derivatives of human glucose-dependent insulinotropic polypeptide (rmGIP) and glucagon-like peptide 1 (rmGLP-1) has been carried out as part of the project to create a prototype of a two-component drug. The aims were to increase the activity of GIP derivatives and obtain antagonists of GIP and GLP-1 receptors for selective neutralization of the activity of the corresponding components of a promising drug. For this purpose, well-known mutations were introduced into the structure of the basic human rmGIP(1‒42)h variant: a deletion of residues 32–42 and a H18R substitution, which is species specific for the mouse/rat hormones. The hypoglycemic activity of the drugs was measured using a glucose tolerance test on healthy mice. In most cases, the engineered mutations turned out to be unexpectedly ineffective or did not affect the hypoglycemic activity of GIP derivatives at all. The maximum two-fold increase in activity was recorded only in the modified rmGIP(1‒31) rat variant, which contained both mutations simultaneously. <i>Inactivated</i> rmGIP(3‒31)rat and rmGLP-1(3‒31) derivatives, containing the deletion of two N-terminal residues, specific for natural antagonists of the GIP and GLP-1 receptors (GIPR and GLP-1R, respectively) individually exhibited the expected dose-dependent antagonistic activity. At the same time, their equimolar mixture, instead of the expected additive effect, showed a complete loss of sugar-increasing activity. Based on the obtained results, we formulated the hypothesis about the ability of metabolites of the derivatives of incretin hormones GIP and GLP-1 to interact with each other in the process of glycemic regulation. This fact should be taken into account when studying the mechanisms of glycemic control and developing drugs based on agonists and antagonists of GIP and GLP-1 receptors.</p></div>","PeriodicalId":466,"journal":{"name":"Applied Biochemistry and Microbiology","volume":null,"pages":null},"PeriodicalIF":1.0,"publicationDate":"2024-01-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142411444","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
Optimization of Factors Affecting the Efficiency of Agrobacterium-Mediated Transformation of Wolffia arrhiza 优化影响农杆菌介导的狼尾草转化效率的因素
IF 1 4区 生物学
Applied Biochemistry and Microbiology Pub Date : 2024-01-12 DOI: 10.1134/S0003683823090089
A. N. Shvedova, P. A. Khvatkov, S. V. Dolgov
{"title":"Optimization of Factors Affecting the Efficiency of Agrobacterium-Mediated Transformation of Wolffia arrhiza","authors":"A. N. Shvedova,&nbsp;P. A. Khvatkov,&nbsp;S. V. Dolgov","doi":"10.1134/S0003683823090089","DOIUrl":"10.1134/S0003683823090089","url":null,"abstract":"<div><p>Plants of the duckweed family (<i>Lemna</i>, <i>Spirodela</i>) are actively used as expression platforms for the production of recombinant proteins due to a number of their advantages over other crops (small size, rapid vegetative reproduction, and high protein content in tissues). Rootless wolffia (<i>Wolffia arrhiza</i> (L.) Horkel ex Wimm) is a promising producer from the Lemnaceae family. Current <i>Wolffia</i> transformation protocols have an efficiency of approximately 0.36%. Based on transient expression, we have identified the most efficient <i>Agrobacterium</i> strain, EHA105, for the <i>W. arrhiza</i> transformation. An effective balance of growth regulators was selected for use at the first passage of cultivation and selection of transformed explants: 2,4-dichlorophenoxyacetic acid, 2.5 mg/L and 6-benzylaminopurine, 1.5 mg/L. The transformation efficiency of <i>W. arrhiza</i> was 0.54%, which is 1.5 times higher than in known protocols.</p></div>","PeriodicalId":466,"journal":{"name":"Applied Biochemistry and Microbiology","volume":null,"pages":null},"PeriodicalIF":1.0,"publicationDate":"2024-01-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139459234","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
A Study of the Influence of L-Lysine and its Transporter LysP on the Characteristics of the L-Threonine Producer Strain 赖氨酸及其转运体 LysP 对赖氨酸生产菌株特性的影响研究
IF 1 4区 生物学
Applied Biochemistry and Microbiology Pub Date : 2024-01-12 DOI: 10.1134/S0003683823090090
A. A. Khozov, D. M. Bubnov, T. V. Vybornaya, M. D. Kudina, A. A. Stepanova, O. E. Melkina, S. V. Molev, S. S. Filippova, A. I. Netrusov, S. P. Sineoky
{"title":"A Study of the Influence of L-Lysine and its Transporter LysP on the Characteristics of the L-Threonine Producer Strain","authors":"A. A. Khozov,&nbsp;D. M. Bubnov,&nbsp;T. V. Vybornaya,&nbsp;M. D. Kudina,&nbsp;A. A. Stepanova,&nbsp;O. E. Melkina,&nbsp;S. V. Molev,&nbsp;S. S. Filippova,&nbsp;A. I. Netrusov,&nbsp;S. P. Sineoky","doi":"10.1134/S0003683823090090","DOIUrl":"10.1134/S0003683823090090","url":null,"abstract":"<div><p>In this work, it was shown for the first time that inactivation of the L-lysine uptake transport system from the external environment leads to an increase in the level of L-threonine synthesis by the <i>Escherichia coli</i> strain that produces it, while the addition of lysine to the culture medium reduces the productivity of the unmodified strain, which indicates the influence of the intracellular pool of lysine on the efficiency of threonine biosynthesis. A study of the possible mechanisms of this influence showed that neither the previously known inhibition of aspartate kinase III (LysC) activity, nor the repression of the synthesis of aspartate semialdehyde dehydrogenase (Asd) and glutamate dehydrogenase (GdhA) individually are reasons for the decrease in culture productivity. The results we obtained may indicate both the presence of a previously unknown mechanism for the regulation of threonine metabolism by lysine and the fact that several enzymes in the threonine biosynthesis pathway are simultaneously affected by this amino acid. At the same time, changing the permeability of the membrane to lysine, or reducing its intracellular concentration as a result of changing the efficiency of its biosynthesis, is a promising approach for improving threonine-producing strains.</p></div>","PeriodicalId":466,"journal":{"name":"Applied Biochemistry and Microbiology","volume":null,"pages":null},"PeriodicalIF":1.0,"publicationDate":"2024-01-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142411441","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
New pAraDH2 Promoter for Metabolic Engineering of the Yarrowia lipolytica Yeast 用于脂溶性亚罗酵母代谢工程的新型 pAraDH2 启动子
IF 1 4区 生物学
Applied Biochemistry and Microbiology Pub Date : 2024-01-12 DOI: 10.1134/S0003683823090120
M. O. Taratynova, Iu. M. Fediayeva, D. A. Dementiev, O. E. Melkina, T. V. Yuzbashev, S. P. Sineoky, E. Y. Yuzbasheva
{"title":"New pAraDH2 Promoter for Metabolic Engineering of the Yarrowia lipolytica Yeast","authors":"M. O. Taratynova,&nbsp;Iu. M. Fediayeva,&nbsp;D. A. Dementiev,&nbsp;O. E. Melkina,&nbsp;T. V. Yuzbashev,&nbsp;S. P. Sineoky,&nbsp;E. Y. Yuzbasheva","doi":"10.1134/S0003683823090120","DOIUrl":"10.1134/S0003683823090120","url":null,"abstract":"<p>The ability to utilize a number of polyhydric alcohols as a sole carbon source has been studied in the <i>Yarrowia lipolytica</i> yeast. The efficiency of the promoter of the <i>Y. lipolytica</i> native <i>AraDH2</i> gene encoding the enzyme D-mannitol/D-arabitol dehydrogenase was assessed during yeast growth on a minimal medium with different carbon sources. For this purpose, the promoter region of the <i>AraDH2</i> gene was transcriptionally fused with the green fluorescent protein <i>hrGFP</i> gene, and the construct was used to transform <i>Y. lipolytica</i>. A β-carotene producing strain of <i>Y. lipolytica</i> was created using the described promoter; the strain carried the <i>Mucor circinelloides CarRP</i> and <i>CarB</i> genes encoding the bifunctional enzyme phytoene synthase/lycopene β-cyclase (CarRP) and phytoene dehydrogenase (CarB) as well as the <i>GGPPSs7</i> gene <i>Synechococcus</i> sp<i>.</i> geranylgeranyl pyrophosphate synthase. The nucleotide sequence encoding the fused CarRP and GGPPSs7 under the regulation of the pAraDH2 promoter and the <i>CarB</i> gene under the control of the pTEF promoter were introduced into the yeast genome. As a result, a transformant was obtained capable of producing 66.3, 121.2, and 148.9 mg/L of β-carotene after 5 days of cultivation in test tubes on media containing glycerol, sucrose, and glucose, respectively. The obtained results testify to the high potential of the pAraDH2 promoter in the field of genetic engineering.</p>","PeriodicalId":466,"journal":{"name":"Applied Biochemistry and Microbiology","volume":null,"pages":null},"PeriodicalIF":1.0,"publicationDate":"2024-01-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142411451","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
On the Question of the Metabolic Costs of the Main Metabolic Precursors in Escherichia coli 关于大肠杆菌中主要代谢前体的代谢成本问题
IF 1 4区 生物学
Applied Biochemistry and Microbiology Pub Date : 2024-01-12 DOI: 10.1134/S0003683823090041
L. I. Golubeva, E. S. Kovaleva, S. V. Mashko
{"title":"On the Question of the Metabolic Costs of the Main Metabolic Precursors in Escherichia coli","authors":"L. I. Golubeva,&nbsp;E. S. Kovaleva,&nbsp;S. V. Mashko","doi":"10.1134/S0003683823090041","DOIUrl":"10.1134/S0003683823090041","url":null,"abstract":"<div><p>The term <i>metabolic cost</i> (MС) is often used for assessment of energy consumption in the biosynthesis of various substances under different growth conditions or by different cell types. The MC of the metabolite is calculated according to a specified algorithm in universal ~P units, multiples of ATP molecules hydrolyzed to ADP and inorganic phosphate. Our analysis of the published data showed that the interpretation of the MC concept and the algorithms for its calculation, proposed by different authors, differ significantly. Since the MС is often considered in connection with system-level tasks, such as the metabolic flux analysis and the natural selection mechanisms, it seems appropriate to characterize this concept in detail. In this work, the term MС was clearly defined and used to calculate the energy consumption for the synthesis of 13 metabolic precursors of <i>Escherichia coli</i> biomass based on the modern model of the central metabolism of this bacterium. It was found that the MC, expressed in units of stored or hydrolyzed ATP molecules (~P), depends on the characteristics of the metabolism of an individual organism, its culturing conditions, and the P/O ratio, which characterizes the number of ATP molecules formed during the transfer of one electron pair to one oxygen atom in oxidative phosphorylation.</p></div>","PeriodicalId":466,"journal":{"name":"Applied Biochemistry and Microbiology","volume":null,"pages":null},"PeriodicalIF":1.0,"publicationDate":"2024-01-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142411443","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 Biotechnological Potential of Methylotrophic Yeast Komagataella phaffii (Pichia pastoris) for Assembly of Bacteriophage MS2 Virus-Like Particles 噬甲酵母 Komagataella phaffii(Pichia pastoris)组装噬菌体 MS2 病毒样颗粒的生物技术潜力
IF 1 4区 生物学
Applied Biochemistry and Microbiology Pub Date : 2024-01-12 DOI: 10.1134/S0003683823090028
L. N. Borschevskaya, T. L. Gordeeva, E. B. Pichkur, V. R. Samygina, S. P. Sineoky
{"title":"The Biotechnological Potential of Methylotrophic Yeast Komagataella phaffii (Pichia pastoris) for Assembly of Bacteriophage MS2 Virus-Like Particles","authors":"L. N. Borschevskaya,&nbsp;T. L. Gordeeva,&nbsp;E. B. Pichkur,&nbsp;V. R. Samygina,&nbsp;S. P. Sineoky","doi":"10.1134/S0003683823090028","DOIUrl":"10.1134/S0003683823090028","url":null,"abstract":"<div><p>Successful assembly of bacteriophage MS2 virus-like particles (VLPs) from a secreted recombinant capsid protein in the culture medium of the <i>Komagataella phaffii</i> methylotrophic yeast has been shown. The yield of VLPs was 5 g/L and reached 30% of the total protein of the culture liquid supernatant. The VLPs were well-ordered icosahedral structures with a diameter of 26‒28 nm, which was confirmed by transmission electron microscopy. A simple method for the isolation and purification of the VLPs was proposed, which ensures the purity of the target protein structures of more than 90%. The results we obtained can be used for development of a technology for the large-scale production of recombinant vaccines based on bacteriophage MS2 VLPs.</p></div>","PeriodicalId":466,"journal":{"name":"Applied Biochemistry and Microbiology","volume":null,"pages":null},"PeriodicalIF":1.0,"publicationDate":"2024-01-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142411462","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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