Current Research in Biotechnology最新文献

{"title":"Therapeutic potential of lipopeptide biosurfactant-fabricated copper oxide nanoparticles: Mechanistic insight into their biocompatibility using zebra fish","authors":"Tamanna Bhuyan ,&nbsp;Yugal Kishore Mohanta ,&nbsp;Kaustuvmani Patowary ,&nbsp;Surjendu Maity ,&nbsp;Debasis Nayak ,&nbsp;Kangkan Deka ,&nbsp;K. Meenakshi Sundaram ,&nbsp;Saravanan Muthupandian ,&nbsp;Hemen Sarma","doi":"10.1016/j.crbiot.2024.100227","DOIUrl":"10.1016/j.crbiot.2024.100227","url":null,"abstract":"<div><p>Nanoscale copper oxide (CuO NPs) with diameters in the 80–150 nm range has been biosynthesized using lipopeptide biosurfactant derived from <em>Bacillus vallismortis</em> and characterized by XRD and FE-SEM. The CuO NPs could be introduced as nanocarrier systems for combination therapy and a potential candidate for antibacterial, antioxidant, anticancer, and anti-diabetic activity. The antibacterial activity of CuO NPs was studied by incorporating the nanoparticles with fluorescent antibiotic Ciprofloxacin HCL (CIP) to form CIP@CuO NPs and tracked inside HEK-293 cell lines. The MIC values of CIP@CuO NPs against 1 × 10⁶ CFU ml⁻¹ <em>Pseudomonas aeruginosa</em> was determined to be 76 µg ml⁻¹and 69 µg ml⁻¹ against 1 × 10⁶ CFU ml⁻¹ <em>Staphylococcus aureus</em>. The CuO NPs were conjugated with the anticancer drug Doxorubicin (DOX) to form DOX@CuONPs, improving delivery toward cancer (HeLa) cells. The intracellular uptake of the drug-loaded CuO NPs was confirmed from confocal micrographs. Finally, the <em>in vitro</em> anti-diabetic activity of lipopeptide-coated CuO NPs was confirmed by the inhibitory activity of α-amylase. In contrast, the <em>in vivo</em> anti-diabetic efficacy of CuO NPs was validated by a significant reduction in blood glucose and glutathione levels. The CuO NPs positively affected the histopathological changes of the pancreas in induced diabetic mice. Cytotoxicity testing with Zebrafish demonstrated abnormal organ development with varying viability and hatching rates at 72 and 96 hpf, with an LC₅₀ of 45 µg/l. Aside from the various potential medicinal characteristics, the study provided valuable information on cytotoxic impact, which can be used in future investigations of their eco-toxicological impacts.</p></div>","PeriodicalId":52676,"journal":{"name":"Current Research in Biotechnology","volume":"7 ","pages":"Article 100227"},"PeriodicalIF":5.6,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2590262824000534/pdfft?md5=8d3f4605547dc3b7059e4f7c85912037&pid=1-s2.0-S2590262824000534-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141052066","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"pH-dependent hydrogels obtained by low molecular weight derivatives of aspartic acid and glutamic acid (L-Asp and L-Glu)","authors":"Daniela Tsekova,&nbsp;Vasilena Kondova,&nbsp;Konstantin Dochev,&nbsp;Borislav Anchev","doi":"10.1016/j.crbiot.2024.100257","DOIUrl":"10.1016/j.crbiot.2024.100257","url":null,"abstract":"<div><div>We report here the synthesis of two new anionic gemini surfactants, derivatives of L-Asp and L-Glu with analogous structure and their applications as low molecular weight gelators. Conditions for formation of pH-dependent hydrogels and their stability are presented and discussed. Although both compounds possess very close molecular structures, only one of them – the derivative of L-Asp, can form stable hydrogels. Loading of such a hydrogel with silver nanoparticles and the conditions of their release are also studied and described. Different methods to analyze molecular and supramolecular structures, such as NMR, FTIR, UV–VIS and SEM, are used to characterize the compounds and also to understand and follow the processes of loading and release of silver nanoparticles. It was found that a stable hydrogel can be formed only in acidic solution, while release can happen only at basic condition – over pH ≥ 9. The results obtained show that such pH-dependent hydrogels can be used for slowly and gradually supply of active compounds at necessity, expressed through changing the pH of the living tissue.</div></div>","PeriodicalId":52676,"journal":{"name":"Current Research in Biotechnology","volume":"8 ","pages":"Article 100257"},"PeriodicalIF":3.6,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142421326","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Functional study of residual iCre activity relevant for split-Cre applications","authors":"Antea Minetti ,&nbsp;Noemi Barsotti ,&nbsp;Massimo Pasqualetti","doi":"10.1016/j.crbiot.2024.100263","DOIUrl":"10.1016/j.crbiot.2024.100263","url":null,"abstract":"<div><div>Cre-lox system is a major tool in mouse molecular genetics instrumental in promoting somatic recombination to spatiotemporally control transcriptional activation/inhibition in subsets of cells or tissues <em>in vivo</em>. A critical factor behind this system may be represented by the availability of a specific promoter driving Cre expression in the cell subset of interest. Split-Cre recombinase system represents an evolution that circumvents this limitation using split N- and C-terminal domains of Cre recombinase placed under the control of two distinct promoters defining an intersectional domain where functional complementation of Cre protein fragments is obtained. This system is a valuable tool for controlling Cre recombinase activity in a spatially and temporally defined manner based on the assumption that neither N- or C-terminal Cre fragments alone have recombinase activity. However, residual recombinase activity of one of the two fragments can occur leading to confounding experimental results. In this work, we delve into characterizing functional activity of different N-terminal deleted codon-optimized Cre (iCre) isoforms to refine Split-Cre-based technologies, aiming to avoid uncontrolled recombinase events. Given the presence of several methionine residues in the amino acidic iCre sequence, we explored whether these residues could serve as potential translation start sites, resulting in truncated isoforms that might retain recombinase activity. To address this question, we tested in HEK293T cells whether site-specific recombination was retained in progressively amino-terminal deleted iCre isoforms. Our results reveal residual enzymatic activity of most amino-terminal deleted isoforms of iCre whose ATG start codon is located downstream of the commonly used split site. This insight holds significance for future refinements of the widely used Split-Cre system, providing information to avoid false positive results stemming from unwanted activity.</div></div>","PeriodicalId":52676,"journal":{"name":"Current Research in Biotechnology","volume":"8 ","pages":"Article 100263"},"PeriodicalIF":3.6,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142526261","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Production of genetically engineered designer biodiesel from yeast lipids","authors":"Benjamin Ouellet,&nbsp;A.M. Abdel-Mawgoud","doi":"10.1016/j.crbiot.2024.100189","DOIUrl":"10.1016/j.crbiot.2024.100189","url":null,"abstract":"<div><p>Biodiesels constitute a growing class of fuel in a world that is increasingly inclined towards more ecological and sustainable energy. Despite their many advantages, biodiesels have limited cold flow properties and larger NO_X emissions. These limitations are mostly attributed to the chemical compositions of biodiesels which are dictated by the chemical compositions of their feedstock oils. Accordingly, this study presents a novel approach to produce Genetically Engineered Biodiesel (GEB) whose chemical composition can be controlled by the genetic manipulation of oleaginous yeast oils for the production of designer biodiesels with improved properties and performances. Using full-factorial central composite design, the best chemical composition of an optimal biodiesel was predicted. Then, simple and combined <em>MFE1</em>, <em>PEX10</em> and <em>POX2</em> mutants of the oleaginous yeast <em>Yarrowia lipolytica</em> were constructed. These mutants showed interesting lipid profiles where their biodiesels are predicted to have better cold flow properties. These mutants showed also higher lipid titers by 2–3 folds compared to the parent strain. This study provides an approach for tailor designing of biodiesel properties and performances via genetic engineering. Moreover, it provides solutions potentially enabling biodiesel to be used as a standalone fuel in cold climates without any mixing with petrodiesel.</p></div>","PeriodicalId":52676,"journal":{"name":"Current Research in Biotechnology","volume":"7 ","pages":"Article 100189"},"PeriodicalIF":5.6,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2590262824000157/pdfft?md5=f48b6aa009728f6521fdbc1f802f8745&pid=1-s2.0-S2590262824000157-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139826723","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Reassigning the role of a mesophilic xylan hydrolysing family GH43 β-xylosidase from Bacteroides ovatus, BoExXyl43A as exo-β-1,4-xylosidase","authors":"Parmeshwar Vitthal Gavande ,&nbsp;Shyam Ji ,&nbsp;Vânia Cardoso ,&nbsp;Carlos M.G.A. Fontes ,&nbsp;Arun Goyal","doi":"10.1016/j.crbiot.2024.100191","DOIUrl":"https://doi.org/10.1016/j.crbiot.2024.100191","url":null,"abstract":"<div><p>The recombinant 40 kDa <em>Bo</em>ExXyl43A glycoside hydrolase family 43 (GH43) from bacterium <em>Bacteroides ovatus</em> exhibited highest specific activity (U/mg) against corn cob xylan (136.8), followed by Beechwood xylan (81.1), Carbosynth xylan (69.3), 4-<em>O</em>-D-methylglucuronoxylan (61.4) and Birchwood xylan (59.9). <em>Bo</em>ExXyl43A demonstrated optimal performance at 37 °C and pH 7.6 with V_max and K_m of 141.8 U/mg and 4.0 mg/mL as well as 64.1 U/mg and 6.0 mg/mL against corn cob and Birchwood xylan, respectively. The activity of <em>Bo</em>ExXyl43A increased by 48 % by addition of 10 mM Ca²⁺ ions, while 1 mM EDTA or 1 mM EGTA decreased its activity by 100 % or 42.5 %, respectively, highlighting its calcium-ion dependence. Thin-layer chromatography (TLC) analysis of <em>Bo</em>ExXyl43A hydrolysates of Birchwood and Beechwood xylan as well as that of various xylooligosaccharides (DP2-DP9) from corn cob xylan showed the release of D-xylose, identifying it as an <em>exo</em>-β-1,4-xylosidase/<em>exo</em>-β-1,4-xylanase (EC 3.2.1.-/3.2.1.37). Moreover, the time-dependent TLC analysis of xylobiose hydrolysis showed release of D-xylose units, confirming its β-xylosidase activity. <em>Bo</em>ExXyl43A also exhibited <em>exo</em>-1,4-β-xylosidase activity on Larchwood and Carbosynth xylans. Notably, it released D-xylose from α-L-Araf²-xylotriose demonstrating its activity against decorated xylooligosaccharides. <em>Bo</em>ExXyl43A's <em>exo</em>-1,4-β-xylosidase and residual β-xylosidase activity on xylan and xylobiose, respectively, could potentially enhance xylan saccharification efficiency in bioethanol-based refineries. The molecular modeling showed that <em>Bo</em>ExXyl43A has 5-bladed β-propeller structure with a very shallow active-site having −1, +1 and + 2 subsites, which could accommodate three D-xylose units of longer xylan like xylododecaose thus supporting its exoxylosidase activity.</p></div>","PeriodicalId":52676,"journal":{"name":"Current Research in Biotechnology","volume":"7 ","pages":"Article 100191"},"PeriodicalIF":5.6,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2590262824000170/pdfft?md5=85bbdabc14d35daf9f93605f5c740482&pid=1-s2.0-S2590262824000170-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140030126","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Differential effect of nine cinnamic acid derivatives on the biocatalytic activity of Candida antarctica lipase type B","authors":"Federico Zappaterra ,&nbsp;Domenico Meola ,&nbsp;Francesco Presini ,&nbsp;Simona Aprile ,&nbsp;Valentina Venturi ,&nbsp;Chiara Nosengo ,&nbsp;Chiara De Luca ,&nbsp;Martina Catani ,&nbsp;Lindomar Alberto Lerin ,&nbsp;Pier Paolo Giovannini","doi":"10.1016/j.crbiot.2024.100231","DOIUrl":"https://doi.org/10.1016/j.crbiot.2024.100231","url":null,"abstract":"<div><p>Naturally occurring cinnamic acid derivatives are a broad family of aromatic carboxylic acids with bioactive properties. Among the cinnamic acid derivatives, for instance, are ferulic acid and caffeic acid, which have been widely studied for their antioxidant and anti-inflammatory properties. These active ingredients are mostly poorly soluble in water, which greatly limits their bioavailability. To increase the bioavailability of these acids, green esterification protocols can be developed exploiting lipases. In particular, this article reports the process optimization for the enzymatic esterification of nine cinnamic acid derivatives with erythritol, a polyol highly soluble in water. The study explores how the different substituents present on the aromatic ring of the cinnamic acid derivatives affect the catalytic capacity of the <em>Candida antarctica</em> lipase type B. The study, conducted through both molecular docking and experimental evidence, shows how hydroxyl groups on the aromatic ring can strongly limit the conversion of the acids to the corresponding esters. At the same time, the degree of unsaturation of the derivative also influences the favorable poses in the active site of the lipase. The best results (yields over 95 %) were obtained with 10 g/L of lipase, a temperature of 90 °C, molar ratio (acid/alcohol) of 3:1, for 72 h of reaction time.</p></div>","PeriodicalId":52676,"journal":{"name":"Current Research in Biotechnology","volume":"8 ","pages":"Article 100231"},"PeriodicalIF":3.6,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2590262824000571/pdfft?md5=b874724fa4df134f59458159b3b02bf1&pid=1-s2.0-S2590262824000571-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141434057","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Peptide lipidation and shortening optimises antibacterial, antibiofilm and membranolytic actions of an amphiphilic polylysine-polyphenyalanine octapeptide","authors":"Bruno Mendes ,&nbsp;Charlotte Edwards-Gayle ,&nbsp;Glyn Barrett","doi":"10.1016/j.crbiot.2024.100240","DOIUrl":"10.1016/j.crbiot.2024.100240","url":null,"abstract":"<div><p>The demand for broad-spectrum antibacterial agents continues with increasing rates of resistance of microbial pathogens to traditional antibiotics. Peptides and lipopeptides are gaining traction as promising novel, class-reference antibiotics for tackling difficult-to-treat infections caused by multi-drug resistant bacteria. To identify novel candidates and expand treatment options in clinical settings, we explored the <em>in vitro</em> antibacterial potential and mode of action of a short octapeptide combining a cationic block of four lysines and a highly hydrophobic segment of four phenylalanines (K4F4), and two K4F4-inspired lipopeptides (Palmitoyl-K4F4 and K4-NH-Palmitoyl). Preliminary AI-based screening had revealed the antimicrobial potential of the K4F4 peptide coupled with limited haemolytic activity. Broth dilution and haemolytic assays have confirmed these <em>in silico</em> predictions. Overall, our lipidated peptides were more active at lower MIC values compared to non-lipidated species, indicating the beneficial impact of tailing lipidation on design of peptide-based antimicrobials. An integrated view of the membrane-active mechanism of these novel therapeutic templates was obtained using a combination of flow cytometry, fluorescence microscopy and dye-based permeabilization assays. K4F4 and its lipidated derivatives act via a fast-disrupting mechanism without inducing bacterial resistance mechanisms in a long-term exposure assay. A K4F4-inspired lipopeptide together with its shorter version (K4-NH-Palmitoyl), were more stable in environments closer emulating physiological conditions, showing a higher antibacterial response in physiological salts and serum than their parent peptide. Our findings reveal the antibacterial and antibiofilm potential of a novel polylysine-polyphenyalanine peptide and highlight the significant contribution of lipidation and shortening as molecular engineering strategies to improve and guide the future design of next-generation membrane-targeting antibiotics.</p></div>","PeriodicalId":52676,"journal":{"name":"Current Research in Biotechnology","volume":"8 ","pages":"Article 100240"},"PeriodicalIF":3.6,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2590262824000662/pdfft?md5=fddf19f74fab0f84efe1a00be76e50af&pid=1-s2.0-S2590262824000662-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141951456","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Biodegradation of (Aminomethyl)phosphonic acid (AMPA) by isolated microbial consortia extracted from biological filters at drinking water treatment plants","authors":"Laura Pickering ,&nbsp;Miles Folkes ,&nbsp;Barrie Holden ,&nbsp;Peter Jarvis ,&nbsp;Pablo Campo ,&nbsp;Francis Hassard","doi":"10.1016/j.crbiot.2024.100248","DOIUrl":"10.1016/j.crbiot.2024.100248","url":null,"abstract":"<div><p>The widespread use of glyphosate has significantly increased its presence in drinking water sources. Aminomethylphosphonic Acid (AMPA), a breakdown product of glyphosate, is challenging to remove from water using conventional treatment methods, posing risks to public health and environmental safety. This work investigates the biodegradation of AMPA by bacteria isolated from three environmental sources, with a focus on determining their potential application in water treatment systems. Two samples were collected from granular activated carbon (GAC) filters of different operational durations at a water treatment facility, and one sample was taken from soil that had historically been treated with glyphosate-based herbicides. Bacterial isolates capable of degrading AMPA were identified from these samples through selective enrichment, and kinetic degradation experiments were then conducted to assess their effectiveness. In environmental samples, after 48 hrs AMPA removal was &gt; 70 % using GAC from an active treatment plant and soil samples removed 19 %. After bacterial isolation a consortium was isolated and from these four isolates were identified, comprising three species, including novel AMPA degraders M−S3 and M−SS (<em>Myroides sp</em>. mNGS23), and P-S92 (<em>Pseudochrobactrum saccharolyticum</em>). Within both minimal media supplemented with AMPA and raw untreated showing substrate concentrations above 10 mg/L whilst the specific degradation rates saw a decrease in substrate concentrations above 100 mg/L. AMPA removal occured in pilot scale sand filters augmented with P-S92 but removal was inconsistent. These findings show the potential of using biodegradation as an effective treatment strategy for AMPA removal from water. The identification of AMPA-degrading bacteria offers a promising solution for enhancing the removal of this persistent pollutant from contaminated waters. Further research is recommended to explore the full-scale application of these isolates in water treatment processes. This study contributes to the development of sustainable water treatment technologies by harnessing the natural degradative capacities of environmental bacteria.</p></div>","PeriodicalId":52676,"journal":{"name":"Current Research in Biotechnology","volume":"8 ","pages":"Article 100248"},"PeriodicalIF":3.6,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2590262824000741/pdfft?md5=e374ae94461dd0bd9ef172b781e1577e&pid=1-s2.0-S2590262824000741-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142152050","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Deciphering the gut microbiome: The revolution of artificial intelligence in microbiota analysis and intervention","authors":"Mohammad Abavisani ,&nbsp;Alireza Khoshrou ,&nbsp;Sobhan Karbas Foroushan ,&nbsp;Negar Ebadpour ,&nbsp;Amirhossein Sahebkar","doi":"10.1016/j.crbiot.2024.100211","DOIUrl":"10.1016/j.crbiot.2024.100211","url":null,"abstract":"<div><p>The human gut microbiome is an intricate ecosystem with profound implications for host metabolism, immune function, and neuroendocrine activity. Over the years, studies have strived to decode this microbial universe, especially its interactions with human health and underlying metabolic processes. Traditional analyses often struggle with the complex interplay within the microbiome due to presumptions of microbial independence. In response, machine learning (ML) and deep learning (DL) provide advanced multivariate and non-linear analytical tools that adeptly capture the complex interactions within the microbiota. With the influx of data from metagenomic next-generation sequencing (mNGS), there's an increasing reliance on these artificial intelligence (AI) subsets to derive actionable insights. This review delves deep into the cutting-edge ML techniques tailored for human gut microbiota research. It further underscores the potential of gut microbiota in shaping clinical diagnostics, prognosis, and intervention strategies, pointing to a future where computational methods bridge the gap between microbiome knowledge and targeted health interventions.</p></div>","PeriodicalId":52676,"journal":{"name":"Current Research in Biotechnology","volume":"7 ","pages":"Article 100211"},"PeriodicalIF":5.6,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2590262824000376/pdfft?md5=245f0081d11c539786fd3fec74e20573&pid=1-s2.0-S2590262824000376-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140795710","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Comparative evaluation of myogenic potential of purebred chicken muscle stem cells","authors":"Hyun Young Jung ,&nbsp;Minsu Kim ,&nbsp;Chang-Kyu Lee ,&nbsp;Myung Yeo ,&nbsp;Sea Hwan Sohn ,&nbsp;Cheorun Jo","doi":"10.1016/j.crbiot.2024.100241","DOIUrl":"10.1016/j.crbiot.2024.100241","url":null,"abstract":"<div><p>We evaluated the myogenic potential of muscle stem cells (MuSCs) derived from three distinct chicken purebreds—Rhode Island Red (RIR), White Leghorn (WL), and Cornish (CN). Chicken MuSCs were isolated from the breast muscles of chicken embryos on embryonic day 18 using a pre-plating method. Subsequently, the cells underwent a three-day proliferation period, followed by a three-day differentiation phase. WL MuSCs exhibited higher myogenic potential initially compared to RIR and CN. Despite a relatively lower proliferation rate, WL demonstrated a higher proportion of PAX7-positive cells and showed higher expression of myogenic regulatory factor genes than the other breeds. During differentiation, MuSCs from WL formed thicker muscle fibers and showed the highest proportion of myosin-heavy chain-positive cells than MuSCs from other breeds. Additionally, the expression of <em>MYH1</em>, associated with muscle maturation, was highest in WL. Overall, this finding suggests that the myogenic potential of MuSCs from WL surpasses those of RIR and CN. Given the fact that WL is primarily used for egg laying with a low growth rate in the traditional poultry industry, the present study highlights the crucial distinction between selecting production characteristics in conventional animal husbandry and those desirable for cultured meat production.</p></div>","PeriodicalId":52676,"journal":{"name":"Current Research in Biotechnology","volume":"8 ","pages":"Article 100241"},"PeriodicalIF":3.6,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2590262824000674/pdfft?md5=6a87d9b92152f144f5a06ea51c0b0bf6&pid=1-s2.0-S2590262824000674-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141838358","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}