Applied Microbiology and Biotechnology最新文献

{"title":"Biosynthesis of ergothioneine: current state, achievements, and perspectives","authors":"Shun Sato,&nbsp;Azusa Saika,&nbsp;Tatsuyuki Koshiyama,&nbsp;Yukihiro Higashiyama,&nbsp;Tokuma Fukuoka,&nbsp;Tomotake Morita","doi":"10.1007/s00253-025-13476-4","DOIUrl":"10.1007/s00253-025-13476-4","url":null,"abstract":"<p>Ergothioneine (EGT) is a derivative of the amino acid L-histidine that is well known for its strong antioxidant properties. Recent studies on the functional characterization of EGT in both in vivo and in vitro systems have demonstrated its potential applications in pharmaceuticals, food, and cosmetics. The growing demand for EGT in novel applications necessitates the development of safe and cost-effective mass production technologies. Consequently, microbial fermentation for EGT biosynthesis has attracted significant attention. This review focuses on the biosynthesis of EGT via microbial fermentation, explores its biosynthetic mechanisms, and summarizes the latest advancements for industrial EGT production using engineered microbial strains.</p><p>• <i>Ergothioneine (EGT) is an L-histidine derivative with strong antioxidant property.</i></p><p>• <i>Recent studies have revealed certain groups of microbes produce EGT naturally.</i></p><p>• <i>Superior EGT producers by genetic modification have been created.</i></p>","PeriodicalId":8342,"journal":{"name":"Applied Microbiology and Biotechnology","volume":"109 1","pages":""},"PeriodicalIF":3.9,"publicationDate":"2025-04-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00253-025-13476-4.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143821966","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Harnessing the power of biosensors for environmental monitoring of pesticides in water","authors":"Filipa Mendes,&nbsp;Beatriz O. Machado,&nbsp;Bruno B. Castro,&nbsp;Maria João Sousa,&nbsp;Susana R. Chaves","doi":"10.1007/s00253-025-13461-x","DOIUrl":"10.1007/s00253-025-13461-x","url":null,"abstract":"<p>The current strong reliance on synthetic chemicals, namely pesticides, is far from environmentally sustainable. These xenobiotics contribute significantly to global change and to the current biodiversity crisis, but have been overlooked when compared to other agents (e.g., climate change). Aquatic ecosystems are particularly vulnerable to pesticides, making monitoring programs essential to preserve ecosystem health, safeguard biodiversity, ensure water quality, and mitigate potential human health risks associated with contaminated water sources. Biosensors show great potential as time/cost-effective and disposable systems for the high-throughput detection (and quantification) of these pollutants. In this mini-review, we provide an overview of biosensors specifically developed for environmental water monitoring, covering different pesticide classes (and active ingredients), and types of biosensors (according to the bio-recognition element) and transducers, as well as the nature of sample matrices analyzed. We highlight the variety of biosensors that have been developed and successfully applied to detection of pesticides in aqueous samples, including enzymatic biosensors, immunosensors, aptasensors, and whole cell–based biosensors. While most biosensors have been designed to detect insecticides, expanding their compound target range could significantly streamline monitoring of environmental contaminants. Despite limitations related to stability, reproducibility, and interference from environmental factors, biosensors represent a promising and sustainable technology for pesticide monitoring in the aquatic environments, offering sensitivity and specificity, as well as portability and real-time results. We propose that biosensors would be most effective as an initial screening step in a tiered assessment, complementing conventional methods.</p><p>• <i>Pesticides harm aquatic ecosystems and biodiversity, requiring better monitoring</i></p><p>• <i>Biosensors offer cost-effective solutions to detect pesticides in water samples</i></p><p>• <i>Biosensors complement conventional methods as a sustainable tool for initial screens</i></p>","PeriodicalId":8342,"journal":{"name":"Applied Microbiology and Biotechnology","volume":"109 1","pages":""},"PeriodicalIF":3.9,"publicationDate":"2025-04-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00253-025-13461-x.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143821967","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Mycotoxin-free Aspergillus oryzae strain lineage for alternative and novel protein production at industrial scale","authors":"Jan Lehmbeck,&nbsp;Birgitte Andersen,&nbsp;Javier Sáez-Sáez,&nbsp;Jens Christian Frisvad,&nbsp;José Arnau","doi":"10.1007/s00253-025-13482-6","DOIUrl":"10.1007/s00253-025-13482-6","url":null,"abstract":"<p>Advanced industrial strains of <i>Aspergillus oryzae</i> have been used for decades for the production of recombinant proteins including food and feed enzymes at large scale. The <i>A. oryzae</i> strain lineage evaluated in this review derives from the proprietary Novozymes (now Novonesis) strain collection. <i>A. oryzae</i> wild-type strains have the potential to produce three different mycotoxins (aflatoxins (AFL), cyclopiazonic acid (CPA), and 3-nitropropionic acid (3-NPA)). Here, we review the work originally performed at Novozymes to identify a strain (BECh1) that contained a large chromosomal deletion comprising both AFL and CPA gene clusters, significantly improving the safety of the lineage. The description of the deleted region is presented here. As the genetic basis for 3-NPA biosynthesis was recently revealed, we describe here that this <i>A. oryzae</i> lineage contains an additional large deletion that encompasses the 3-NPA biosynthetic genes <i>npaA</i> and <i>npaB</i>, thereby rendering the strains unable to produce any mycotoxin. Further strain development has resulted in strains devoid of penicillin production by inactivation of the penicillin G gene cluster (<i>penG</i>). This strain lineage represents the first example of mycotoxin-free <i>A. oryzae</i> for production of recombinant (alternative) novel food proteins. Recently, bovine beta-lactoglobulin made using a strain of this lineage has received GRAS status and can be commercialized for use in food in the USA. With its history of safe use in food and feed, the lack of toxigenic potential and the ability to differentiate strains with modern technologies, this <i>A. oryzae</i> strain can be considered safe as other organisms with a Quality Presumption of Safety (QPS) status in Europe. QPS is not applicable to filamentous fungi and only granted at the species level to bacteria and a few yeast species. We suggest modernizing the QPS concept to become strain rather than species specific and present arguments to qualify this strain lineage as QPS or QPS-like.</p><p><i>• The biosynthetic genes for 3-nitropropionic acid have been recently characterized.</i></p><p><i>• An industrial strain lineage for food protein production lacks all known mycotoxin genes.</i></p><p><i>• Proteins produced in this mycotoxin-free lineage should entail lower regulatory requirements.</i></p>","PeriodicalId":8342,"journal":{"name":"Applied Microbiology and Biotechnology","volume":"109 1","pages":""},"PeriodicalIF":3.9,"publicationDate":"2025-04-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00253-025-13482-6.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143824587","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Identification of protein-degraders in an anaerobic digester by protein stable isotope probing and metagenomics","authors":"Zhe Deng,&nbsp;Jan Struckmann Poulsen,&nbsp;Jeppe Lund Nielsen,&nbsp;David G. Weissbrodt,&nbsp;Henri Spanjers,&nbsp;Jules B. van Lier","doi":"10.1007/s00253-025-13483-5","DOIUrl":"10.1007/s00253-025-13483-5","url":null,"abstract":"<p>Presence of carbohydrates hampers protein degradation in anaerobic digesters. To understand this phenomenon, we used proteogenomics to identify the active protein-degraders in the presence of low and high carbohydrates concentrations. Active metabolic pathways of the identified protein-degraders were investigated using proteomics with ¹³C-protein substrates (protein stable isotope probing). Results showed that 1) <i>Acinetobacter</i> was the active protein-degraders under both protein-fed and protein-glucose mixture-fed conditions, 2) the relative abundance of <i>Acinetobacter</i> was not affected by the presence of carbohydrates, 3) the incorporation of the ¹³C-labelled protein substrate was predominantly observed in outer membrane-bound proteins and porin proteins, which are associated with proteinases or the transportation of amino acids across the cell wall. The <i>Acinetobacter</i> metabolic model and the incubation conditions suggested that glucose and proteins were degraded through anaerobic respiration. The negative impact of carbohydrates on protein biodegradation was attributed to <i>Acinetobacter</i>'s preference for carbohydrates. This work highlights that efficient degradation of protein and carbohydrate mixtures in anaerobic digesters requires a staged or time-phased approach and enrichment of active protein-degraders, offering a new direction for process optimization in anaerobic digestion systems.</p><p>• <i>Acinetobacter identified for the first time as main anaerobic protein-degrader</i></p><p>• <i>Metabolic model revealed protein degradation via anaerobic respiration</i></p><p>• <i>Metabolic pathway analysis indicated SO</i>_<i>4</i>^<i>2−</i><i> or Fe</i>^<i>3+</i><i> as terminal electron acceptors</i></p>","PeriodicalId":8342,"journal":{"name":"Applied Microbiology and Biotechnology","volume":"109 1","pages":""},"PeriodicalIF":3.9,"publicationDate":"2025-04-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00253-025-13483-5.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143809222","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Candida albicans: the current status regarding vaginal infections","authors":"Margarida Faustino,&nbsp;Carlos M. H. Ferreira,&nbsp;Ana Margarida Pereira,&nbsp;Ana P. Carvalho","doi":"10.1007/s00253-025-13478-2","DOIUrl":"10.1007/s00253-025-13478-2","url":null,"abstract":"<p>Vaginal infections caused by <i>Candida albicans</i> are a significant global health concern due to their recurrence and negative impact on quality of life. This review examines the pathogenesis of <i>C. albicans</i> infections, emphasizing critical virulence factors such as biofilm formation, adherence, and phenotypic switching. Risk factors include immune system suppression, antibiotic use, and hormonal changes, all of which can lead to fungal overgrowth and infection. Current prevention and/or treatment strategies primarily rely on antifungal therapies, personal hygiene practices, and probiotics. However, challenges like antifungal resistance, recurrence, and limited treatment efficacy highlight the need for innovative approaches. Therefore, emerging methods such as novel antifungal agents, vaccines, and nanotechnology-based delivery systems offer promising advancements to improve infection control. Additionally, the immune system plays a key role in preventing <i>C. albicans</i> infections, with both innate and adaptive immunity acting to restrict fungal colonization and growth. Commercially available products, such as antifungal creams, vaginal probiotics, and hygiene solutions, are practical options but often lack long-term efficacy. Persistent challenges, including resistance, patient noncompliance, and restricted access to emerging therapies, hinder comprehensive prevention and treatment efforts. Thus, future research should focus on promoting interdisciplinary approaches, integrating personalized medicine, and enhancing healthcare accessibility. This review intends to present the current state of the art within the abovementioned issues and to enhance the understanding of the multifactorial nature of <i>C. albicans</i> infections and advanced prevention strategies, which are essential to reduce the burden of vaginal candidiasis worldwide and improve patient quality of life outcomes.</p><p>• <i>Candida albicans pathogenesis involves biofilms, adherence, and phenotypic switching.</i></p><p>• <i>Vaccines, nanotechnology, and new drugs offer improved prevention and treatment.</i></p><p>• <i>Addressing antifungal resistance and patient compliance is key for prevention success.</i></p>","PeriodicalId":8342,"journal":{"name":"Applied Microbiology and Biotechnology","volume":"109 1","pages":""},"PeriodicalIF":3.9,"publicationDate":"2025-04-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00253-025-13478-2.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143818291","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Novel processes to obtain pneumococcal surface proteins for vaccines","authors":"Viviane Maimoni Gonçalves","doi":"10.1007/s00253-025-13440-2","DOIUrl":"10.1007/s00253-025-13440-2","url":null,"abstract":"<p>Current pneumococcal vaccines are based on the protection offered by capsular polysaccharides from only a few from &gt; 100 serotypes; therefore, serotype-independent vaccines composed of pneumococcal surface proteins are being developed. Despite the immense number of publications on the discovery, characterization, and evaluation of new pneumococcal vaccine candidates, there are very few that describe the bioprocess development, which is an essential step to generate material for pre-clinical and clinical tests, to obtain enough protein amount for physical–chemical, biochemical, and biological characterization, and to understand critical product and process attributes. Here, aspects of production and purification processes of pneumococcal surface proteins are reviewed, the most common bioreactor cultivation strategies are discussed, and important features of the purification process are explored to bring new insights about the correlation between protein structure and chromatography. The process development oriented to an industrial scale is an essential step for the success of novel protein-based pneumococcal vaccines and can preclude problems that could be hardly identified at flask scale production. Moreover, the early bioprocess development should favor a smooth scale-up and transfer of the process to GMP facilities for future production of new pneumococcal vaccines.</p><p>• <i>Early bioprocess development is crucial to advancing pneumococcal protein vaccines.</i></p><p>• <i>Bioreactor cultivation can help to identify possible process bottlenecks.</i></p><p>• <i>Structural features of similar proteins can orient purification process development.</i></p>","PeriodicalId":8342,"journal":{"name":"Applied Microbiology and Biotechnology","volume":"109 1","pages":""},"PeriodicalIF":3.9,"publicationDate":"2025-04-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00253-025-13440-2.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143818289","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Production and application of peptidyl-lys metalloendopeptidase: advances, challenges, and future perspectives","authors":"Uzair Ahmed,&nbsp;Katrin Ochsenreither,&nbsp;Thomas Eisele","doi":"10.1007/s00253-025-13473-7","DOIUrl":"10.1007/s00253-025-13473-7","url":null,"abstract":"<div><p>Peptidyl-lys metalloendopeptidases (PKMs) are enzymes that selectively cleave peptide bonds at the N-terminus of lysine residues present in the P1′ position, making them valuable tools in proteomics. This mini-review presents an overview of PKMs, covering their traditional production from native sources, recent advances in recombinant production, and the current limitations in availability. The historical and current applications of PKMs in proteomics are discussed, highlighting their role in protein sequencing, peptide mapping, and mass spectrometry-based studies. Advances in recombinant technology now enable tailored modifications to PKM, allowing it to function not only as a sister enzyme to LysC but also to trypsin, thereby enhancing its suitability for specific analytical applications. The mini-review concludes with a forward-looking statement on PKM research, emphasizing the potential to broaden its use in novel proteomic methods and other applications.</p></div>","PeriodicalId":8342,"journal":{"name":"Applied Microbiology and Biotechnology","volume":"109 1","pages":""},"PeriodicalIF":3.9,"publicationDate":"2025-04-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00253-025-13473-7.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143809221","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Application of a replicative targetable vector system for difficult-to-manipulate streptomycetes","authors":"Juan Pablo Gomez-Escribano,&nbsp;Alina Zimmermann,&nbsp;Shu-Ning Xia,&nbsp;Meike Döppner,&nbsp;Julia Moschny,&nbsp;Chambers C. Hughes,&nbsp;Yvonne Mast","doi":"10.1007/s00253-025-13477-3","DOIUrl":"10.1007/s00253-025-13477-3","url":null,"abstract":"<p>The low frequency of homologous recombination together with poor efficiency in introducing DNA into the cell are the main factors hampering genetic manipulation of some bacterial strains. We faced this problem when trying to construct mutants of <i>Streptomyces iranensis</i> DSM 41954, a strain in which conjugation is particularly inefficient, and suicidal vectors had failed to yield any exconjugants. In this work, we report the construction and application of a conjugative replicative vector, pDS0007, which allows selection of exconjugants even with poor conjugation efficiency. The persistence of the construct inside the cell for as long as required facilitates the homologous recombination events leading to single and double crossovers. While it was confirmed that the vector is frequently lost without selection, the recognition sequence for the I-SceI endonuclease was included in the backbone of pDS0007. The presence of a I-SceI recognition sequence would allow to force the loss of the vector and the appearance of double crossover recombinants by introducing a second construct (e.g. pIJ12742) that expresses a <i>Streptomyces</i> codon–optimised gene encoding the I-SceI endonuclease. To facilitate screening for vector-free clones, the construct also carries a <i>Streptomyces</i> codon–optimised <i>gusA</i> gene encoding the β-glucuronidase expressed from a constitutive promoter. We prove the usefulness of this vector and strategy with the strain <i>S. iranensis</i> DSM 41954, in which we could readily delete an essential gene of a newly discovered biosynthetic pathway for a phosphonate-containing natural product, which led to loss of phosphonate production according to ³¹P NMR spectroscopy.</p><p><i>• pDS0007 is a new vector for gene-targeting in difficult-to-manipulate streptomycetes.</i></p><p><i>• pDS0007 is self-replicative but easy to cure, targetable and allows visual screening.</i></p><p><i>• pDS0007 was used to prove the discovery of a novel phosphonate biosynthetic pathway.</i></p>","PeriodicalId":8342,"journal":{"name":"Applied Microbiology and Biotechnology","volume":"109 1","pages":""},"PeriodicalIF":3.9,"publicationDate":"2025-04-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00253-025-13477-3.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143818290","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Identification of chicken-derived antibodies targeting the Candida albicans Als3 protein","authors":"Chi-Hsin Lee,&nbsp;Chao-Jung Wu,&nbsp;Fang-Yi Yen,&nbsp;Jia-Yun Chiang,&nbsp;Ting-Jing Shen,&nbsp;Sy-Jye Leu,&nbsp;Chuang-Rung Chang,&nbsp;Hsiu-Jung Lo,&nbsp;Bor-Yu Tsai,&nbsp;Yan-Chiao Mao,&nbsp;Valencia Andriani,&nbsp;Priskila Cherisca Thenaka,&nbsp;Wei-Chu Wang,&nbsp;Yu-Pin Chao,&nbsp;Yi-Yuan Yang","doi":"10.1007/s00253-025-13469-3","DOIUrl":"10.1007/s00253-025-13469-3","url":null,"abstract":"<p><i>Candida albicans</i> is a major opportunistic pathogen, responsible for nearly half of clinical candidemia cases. The rising prevalence of azole-resistant <i>Candida</i> species represents a significant clinical challenge, underscoring the urgent need for alternative therapeutic strategies. Monoclonal antibody-based therapies have emerged as a promising and cost-effective approach to combating <i>Candida</i> infections. Agglutinin-like sequence protein 3 (Als3), a key cell surface protein of <i>C. albicans</i>, plays a pivotal role in adherence and biofilm formation, both of which are essential for its pathogenesis. In this study, recombinant Als3 protein was purified and utilized to immunize chickens, resulting in the production of Als3-specific immunoglobulin Y (IgY) antibodies. Two single-chain variable fragment (scFv) antibody libraries were subsequently constructed using phage display technology, yielding transformant counts of 5.3 × 10⁷ and 2.8 × 10⁷, respectively. Phage-based enzyme-linked immunosorbent assay (ELISA) revealed enhanced signals following bio-panning, enabling the identification and sequence validation of three scFv antibodies. These scFv antibodies exhibited strong binding activities to Als3, as confirmed through ELISA and western blot analyses. Binding affinities were determined to be ~ 10⁻⁸ M via serial titration ELISA and competitive ELISA. Additionally, the selected scFv antibodies specifically recognized endogenous Als3 protein in <i>C. albicans</i>, as demonstrated by western blot and cell-based ELISA assays. In conclusion, this study successfully generated and characterized high-affinity scFv antibodies targeting Als3, which exhibited exceptional specificity and binding activity. These findings highlight their potential as promising immunotherapeutic candidates for the treatment of <i>C. albicans</i> infections.</p><p>• <i>The Als3 protein of C. albicans is a critical biomarker and therapeutic target</i></p><p>• <i>Chicken-derived scFv antibodies against Als3 were developed via phage display</i></p><p>• <i>The scFv antibodies showed strong binding to endogenous Als3 in C. albicans</i></p>","PeriodicalId":8342,"journal":{"name":"Applied Microbiology and Biotechnology","volume":"109 1","pages":""},"PeriodicalIF":3.9,"publicationDate":"2025-04-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00253-025-13469-3.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143801224","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Characterization of β-glucosidase activity of a Lactiplantibacillus plantarum 6-phospho-β-glucosidase","authors":"Ravish Godse,&nbsp;Joyleen M. Fernandes,&nbsp;Ram Kulkarni","doi":"10.1007/s00253-025-13472-8","DOIUrl":"10.1007/s00253-025-13472-8","url":null,"abstract":"<p>β-Glucosidases are useful for hydrolysis of glycosidically-bound volatiles (GBV), thereby facilitating the release of aroma chemicals from the fruit matrices. In this study, 10 putative glycosyl hydrolases belonging to GH1 family from <i>Lactiplantibacillus plantarum</i> NCIM 2903 were cloned and recombinantly expressed. Interestingly, only one (LpBgl5) of the nine soluble proteins, previously characterized as a 6-phospho-β-glucosidase showed β-glucosidase activity which was further characterized. The enzyme had an optimum pH and temperature of 6 and 40°C, respectively, and was categorized as aryl-β-glucosidase due to its ability to hydrolyze different natural as well as synthetic glucosides except cellobiose. The enzyme exhibited functional activity across multiple substrates, with relative activity decreasing sequentially from β-xylosidase to β-glucosidase and finally β-mannosidase. The β-xylosidase and β-glucosidase activities of LpBgl5 were stimulated up to 300% and 700% in the presence of 4 M xylose and 4 M glucose, respectively. The enzyme could also hydrolyze GBV from mango. To our knowledge, this is the first recombinant β-glucosidase/β-xylosidase/β-mannosidase from <i>L. plantarum</i> to have potential for aroma enhancement in fruit products.</p><p>•<i> A recombinant β-glycosidase from Lactiplantibacillus plantarum was characterized.</i></p><p>•<i> The enzyme showed higher β-xylosidase activity than β-glucosidase activity.</i></p><p>•<i> The enzyme could also hydrolyze glycosidically bound volatiles from mango.</i></p>","PeriodicalId":8342,"journal":{"name":"Applied Microbiology and Biotechnology","volume":"109 1","pages":""},"PeriodicalIF":3.9,"publicationDate":"2025-04-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00253-025-13472-8.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143801222","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}