Biotechnology for biofuels and bioproducts最新文献

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Efficient preparation of fatty acid methyl esters using liquid lipase from thermotolerant fungus Rasamsonia emersonii via synergistic strategies. 利用液体脂肪酶协同制备耐高温真菌罗森氏菌脂肪酸甲酯。
IF 6
Biotechnology for biofuels and bioproducts Pub Date : 2026-08-01 DOI: 10.1186/s13068-026-02801-2
Jiang-Ke Yang, Ying Han, Lin-Jun Wei, De-Ming Rao, Lei Lei
{"title":"Efficient preparation of fatty acid methyl esters using liquid lipase from thermotolerant fungus Rasamsonia emersonii via synergistic strategies.","authors":"Jiang-Ke Yang, Ying Han, Lin-Jun Wei, De-Ming Rao, Lei Lei","doi":"10.1186/s13068-026-02801-2","DOIUrl":"https://doi.org/10.1186/s13068-026-02801-2","url":null,"abstract":"<p><p>Lipase-catalyzed biodiesel preparation in non-aqueous media has the advantages of reduced energy consumption, simplified recovery of fatty acid methyl esters (FAMEs), and minimized environment pollution, etc. To discover a novel thermophilic lipase, achieve its high-level expression, and develop it as an efficient liquid biocatalyst for FAMEs production via methanolysis of plant oils in non-aqueous media, a lipase gene from the thermophilic fungus Rasamsonia emersonii was cloned and efficiently expressed through synergistic strategies including computational codon optimization and increased gene dosage in the host genome. The resulting liquid lipase preparation was directly employed as a biocatalyst for FAMEs production. Under optimized reaction conditions, a conversion rate of approximately 95% was achieved. This study provides a feasible approach for the large-scale production of thermophilic lipase. The strategy of directly using of liquid lipase as a biocatalyst for FAMEs preparation substantially simplifies enzyme immobilization, regeneration, and product recovery processes, offering an efficient alternative for enzymatic FAMEs production.</p>","PeriodicalId":93909,"journal":{"name":"Biotechnology for biofuels and bioproducts","volume":"19 1","pages":""},"PeriodicalIF":6.0,"publicationDate":"2026-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149290636","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Improving silage fermentation of distilled grain waste-based spent mushroom substrate using indigenous lactic acid bacteria: metagenomic insights. 利用本地乳酸菌改进以谷物残渣为基础的废蘑菇底物的青贮发酵:宏基因组的见解。
IF 6
Biotechnology for biofuels and bioproducts Pub Date : 2026-07-31 DOI: 10.1186/s13068-026-02803-0
Xinlei Zhang, Diao Yin, Pengyu Liu, Jialun Song, Zemin Fang, Juanjuan Liu
{"title":"Improving silage fermentation of distilled grain waste-based spent mushroom substrate using indigenous lactic acid bacteria: metagenomic insights.","authors":"Xinlei Zhang, Diao Yin, Pengyu Liu, Jialun Song, Zemin Fang, Juanjuan Liu","doi":"10.1186/s13068-026-02803-0","DOIUrl":"https://doi.org/10.1186/s13068-026-02803-0","url":null,"abstract":"<p><strong>Background: </strong>Rising global mushroom production calls for recycling spent mushroom substrate (SMS). However, its high moisture content, susceptibility to spoilage, and low abundance of indigenous lactic acid bacteria (LAB) limit its use as silage. In this study, an effective silage inoculation strategy was developed to transform SMS derived from composted distilled grain waste (DGW) and colonized by Pleurotus ostreatus.</p><p><strong>Results: </strong>Three indigenous lactic acid bacteria, including Limosilactobacillus fermentum L2, Weissella paramesenteroides W1, and Pediococcus acidilactici P1, were isolated and selected for their rapid growth and acidification capacity, and applied individually or in combination at different stages of fungal colonization. Compared with a commercial inoculant, all indigenous lactic acid bacteria (LAB) treatments, especially a combination of L. fermentum L2 and P. acidilactici P1, significantly enhanced silage fermentation, as evidenced by lower pH (4.04-4.73), 31-fold and 1.87-fold increases in lactic acid and acetic acid production, respectively, improved crude protein retention, and preserved dry matter contents. KEGG enrichment analysis demonstrated that carbon metabolic flux was markedly redirected toward lactic acid fermentation, while pathways related to protein degradation and biosafety were significantly suppressed in LAB-treated SMS silage. Weighted metabolic analysis revealed that LAB contributed most to fermentative processes, thereby enriching Pediococcus, Weissella, and Lactobacillus, whereas the contributions of non-LAB and potentially harmful microorganisms were substantially reduced.</p><p><strong>Conclusion: </strong>These results indicate that indigenous LAB enhance the ensiling efficiency of SMS by driving functional reallocation and pathway-level dominance, thereby improving fermentation efficiency, stability, and nutritional quality, highlighting their potential for promoting SMS silage as a high-quality ruminant feed resource.</p>","PeriodicalId":93909,"journal":{"name":"Biotechnology for biofuels and bioproducts","volume":"19 1","pages":""},"PeriodicalIF":6.0,"publicationDate":"2026-07-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149290653","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Host-dependent activities of prenyltransferases in yeast and tobacco for cell-free cannflavin biosynthesis. 酵母和烟草无细胞生物合成中戊烯基转移酶的宿主依赖性活性。
IF 6
Biotechnology for biofuels and bioproducts Pub Date : 2026-07-29 DOI: 10.1186/s13068-026-02800-3
Sung-Eun Lee, Saet Buyl Lee, Hyun Ju Jung, Ji-Su Kim, Hyoseon Choi, Sangchul Choi, Beom-Gi Kim
{"title":"Host-dependent activities of prenyltransferases in yeast and tobacco for cell-free cannflavin biosynthesis.","authors":"Sung-Eun Lee, Saet Buyl Lee, Hyun Ju Jung, Ji-Su Kim, Hyoseon Choi, Sangchul Choi, Beom-Gi Kim","doi":"10.1186/s13068-026-02800-3","DOIUrl":"10.1186/s13068-026-02800-3","url":null,"abstract":"<p><p>Cannflavins are prenylated flavones found in Cannabis sativa that exhibit potent anti-inflammatory activities, but their low natural abundance limits pharmacological exploitation. Biotechnological strategies are therefore needed to support cannflavin production. Here, we evaluated yeast (Saccharomyces cerevisiae) and Nicotiana benthamiana as heterologous platforms for cell-free cannflavin biosynthesis. Six plant- and microbe-derived prenyltransferases (PTs) were expressed in both hosts and assessed for apparent cannflavin-forming activity using cell-free enzyme assays. In yeast-derived microsomal assays, CsPT3 from C. sativa produced cannflavin A (CFL-A) and cannflavin B (CFL-B), and removal of its predicted N-terminal transit peptide enhanced apparent CFL-A and CFL-B formation. By contrast, CsPT3 and cytCsPT3 did not produce detectable cannflavins in N. benthamiana-derived crude extract assays. Instead, the soluble microbial PT NphB supported CFL-A formation in N. benthamiana-derived enzyme preparations. We further established a crude extract-based one-pot assay in N. benthamiana and examined the effects of codon optimization of NphB, assay pH, and Agrobacterium inoculum density on apparent CFL-A formation. These results demonstrate that cannflavin-forming PT activity is highly dependent on host context and expression conditions. This comparative cell-free approach identifies suitable enzyme-host combinations for cannflavin biosynthesis and provides a practical platform for screening and improving prenylated flavonoid production.</p>","PeriodicalId":93909,"journal":{"name":"Biotechnology for biofuels and bioproducts","volume":"19 1","pages":""},"PeriodicalIF":6.0,"publicationDate":"2026-07-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13700126/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149278643","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}
引用次数: 0
G-protein signaling components differentially regulate the activity of multiple cellulase enzyme classes in Neurospora crassa. 粗神经孢子虫g蛋白信号组分对多种纤维素酶活性的调控存在差异。
IF 6
Biotechnology for biofuels and bioproducts Pub Date : 2026-06-05 DOI: 10.1186/s13068-026-02779-x
Yagna Oza, Katherine A Borkovich
{"title":"G-protein signaling components differentially regulate the activity of multiple cellulase enzyme classes in Neurospora crassa.","authors":"Yagna Oza, Katherine A Borkovich","doi":"10.1186/s13068-026-02779-x","DOIUrl":"10.1186/s13068-026-02779-x","url":null,"abstract":"<p><strong>Background: </strong>Heterotrimeric G-protein subunits, adenylyl cyclase, and Regulators of G-protein Signaling (RGS) proteins are required for the conversion of cellulose to glucose in the model filamentous fungus Neurospora crassa. Transcriptomics has revealed roles for several of these genes in the expression of specific cellulase enzyme classes, including endo-β-1,4-glucanases (endoglucanase), exo-β-1,4-glucanases (cellobiohydrolases), β-1,4-glucosidases (β-glucosidases), polysaccharide monooxygenases and cellobiose dehydrogenases.</p><p><strong>Results: </strong>In this study, we measured endoglucanase, cellobiohydrolase and β-glucosidase enzyme activities in secretomes from all G-protein subunit and RGS single mutants, Gα multiple mutants, and the adenylyl cyclase mutant Δcr-1 after transfer from glucose to cellulose medium. We observed that the Gα subunits gna-1 and gna-3 together are required for endoglucanase activity. cr-1 is essential, while gna-2 synergizes with gna-3 to regulate cellobiohydrolase activity. Multiple G-protein genes impacted β-glucosidase activity to some extent, but none were essential for activity. cAMP supplementation of the G protein mutants resulted in the greatest increase in endoglucanase and cellobiohydrolase activity, suggesting an important role for cAMP levels in the activity of these enzyme classes. Among the RGS mutants, the Δrgs-2 strain has greatly reduced activity for all three enzyme classes, like the strain expressing the constitutively active gna-3<sup>Q208L</sup> allele. In contrast, the Δrgs-1 mutant and the gna-1<sup>Q204L</sup> strain showed significantly higher endoglucanase activity as compared to wild type.</p><p><strong>Conclusions: </strong>Taken together, our results indicate that G protein signaling components differentially impact the activity of three major cellulase enzyme classes in N. crassa. Our findings will inform future strain engineering approaches to increase production of specific cellulase activities in culture supernatants of filamentous fungi.</p>","PeriodicalId":93909,"journal":{"name":"Biotechnology for biofuels and bioproducts","volume":" ","pages":""},"PeriodicalIF":6.0,"publicationDate":"2026-06-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1186/s13068-026-02779-x.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148177354","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}
引用次数: 0
Wastewater-to-biofuels and bioproducts through integrated anaerobic digestion, bioelectrochemical systems, and algal biorefineries: a systematic review of techno-economic and life-cycle evidence. 通过综合厌氧消化、生物电化学系统和藻类生物炼制废水转化为生物燃料和生物产品:技术经济和生命周期证据的系统回顾。
IF 6
Biotechnology for biofuels and bioproducts Pub Date : 2026-05-30 DOI: 10.1186/s13068-026-02778-y
Isnanik Juni Fitriyah, Sulistyo Saputro, Sajidan Sajidan
{"title":"Wastewater-to-biofuels and bioproducts through integrated anaerobic digestion, bioelectrochemical systems, and algal biorefineries: a systematic review of techno-economic and life-cycle evidence.","authors":"Isnanik Juni Fitriyah, Sulistyo Saputro, Sajidan Sajidan","doi":"10.1186/s13068-026-02778-y","DOIUrl":"10.1186/s13068-026-02778-y","url":null,"abstract":"<p><p>Wastewater management is increasingly shifting from conventional pollution control toward resource recovery systems that support clean water access, renewable energy production, and circular bioeconomy development. This systematic review synthesizes the literature on wastewater-to-biofuels and bioproducts through the integration of anaerobic digestion, bioelectrochemical systems, and algal biorefineries, with particular attention to techno-economic analysis and life-cycle assessment evidence. A systematic literature review was conducted on peer-reviewed studies published between 2005 and 2025, resulting in 90 selected articles that were analyzed through thematic and comparative synthesis. The findings show a clear transition from single-technology optimization toward integrated systems based on the water-energy-nutrient nexus. Anaerobic digestion remains the most mature pathway for organic load reduction and biogas production, while bioelectrochemical systems provide additional opportunities for electricity and hydrogen recovery. Algal biorefineries strengthen nutrient recovery and expand the production of biomass-based bioproducts. Comparative synthesis indicates that integrated systems can outperform single technologies when organic load, nutrient availability, process compatibility, operational scale, and product valorization are aligned. Integration may become counterproductive when additional capital cost, operational complexity, energy demand, or downstream processing burdens exceed the value of recovered resources. The TEA-LCA synthesis demonstrates that technology selection should be guided by trade-offs between economic feasibility and environmental performance rather than by technical efficiency alone. This review contributes a decision-oriented synthesis for selecting single or integrated wastewater-to-biofuels configurations that are technically feasible, economically viable, and environmentally sustainable.</p>","PeriodicalId":93909,"journal":{"name":"Biotechnology for biofuels and bioproducts","volume":" ","pages":""},"PeriodicalIF":6.0,"publicationDate":"2026-05-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13430706/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148102453","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}
引用次数: 0
Engineering of a LysG-derived arginine-specific biosensor for high-throughput screening of arginine overproducers in Corynebacterium glutamicum. 谷氨酸棒状杆菌精氨酸过量产生者高通量筛选赖氨酸衍生精氨酸特异性生物传感器的工程设计。
IF 6
Biotechnology for biofuels and bioproducts Pub Date : 2026-05-25 DOI: 10.1186/s13068-026-02776-0
Ningyun Cai, Ye Wang, Pengcheng Ren, Deming Rao, Tuo Shi, Ziyao Wang, Jie Shen, Wenjuan Zhou, Linlin Qi, Lixian Wang, Ning Chen, Jiuzhou Chen, Ping Zheng, Jibin Sun
{"title":"Engineering of a LysG-derived arginine-specific biosensor for high-throughput screening of arginine overproducers in Corynebacterium glutamicum.","authors":"Ningyun Cai, Ye Wang, Pengcheng Ren, Deming Rao, Tuo Shi, Ziyao Wang, Jie Shen, Wenjuan Zhou, Linlin Qi, Lixian Wang, Ning Chen, Jiuzhou Chen, Ping Zheng, Jibin Sun","doi":"10.1186/s13068-026-02776-0","DOIUrl":"10.1186/s13068-026-02776-0","url":null,"abstract":"<p><p>Arginine is a semi-essential amino acid and holds significant value in the pharmaceutical and nutraceutical industries. Corynebacterium glutamicum is a promising host for arginine production, yet its industrial titers remain limited. Biosensor-based high-throughput screening enables rapid isolation of overproducers. However, the native LysG-based biosensor in C. glutamicum lacks arginine specificity, limiting its efficiency for screening high arginine-producing strains. Here, we developed an arginine-specific biosensor pLysG<sup>F222I</sup> in C. glutamicum, by combining semi-rational design and directed evolution of LysG, an endogenous regulator responsive to basic amino acids. Structural and interaction analyses revealed that the F222I substitution in LysG retained high affinity for arginine while significantly decreasing its responsiveness to histidine and lysine. Subsequently, this arginine-specific biosensor was successfully applied to screen a library of N-acetylglutamate kinase (NAGK) mutants, identifying 18 novel NAGK mutants with enhanced arginine production compared with previously reported variants. The strain integrated with the optimal NAGK mutant was further subjected to mutagenesis and screening, yielding an engineered strain that achieved an arginine titer of 56.07 g/L in a 5-L bioreactor, a 42% increase relative to the original starting strain. Overall, this study provides a powerful tool for accelerating the metabolic engineering of C. glutamicum for high-level arginine production.</p>","PeriodicalId":93909,"journal":{"name":"Biotechnology for biofuels and bioproducts","volume":" ","pages":""},"PeriodicalIF":6.0,"publicationDate":"2026-05-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13450260/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148019184","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}
引用次数: 0
Reverse prediction of carbohydrate esterase polysaccharide targets. 糖类酯酶多糖靶点的反向预测。
IF 6
Biotechnology for biofuels and bioproducts Pub Date : 2026-05-19 DOI: 10.1186/s13068-026-02767-1
Kristian Barrett, Jesper Holck, Anne S Meyer
{"title":"Reverse prediction of carbohydrate esterase polysaccharide targets.","authors":"Kristian Barrett, Jesper Holck, Anne S Meyer","doi":"10.1186/s13068-026-02767-1","DOIUrl":"10.1186/s13068-026-02767-1","url":null,"abstract":"<p><strong>Background: </strong>Carbohydrate esterases (CEs) catalyze the selective removal of ester-linked substituents from complex polysaccharides, influencing biomass bioprocessing. Predicting CE substrate specificity remains challenging due to the functional diversity and limited experimental characterization of CEs. Classic full sequence-based alignment approaches often fail to capture functional nuances across distant homologs.</p><p><strong>Results: </strong>Here, we introduce a reverse prediction framework that leverages genomic context, specifically polysaccharide utilization loci (PULs), to infer natural polysaccharide targets of CE families. By integrating motif-based functional groups with large-scale co-occurrence analysis across Bacteroidota genomes, we identify substrate preferences at the clade level for 20 CE families. Subdivision of families into clades mitigated any polyspecificity observed when families were treated as a whole, highlighted unexplored regions within CE1, CE2, CE3, CE6, CE7, CE14, CE15, CE19, CE20, and partly within CE8 and CE12, and expanded functional coverage by up to 50% compared to characterized members alone.</p><p><strong>Conclusions: </strong>The approach and the data reveal substantial functional subdivision of the CE families, enabling prediction of specific targets including arabinoxylan, β-mannan, pectin sub-structures, and glycosaminoglycans. Reverse prediction thus offers a powerful tool for guiding enzyme discovery and designing tailored enzyme cocktails for biomass valorization.</p>","PeriodicalId":93909,"journal":{"name":"Biotechnology for biofuels and bioproducts","volume":" ","pages":""},"PeriodicalIF":6.0,"publicationDate":"2026-05-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13450560/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147977787","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}
引用次数: 0
Recent advances in microbial ε-poly-L-lysine fermentation and its diverse applications 微生物ε-聚赖氨酸发酵研究进展及其广泛应用
Biotechnology for biofuels and bioproducts Pub Date : 2022-06-16 DOI: 10.1186/s13068-022-02166-2
Shubo Li, Yunren Mao, Lifei Zhang, Miao Wang, Jinhao Meng, Xiaoling Liu, Yunxia Bai, Yuan Guo
{"title":"Recent advances in microbial ε-poly-L-lysine fermentation and its diverse applications","authors":"Shubo Li, Yunren Mao, Lifei Zhang, Miao Wang, Jinhao Meng, Xiaoling Liu, Yunxia Bai, Yuan Guo","doi":"10.1186/s13068-022-02166-2","DOIUrl":"https://doi.org/10.1186/s13068-022-02166-2","url":null,"abstract":"","PeriodicalId":93909,"journal":{"name":"Biotechnology for biofuels and bioproducts","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2022-06-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"43809026","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 7
Integrative transcriptome and proteome analyses of Trichoderma longibrachiatum LC and its cellulase hyper-producing mutants generated by heavy ion mutagenesis reveal the key genes involved in cellulolytic enzymes regulation 通过重离子诱变产生的长achiatum木霉LC及其纤维素酶高产突变体的综合转录组和蛋白质组分析,揭示了参与纤维素酶调控的关键基因
Biotechnology for biofuels and bioproducts Pub Date : 2022-06-03 DOI: 10.1186/s13068-022-02161-7
Miaoyin Dong, Shu-Yang Wang, Fuqiang Xu, G. Xiao, Jin Bai, Junkai Wang, Xisi Sun
{"title":"Integrative transcriptome and proteome analyses of Trichoderma longibrachiatum LC and its cellulase hyper-producing mutants generated by heavy ion mutagenesis reveal the key genes involved in cellulolytic enzymes regulation","authors":"Miaoyin Dong, Shu-Yang Wang, Fuqiang Xu, G. Xiao, Jin Bai, Junkai Wang, Xisi Sun","doi":"10.1186/s13068-022-02161-7","DOIUrl":"https://doi.org/10.1186/s13068-022-02161-7","url":null,"abstract":"","PeriodicalId":93909,"journal":{"name":"Biotechnology for biofuels and bioproducts","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2022-06-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"45027276","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 5
Genetic modifications of critical regulators provide new insights into regulation modes of raw-starch-digesting enzyme expression in Penicillium 关键调控因子的遗传修饰为青霉菌中原料淀粉消化酶表达的调控模式提供了新的见解
Biotechnology for biofuels and bioproducts Pub Date : 2022-05-31 DOI: 10.1186/s13068-022-02162-6
Shengfang Zhao, Boyu Xiang, Le Yang, Jie Chen, Cui Zhu, Yu Chen, Jun Cui, Shengbiao Hu, Yibo Hu
{"title":"Genetic modifications of critical regulators provide new insights into regulation modes of raw-starch-digesting enzyme expression in Penicillium","authors":"Shengfang Zhao, Boyu Xiang, Le Yang, Jie Chen, Cui Zhu, Yu Chen, Jun Cui, Shengbiao Hu, Yibo Hu","doi":"10.1186/s13068-022-02162-6","DOIUrl":"https://doi.org/10.1186/s13068-022-02162-6","url":null,"abstract":"","PeriodicalId":93909,"journal":{"name":"Biotechnology for biofuels and bioproducts","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2022-05-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"46175562","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 4
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