First evidence of keratinolytic activity in Simplicillium aogashimaense isolated from wool-pellet-amended soil.

IF 5.8 2区 生物学 Q1 BIOTECHNOLOGY & APPLIED MICROBIOLOGY
Clémentine Isembart, Zoé Bruchon, Jean-Michel Yao, Boris Zimmermann, Cristian Bolaño Losada, Achim Kohler, Paige Heavyside, Volha Shapaval
{"title":"First evidence of keratinolytic activity in Simplicillium aogashimaense isolated from wool-pellet-amended soil.","authors":"Clémentine Isembart, Zoé Bruchon, Jean-Michel Yao, Boris Zimmermann, Cristian Bolaño Losada, Achim Kohler, Paige Heavyside, Volha Shapaval","doi":"10.1186/s12934-026-03066-y","DOIUrl":null,"url":null,"abstract":"<p><strong>Background: </strong>Keratin-rich waste such as wool and feather wastes are generated in large quantities worldwide and remain difficult to valorize due to the structural resilience of keratin, that is reinforced by disulfide bonds. Microbial degradation offers a sustainable approach for converting these wastes into value-added products. In this study, keratin-degrading fungi were isolated from garden soils amended with wool pellets used as organic fertilizer. Three fungal strains showing keratinolytic activity were selected based on halo formation on keratin-containing agar media. Among them, Simplicillium aogashimaense was chosen for detailed characterization due to its non-pathogenic status, limited representation in the literature, and the absence of previously reported proteolytic or keratinolytic activity.</p><p><strong>Results: </strong>Feather meal degradation by S. aogashimaense was investigated during 12 days of submerged cultivation. The strain demonstrated strong keratinolytic potential, achieving up to 80% feather meal mass reduction. Biochemical analysis of the resulting hydrolysates, including protease activity, elemental composition, amino acid profiles, ammonium and sulfur concentrations, pH dynamics, and overall biochemical profile, revealed a multiphasic degradation pattern. The initial phase (days 1-3) was characterized by rapid feather breakdown, elevated protease activity, ammonium release, and preferential liberation of surface-accessible amino acids, indicating efficient enzymatic attack on exposed keratin domains. The intermediate phase (days 4-6) during which general protease activity declines along with the fungal biomass. This period is likely to correspond to a shift from feather degradation to assimilation and intracellular metabolism. During the final phase (days 7-12), measured parameters stabilized, consistent with maximal substrate degradation and subsequent assimilation of soluble hydrolysis products by the fungus.</p><p><strong>Conclusions: </strong>This study provides the first evidence that S. aogashimaense exhibits keratin-degrading capability, identifying it as a previously unrecognized keratinolytic fungal species. These findings broaden current understanding of fungal keratin degradation and highlight the potential of S. aogashimaense for sustainable bioconversion of feather waste and other keratin-rich residues. Further optimization and mechanistic investigation of its enzymatic system may support future biotechnological applications in waste valorization.</p>","PeriodicalId":18582,"journal":{"name":"Microbial Cell Factories","volume":" ","pages":""},"PeriodicalIF":5.8000,"publicationDate":"2026-07-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13587383/pdf/","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Microbial Cell Factories","FirstCategoryId":"5","ListUrlMain":"https://doi.org/10.1186/s12934-026-03066-y","RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"BIOTECHNOLOGY & APPLIED MICROBIOLOGY","Score":null,"Total":0}
引用次数: 0

Abstract

Background: Keratin-rich waste such as wool and feather wastes are generated in large quantities worldwide and remain difficult to valorize due to the structural resilience of keratin, that is reinforced by disulfide bonds. Microbial degradation offers a sustainable approach for converting these wastes into value-added products. In this study, keratin-degrading fungi were isolated from garden soils amended with wool pellets used as organic fertilizer. Three fungal strains showing keratinolytic activity were selected based on halo formation on keratin-containing agar media. Among them, Simplicillium aogashimaense was chosen for detailed characterization due to its non-pathogenic status, limited representation in the literature, and the absence of previously reported proteolytic or keratinolytic activity.

Results: Feather meal degradation by S. aogashimaense was investigated during 12 days of submerged cultivation. The strain demonstrated strong keratinolytic potential, achieving up to 80% feather meal mass reduction. Biochemical analysis of the resulting hydrolysates, including protease activity, elemental composition, amino acid profiles, ammonium and sulfur concentrations, pH dynamics, and overall biochemical profile, revealed a multiphasic degradation pattern. The initial phase (days 1-3) was characterized by rapid feather breakdown, elevated protease activity, ammonium release, and preferential liberation of surface-accessible amino acids, indicating efficient enzymatic attack on exposed keratin domains. The intermediate phase (days 4-6) during which general protease activity declines along with the fungal biomass. This period is likely to correspond to a shift from feather degradation to assimilation and intracellular metabolism. During the final phase (days 7-12), measured parameters stabilized, consistent with maximal substrate degradation and subsequent assimilation of soluble hydrolysis products by the fungus.

Conclusions: This study provides the first evidence that S. aogashimaense exhibits keratin-degrading capability, identifying it as a previously unrecognized keratinolytic fungal species. These findings broaden current understanding of fungal keratin degradation and highlight the potential of S. aogashimaense for sustainable bioconversion of feather waste and other keratin-rich residues. Further optimization and mechanistic investigation of its enzymatic system may support future biotechnological applications in waste valorization.

从羊毛颗粒改良土壤中分离的奥格什马氏Simplicillium角朊酶活性的首个证据。
背景:富含角蛋白的废物,如羊毛和羽毛废物,在世界范围内大量产生,由于角蛋白的结构弹性,这是由二硫键加强难以估价。微生物降解为将这些废物转化为增值产品提供了可持续的途径。本研究从有机肥羊毛颗粒改良的园林土壤中分离出角蛋白降解真菌。通过在含角蛋白的琼脂培养基上形成光晕,筛选出3株具有角蛋白溶解活性的真菌菌株。其中,由于aoogashimaense的非致病性,在文献中的代表性有限,以及先前没有报道的蛋白水解或角化活性,我们选择了Simplicillium aogashimaense进行了详细的表征。结果:在12天的潜水培养过程中,研究了aoogashimaense对羽毛粉的降解情况。该菌株显示出很强的角蛋白溶解潜力,达到高达80%的羽毛粉质量减少。对水解产物的生化分析,包括蛋白酶活性、元素组成、氨基酸谱、铵和硫浓度、pH动态和总体生化谱,揭示了多相降解模式。初始阶段(1-3天)的特点是羽毛快速分解,蛋白酶活性升高,铵释放,表面可接近的氨基酸优先释放,表明酶对暴露的角蛋白结构域的有效攻击。中间阶段(4-6天),一般蛋白酶活性随真菌生物量下降。这一时期可能对应于从羽毛降解到同化和细胞内代谢的转变。在最后阶段(第7-12天),测量参数稳定,与最大底物降解和随后真菌对可溶性水解产物的同化一致。结论:本研究首次提供了S. aogashimaense具有角蛋白降解能力的证据,确定了它是一种以前未被发现的角蛋白降解真菌。这些发现拓宽了目前对真菌角蛋白降解的认识,并突出了S. aogashimaense在羽毛废物和其他富含角蛋白残留物的可持续生物转化方面的潜力。对其酶促体系的进一步优化和机理研究,可为未来生物技术在废物增值中的应用提供支持。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
Microbial Cell Factories
Microbial Cell Factories 工程技术-生物工程与应用微生物
CiteScore
9.30
自引率
4.70%
发文量
235
审稿时长
2.3 months
期刊介绍: Microbial Cell Factories is an open access peer-reviewed journal that covers any topic related to the development, use and investigation of microbial cells as producers of recombinant proteins and natural products, or as catalyzers of biological transformations of industrial interest. Microbial Cell Factories is the world leading, primary research journal fully focusing on Applied Microbiology. The journal is divided into the following editorial sections: -Metabolic engineering -Synthetic biology -Whole-cell biocatalysis -Microbial regulations -Recombinant protein production/bioprocessing -Production of natural compounds -Systems biology of cell factories -Microbial production processes -Cell-free systems
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:604180095
Book学术官方微信
小红书