دورية أكاديمية
Two-step functional screen on multiple proteinaceous substrates reveals temperature-robust proteases with a broad-substrate range.
| العنوان: | Two-step functional screen on multiple proteinaceous substrates reveals temperature-robust proteases with a broad-substrate range. |
|---|---|
| المؤلفون: | García-Moyano A; NORCE Norwegian Research Centre, Thormøhlens gate 55, 5006, Bergen, Norway., Diaz Y; NORCE Norwegian Research Centre, Thormøhlens gate 55, 5006, Bergen, Norway., Navarro J; Institute of Catalysis, Consejo Superior de Investigaciones Científicas, 28049, Madrid, Spain., Almendral D; Institute of Catalysis, Consejo Superior de Investigaciones Científicas, 28049, Madrid, Spain., Puntervoll P; NORCE Norwegian Research Centre, Thormøhlens gate 55, 5006, Bergen, Norway., Ferrer M; Institute of Catalysis, Consejo Superior de Investigaciones Científicas, 28049, Madrid, Spain., Bjerga GEK; NORCE Norwegian Research Centre, Thormøhlens gate 55, 5006, Bergen, Norway. grbj@norceresearch.no. |
| المصدر: | Applied microbiology and biotechnology [Appl Microbiol Biotechnol] 2021 Apr; Vol. 105 (8), pp. 3195-3209. Date of Electronic Publication: 2021 Mar 26. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: Springer International Country of Publication: Germany NLM ID: 8406612 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1432-0614 (Electronic) Linking ISSN: 01757598 NLM ISO Abbreviation: Appl Microbiol Biotechnol Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Berlin ; New York : Springer International, c1984- |
| مواضيع طبية MeSH: | Metagenome* , Peptide Hydrolases*/genetics, Animals ; Bacteria/genetics ; Endopeptidases ; Temperature |
| مستخلص: | To support the bio-based industry in development of environment-friendly processes and products, an optimal toolbox of biocatalysts is key. Although functional screen of (meta)genomic libraries may potentially contribute to identifying new enzymes, the discovery of new enzymes meeting industry compliance demands is still challenging. This is particularly noticeable in the case of proteases, for which the reports of metagenome-derived proteases with industrial applicability are surprisingly limited. Indeed, proteolytic clones have been typically assessed by its sole activity on casein or skim milk and limited to mild screening conditions. Here, we demonstrate the use of six industry-relevant animal and plant by-products, namely bone, feather, blood meals, gelatin, gluten, and zein, as complementary substrates in functional screens and show the utility of temperature as a screening parameter to potentially discover new broad-substrate range and robust proteases for the biorefinery industry. By targeting 340,000 clones from two libraries of pooled isolates of mesophilic and thermophilic marine bacteria and two libraries of microbial communities inhabiting marine environments, we identified proteases in four of eleven selected clones that showed activity against all substrates herein tested after prolonged incubation at 55 °C. Following sequencing, in silico analysis and recombinant expression in Escherichia coli, one functional protease, 58% identical at sequence level to previously reported homologs, was found to readily hydrolyze highly insoluble zein at temperatures up to 50 °C and pH 9-11. It is derived from a bacterial group whose ability to degrade zein was unknown. This study reports a two-step screen resulting in identification of a new marine metagenome-derived protease with zein-hydrolytic properties at common biomass processing temperatures that could be useful for the modern biorefinery industry. KEY POINTS: • A two-step multi-substrate strategy for discovery of robust proteases. • Feasible approach for shortening enzyme optimization to industrial demands. • A new temperature-tolerant protease efficiently hydrolyzes insoluble zein. |
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| معلومات مُعتمدة: | 634486 H2020 European Research Council; 604814 EU ERANET Marine Biotechnology; BIO2017-85522-R Ministerio de Ciencia, Innovación y Universidades; 281406 Norges Forskningsråd |
| فهرسة مساهمة: | Keywords: Agar screen; Functional metagenomics; Protease M10/M12; Zein |
| المشرفين على المادة: | EC 3.4.- (Endopeptidases) EC 3.4.- (Peptide Hydrolases) |
| تواريخ الأحداث: | Date Created: 20210326 Date Completed: 20210514 Latest Revision: 20210823 |
| رمز التحديث: | 20231215 |
| مُعرف محوري في PubMed: | PMC8053189 |
| DOI: | 10.1007/s00253-021-11235-9 |
| PMID: | 33770243 |
| قاعدة البيانات: | MEDLINE |
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Full Text Finder | تدمد: | 1432-0614 |
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| DOI: | 10.1007/s00253-021-11235-9 |