Evidence map›Paper›PMID 42902070›Full record

ArticleAntonie van Leeuwenhoek2026

Chitinase biosynthesis and antifungal chitin bioconversion by Streptomyces mutabilis Ssg through statistical optimisation: an agro-industrial waste valorisation approach.

Amira Missouri, Amina Khaldi, Mohammed Lamine Benine, Djillali Bassou, Salima Kebbouche Gana, Assia Bensedjad, Mohammed Laraki, Aicha Megherbi, Ali Boumegoura, Giovanni Emiliani and 2 more

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Article in Antonie van Leeuwenhoek, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

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4 · The record

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PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors.

Amira MissouriSynthesis of Environmental Information Laboratory (LSIE), Djillali Liabes University, Sidi Bel Abbes, Algeria.
Amina KhaldiSynthesis of Environmental Information Laboratory (LSIE), Djillali Liabes University, Sidi Bel Abbes, Algeria.
Mohammed Lamine BenineSynthesis of Environmental Information Laboratory (LSIE), Djillali Liabes University, Sidi Bel Abbes, Algeria.
Djillali BassouLaboratory of Physical and Macromolecular Organic Chemistry, Djilali Liabes University, BP89, 22000, Sidi-Bel-Abbes, Algeria.
Salima Kebbouche GanaLaboratoire de Recherche de Bioinformatique, Microbiologie Appliquée et Biomolécules (BMAB), Université de Boumerdes, Boumerdes, Algérie. s.ganakebbouche@univ-boumerdes.dz.ORCID https://orcid.org/0000-0002-6021-7522
Assia BensedjadLaboratory of Process Engineering, Materials and Environment, Faculty of Technology, University of Djillali Liabes, PO Box 89, 22000, Sidi Bel Abbes, Algeria.
Mohammed LarakiSynthesis of Environmental Information Laboratory (LSIE), Djillali Liabes University, Sidi Bel Abbes, Algeria.
Aicha MegherbiLaboratory of the Ecodevelopment Spaces, Natural Sciences and Life Faculty, Djillali Liabes University, 22000, Sidi Bel Abbes, Algeria.
Ali BoumegouraNational Center for Biotechnology Research (CRBT), Laboratory of Molecular Biology, 25016, Constantine, Algeria.
Giovanni EmilianiInstitute for Sustainable Plant Protection, National Research Council of (CNR-IPSP), Via Madonna del Piano 10, 50019, Sesto Fiorentino, Florence, Italy.
Meriem BoucifSynthesis of Environmental Information Laboratory (LSIE), Djillali Liabes University, Sidi Bel Abbes, Algeria.
Fatima Zohra KaissarSynthesis of Environmental Information Laboratory (LSIE), Djillali Liabes University, Sidi Bel Abbes, Algeria.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chitin valorisation through enzymatic bioconversion offers a sustainable route for converting biowastes into value-added bioactive products. In this study, the chitinolytic strain Ssg, showing close phylogenetic affinity with Streptomyces mutabilis, was evaluated for chitinase production in a waste-integrated submerged fermentation system based on crustacean-derived colloidal chitin and supplemented with date seed and orange-peel powders as low-cost co-substrates. The isolate showed a high chitinolytic index of 17.20 ± 0.70. Plackett-Burman screening identified substrate composition and incubation time as key determinants of chitinase production, while Box-Behnken optimisation revealed significant interaction effects and identified the best-performing combination. At 10 g/L date seed powder, 4.08 g/L orange peel powder, and 72 h of incubation, chitinase activity reached 3196 ± 1.73 U/mL, closely matching the predicted value of 3198.01 U/mL. Optimisation increased enzyme production 7.6-fold and reduced fermentation time from 6 days to 72 h. Specific activity also increased from 4870 ± 170 to 13,620 ± 105 U/mg, reflecting stronger chitinolytic performance of the optimised preparation. Both the Optimised Cell-Free Supernatant and the crude chitin hydrolysate exhibited comparable antifungal activity against Aspergillus brasiliensis and Fusarium sp., with a slight advantage for the hydrolysate. The strongest response was observed against Fusarium sp. with the crude chitin hydrolysate, showing an inhibition zone of 24.00 ± 1.00 mm and mycelial growth inhibition of 38.75%. Microscopic observations revealed hyphal deformation and structural disorganisation. Overall, this study establishes a waste-integrated strategy for high-level chitinase production and supports the potential of the Ssg system for chitin bioconversion and biocontrol-oriented applications.

Indexed as

Antifungal AgentsChitinChitinasesIndustrial WasteStreptomycesFermentationAntifungal AgentsChitinChitinasesIndustrial WasteAntifungal activityChitinase productionChitin bioconversionResponse surface methodologyStreptomyces mutabilisWaste valorisation

Identifiers

PMID42902070

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.