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<p>The study re-analyzed the draft genome of <i>Bacillus licheniformis</i> SMIA-2 and generated a reference-guided pseudo-scaffold. Cross-validated genome annotation identified five candidate loci associated with pectin degradation, including putative pectate lyases, polygalacturonase, and downstream uronate-catabolic genes. Submerged fermentation with passion fruit peel flour and corn steep liquor yielded crude enzymatic extracts, which were spray-dried at 110&#xa0;°C using maltodextrin and microcrystalline cellulose as stabilizers. The dried formulation retained pectinase activity for 180&#xa0;days at 5&#xa0;°C and showed additional cellulase, amylase, xylanase, and protease activities. Pectinase displayed optimal activity at pH 8.5 and 70&#xa0;°C, with stability between pH 8.0–8.5 and 65–70&#xa0;°C. Despite not using a reference strain and the absence of some omics analyses, with genomic and industrial claims presented as evidence of biotechnological potential rather than definitive functional validation of individual genes, these results support a sustainable, scalable, and alkaline-tolerant enzyme platform based on agro-industrial residues.</p>

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Scalable production of pectinases from Bacillus licheniformis SMIA-2 using agro-Industrial by-products with genomic insights

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2026年7月25日

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  • Erica Cruz,
  • Larissa Pacheco Ferreira,
  • Albert Remus Romero Rosana,
  • Samara Pinto Custódio Bernardo,
  • Meire Lelis Leal Martins,
  • João Paulo Fabi

摘要

The study re-analyzed the draft genome of Bacillus licheniformis SMIA-2 and generated a reference-guided pseudo-scaffold. Cross-validated genome annotation identified five candidate loci associated with pectin degradation, including putative pectate lyases, polygalacturonase, and downstream uronate-catabolic genes. Submerged fermentation with passion fruit peel flour and corn steep liquor yielded crude enzymatic extracts, which were spray-dried at 110 °C using maltodextrin and microcrystalline cellulose as stabilizers. The dried formulation retained pectinase activity for 180 days at 5 °C and showed additional cellulase, amylase, xylanase, and protease activities. Pectinase displayed optimal activity at pH 8.5 and 70 °C, with stability between pH 8.0–8.5 and 65–70 °C. Despite not using a reference strain and the absence of some omics analyses, with genomic and industrial claims presented as evidence of biotechnological potential rather than definitive functional validation of individual genes, these results support a sustainable, scalable, and alkaline-tolerant enzyme platform based on agro-industrial residues.