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Leveraging mutagenesis for enhanced enzymatic output: Detergent-stable α-amylase and lipase co-production by Bacillus subtilis on kitchen waste.

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Τίτλος: Leveraging mutagenesis for enhanced enzymatic output: Detergent-stable α-amylase and lipase co-production by Bacillus subtilis on kitchen waste.
Συγγραφείς: Aslam A; Department of Biochemistry, Bahauddin Zakariya University, Multan, 60800, Pakistan. Electronic address: aqsaaslam003@gmail.com., Raza JA; Department of Biochemistry, Bahauddin Zakariya University, Multan, 60800, Pakistan. Electronic address: Junaidahmad7773@gmail.com., Andaleeb H; Department of Biochemistry, Bahauddin Zakariya University, Multan, 60800, Pakistan. Electronic address: hina.andleeb@bzu.edu.pk., Ahmed S; Department of Biochemistry, Bahauddin Zakariya University, Multan, 60800, Pakistan. Electronic address: sibtain@bzu.edu.pk., Waseem SMY; Department of Biochemistry, Bahauddin Zakariya University, Multan, 60800, Pakistan. Electronic address: shmyahyawaseem@gmail.com.
Πηγή: International journal of biological macromolecules [Int J Biol Macromol] 2026 Sep; Vol. 374, pp. 153242. Date of Electronic Publication: 2026 Jun 27.
Τύπος έκδοσης: Journal Article
Γλώσσα: English
Στοιχεία περιοδικού: Publisher: Elsevier Country of Publication: Netherlands NLM ID: 7909578 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1879-0003 (Electronic) Linking ISSN: 01418130 NLM ISO Abbreviation: Int J Biol Macromol Subsets: MEDLINE
Imprint Name(s): Publication: Amsterdam : Elsevier
Original Publication: Guildford, Eng., IPC Science and Technology Press.
Ιατρικοί όροι (MeSH): Bacillus subtilis*/genetics , Bacillus subtilis*/enzymology , Bacillus subtilis*/metabolism , Lipase*/biosynthesis , Lipase*/genetics , Lipase*/chemistry , alpha-Amylases*/biosynthesis , alpha-Amylases*/genetics , alpha-Amylases*/chemistry , Detergents*/chemistry , Detergents*/pharmacology , Mutagenesis*, Hydrogen-Ion Concentration ; Enzyme Stability ; Fermentation ; Temperature ; Food Loss and Waste
Περίληψη: The sustainable bioproduction of industrial enzymes from low-cost substrates is a primary objective for circular bioeconomy strategies. This study reports the development of a strain of Bacillus subtilis via strain improvement that is capable of producing both α-amylase and lipase simultaneously from kitchen waste. The bacterium was subjected to EMS mutagenesis to improve its natural secretory potential, and a mutant named Bacillus subtilis 250 was selected based on its concurrent overproduction of both enzymes in a medium containing kitchen waste. Leftover fries and used vegetable oil were identified as major drivers for α-amylase and lipase, respectively. Fermentation conditions were sequentially optimized using One-Factor-At-a-Time (OFAT) and Response Surface Methodology (RSM), resulting in 1.53- and 1.45-fold increases in α-amylase and lipase activities, reaching final yields of 89.4 IU/ml and 74.1 IU/ml, respectively. The partially purified enzyme preparations exhibited apparent optimal activity at pH 7 and 50 °C for α-amylase, and pH 7 and 60 °C for lipase, with considerable activity under alkaline and high-temperature conditions. Both enzymes retain prominent residual activities when incubated with commercial detergents, surfactants, metal ions and additives showcasing their compatibility and industrial stability. This work establishes Bacillus subtilis as a versatile biocatalytic platform for the simultaneous valorization of food waste into industrially relevant amylase and lipase.
(Copyright © 2026. Published by Elsevier B.V.)
Competing Interests: Declaration of competing interest The authors declare that they have no competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
Contributed Indexing: Keywords: Alpha-amylase; Bacillus subtilis; Biodetergent; Food wastes; Kitchen wastes; Lipase; Mutagenesis; Process optimization; Strain improvement
Substance Nomenclature: EC 3.1.1.3 (Lipase)
EC 3.2.1.1 (alpha-Amylases)
0 (Detergents)
0 (Food Loss and Waste)
Entry Date(s): Date Created: 20260627 Date Completed: 20260821 Latest Revision: 20260821
Update Code: 20260821
DOI: 10.1016/j.ijbiomac.2026.153242
PMID: 42364749
Βάση Δεδομένων: MEDLINE
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  Data: Leveraging mutagenesis for enhanced enzymatic output: Detergent-stable α-amylase and lipase co-production by Bacillus subtilis on kitchen waste.
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  Data: <searchLink fieldCode="AU" term="%22Aslam+A%22">Aslam A</searchLink>; Department of Biochemistry, Bahauddin Zakariya University, Multan, 60800, Pakistan. Electronic address: aqsaaslam003@gmail.com.<br /><searchLink fieldCode="AU" term="%22Raza+JA%22">Raza JA</searchLink>; Department of Biochemistry, Bahauddin Zakariya University, Multan, 60800, Pakistan. Electronic address: Junaidahmad7773@gmail.com.<br /><searchLink fieldCode="AU" term="%22Andaleeb+H%22">Andaleeb H</searchLink>; Department of Biochemistry, Bahauddin Zakariya University, Multan, 60800, Pakistan. Electronic address: hina.andleeb@bzu.edu.pk.<br /><searchLink fieldCode="AU" term="%22Ahmed+S%22">Ahmed S</searchLink>; Department of Biochemistry, Bahauddin Zakariya University, Multan, 60800, Pakistan. Electronic address: sibtain@bzu.edu.pk.<br /><searchLink fieldCode="AU" term="%22Waseem+SMY%22">Waseem SMY</searchLink>; Department of Biochemistry, Bahauddin Zakariya University, Multan, 60800, Pakistan. Electronic address: shmyahyawaseem@gmail.com.
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  Data: <searchLink fieldCode="JN" term="%227909578%22">International journal of biological macromolecules</searchLink> [Int J Biol Macromol] 2026 Sep; Vol. 374, pp. 153242. <i>Date of Electronic Publication: </i>2026 Jun 27.
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  Data: <i>Publication</i>: Amsterdam : Elsevier<br /><i>Original Publication</i>: Guildford, Eng., IPC Science and Technology Press.
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  Data: <searchLink fieldCode="MM" term="%22Bacillus+subtilis%22">Bacillus subtilis*</searchLink>/<searchLink fieldCode="MM" term="%22Bacillus+subtilis+genetics%22">genetics</searchLink> <br /><searchLink fieldCode="MM" term="%22Bacillus+subtilis%22">Bacillus subtilis*</searchLink>/<searchLink fieldCode="MM" term="%22Bacillus+subtilis+enzymology%22">enzymology</searchLink> <br /><searchLink fieldCode="MM" term="%22Bacillus+subtilis%22">Bacillus subtilis*</searchLink>/<searchLink fieldCode="MM" term="%22Bacillus+subtilis+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Lipase%22">Lipase*</searchLink>/<searchLink fieldCode="MM" term="%22Lipase+biosynthesis%22">biosynthesis</searchLink> <br /><searchLink fieldCode="MM" term="%22Lipase%22">Lipase*</searchLink>/<searchLink fieldCode="MM" term="%22Lipase+genetics%22">genetics</searchLink> <br /><searchLink fieldCode="MM" term="%22Lipase%22">Lipase*</searchLink>/<searchLink fieldCode="MM" term="%22Lipase+chemistry%22">chemistry</searchLink> <br /><searchLink fieldCode="MM" term="%22alpha-Amylases%22">alpha-Amylases*</searchLink>/<searchLink fieldCode="MM" term="%22alpha-Amylases+biosynthesis%22">biosynthesis</searchLink> <br /><searchLink fieldCode="MM" term="%22alpha-Amylases%22">alpha-Amylases*</searchLink>/<searchLink fieldCode="MM" term="%22alpha-Amylases+genetics%22">genetics</searchLink> <br /><searchLink fieldCode="MM" term="%22alpha-Amylases%22">alpha-Amylases*</searchLink>/<searchLink fieldCode="MM" term="%22alpha-Amylases+chemistry%22">chemistry</searchLink> <br /><searchLink fieldCode="MM" term="%22Detergents%22">Detergents*</searchLink>/<searchLink fieldCode="MM" term="%22Detergents+chemistry%22">chemistry</searchLink> <br /><searchLink fieldCode="MM" term="%22Detergents%22">Detergents*</searchLink>/<searchLink fieldCode="MM" term="%22Detergents+pharmacology%22">pharmacology</searchLink> <br /><searchLink fieldCode="MM" term="%22Mutagenesis%22">Mutagenesis*</searchLink><br /><searchLink fieldCode="MH" term="%22Hydrogen-Ion+Concentration%22">Hydrogen-Ion Concentration</searchLink> ; <searchLink fieldCode="MH" term="%22Enzyme+Stability%22">Enzyme Stability</searchLink> ; <searchLink fieldCode="MH" term="%22Fermentation%22">Fermentation</searchLink> ; <searchLink fieldCode="MH" term="%22Temperature%22">Temperature</searchLink> ; <searchLink fieldCode="MH" term="%22Food+Loss+and+Waste%22">Food Loss and Waste</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: The sustainable bioproduction of industrial enzymes from low-cost substrates is a primary objective for circular bioeconomy strategies. This study reports the development of a strain of Bacillus subtilis via strain improvement that is capable of producing both α-amylase and lipase simultaneously from kitchen waste. The bacterium was subjected to EMS mutagenesis to improve its natural secretory potential, and a mutant named Bacillus subtilis 250 was selected based on its concurrent overproduction of both enzymes in a medium containing kitchen waste. Leftover fries and used vegetable oil were identified as major drivers for α-amylase and lipase, respectively. Fermentation conditions were sequentially optimized using One-Factor-At-a-Time (OFAT) and Response Surface Methodology (RSM), resulting in 1.53- and 1.45-fold increases in α-amylase and lipase activities, reaching final yields of 89.4 IU/ml and 74.1 IU/ml, respectively. The partially purified enzyme preparations exhibited apparent optimal activity at pH 7 and 50 °C for α-amylase, and pH 7 and 60 °C for lipase, with considerable activity under alkaline and high-temperature conditions. Both enzymes retain prominent residual activities when incubated with commercial detergents, surfactants, metal ions and additives showcasing their compatibility and industrial stability. This work establishes Bacillus subtilis as a versatile biocatalytic platform for the simultaneous valorization of food waste into industrially relevant amylase and lipase.<br /> (Copyright © 2026. Published by Elsevier B.V.)
– Name: Abstract
  Label: Competing Interests
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  Data: Declaration of competing interest The authors declare that they have no competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
– Name: SubjectMinor
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  Data: <i>Keywords: </i>Alpha-amylase; Bacillus subtilis; Biodetergent; Food wastes; Kitchen wastes; Lipase; Mutagenesis; Process optimization; Strain improvement
– Name: NumberCAS
  Label: Substance Nomenclature
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  Data: EC 3.1.1.3 (Lipase)<br />EC 3.2.1.1 (alpha-Amylases)<br />0 (Detergents)<br />0 (Food Loss and Waste)
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RecordInfo BibRecord:
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        Value: 10.1016/j.ijbiomac.2026.153242
    Languages:
      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        StartPage: 153242
    Subjects:
      – SubjectFull: Hydrogen-Ion Concentration
        Type: general
      – SubjectFull: Enzyme Stability
        Type: general
      – SubjectFull: Fermentation
        Type: general
      – SubjectFull: Temperature
        Type: general
      – SubjectFull: Food Loss and Waste
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      – SubjectFull: Bacillus subtilis genetics
        Type: general
      – SubjectFull: Bacillus subtilis enzymology
        Type: general
      – SubjectFull: Bacillus subtilis metabolism
        Type: general
      – SubjectFull: Lipase biosynthesis
        Type: general
      – SubjectFull: Lipase genetics
        Type: general
      – SubjectFull: Lipase chemistry
        Type: general
      – SubjectFull: alpha-Amylases biosynthesis
        Type: general
      – SubjectFull: alpha-Amylases genetics
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      – SubjectFull: alpha-Amylases chemistry
        Type: general
      – SubjectFull: Detergents chemistry
        Type: general
      – SubjectFull: Detergents pharmacology
        Type: general
      – SubjectFull: Mutagenesis
        Type: general
    Titles:
      – TitleFull: Leveraging mutagenesis for enhanced enzymatic output: Detergent-stable α-amylase and lipase co-production by Bacillus subtilis on kitchen waste.
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              Text: 2026 Sep
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              Y: 2026
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