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Recombinant thermotolerant alkaline lipase from Lysinibacillus fusiformis for detergent and hard (Ras) cheese applications: cloning, expression, molecular docking, and characterization.

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Title: Recombinant thermotolerant alkaline lipase from Lysinibacillus fusiformis for detergent and hard (Ras) cheese applications: cloning, expression, molecular docking, and characterization.
Authors: El-Sayed GM; Microbial Genetic Department, National Research Centre, Dokki, Giza, 12622, Egypt., Wehaidy HR; Chemistry of Natural and Microbial Products Department, National Research Centre, Dokki, Giza, 12622, Egypt. halolty2009@yahoo.com., Kholif AMM; Dairy Sciences Department, National Research Centre, Dokki, Giza, 12622, Egypt., Salama WH; Molecular Biology Department, National Research Centre, Dokki, Giza, 12622, Egypt., Salim RG; Microbial Genetic Department, National Research Centre, Dokki, Giza, 12622, Egypt.
Source: Microbial cell factories [Microb Cell Fact] 2026 Aug 29; Vol. 25 (1). Date of Electronic Publication: 2026 Aug 29.
Publication Type: Journal Article
Language: English
Journal Info: Publisher: BioMed Central Country of Publication: England NLM ID: 101139812 Publication Model: Electronic Cited Medium: Internet ISSN: 1475-2859 (Electronic) Linking ISSN: 14752859 NLM ISO Abbreviation: Microb Cell Fact Subsets: MEDLINE
Imprint Name(s): Original Publication: London : BioMed Central, [2002-
MeSH Terms: Lipase*/genetics , Lipase*/metabolism , Lipase*/chemistry , Detergents*/chemistry , Detergents*/metabolism , Bacillaceae*/enzymology , Bacillaceae*/genetics , Bacterial Proteins*/genetics , Bacterial Proteins*/metabolism , Bacterial Proteins*/chemistry , Cheese*, Recombinant Proteins/metabolism ; Recombinant Proteins/genetics ; Recombinant Proteins/chemistry ; Cloning, Molecular ; Molecular Docking Simulation ; Enzyme Stability ; Hydrogen-Ion Concentration ; Substrate Specificity
Abstract: Background: Thermostable and alkaline lipases are of significant interest for industrial applications, particularly in detergents and food processing. This study aimed to isolate, clone, and express lipase-encoding genes from a potent bacterial source to produce a thermo-tolerant alkaline lipase with enhanced catalytic efficiency and practical applicability.
Results: Among several bacterial isolates, the most potent lipase producer was identified as Lysinibacillus fusiformis, and its 16 S rRNA sequence was deposited in GenBank (PP757498). Three lipase-encoding genes (est, est2, and lipA) were successfully isolated, cloned, and heterologously expressed in Escherichia coli BL21 (DE3). Their sequences were submitted to GenBank under accession numbers PX136937.1, PX136938.1, and PX136936.1, respectively. The recombinant lipase encoded by lipA (rLipase) exhibited the highest activity (150 U/mL) compared with the native enzyme (56.2 U/mL). Molecular docking analysis demonstrated strong binding affinity of rLipase toward major fatty acid derivatives in olive oil, with the highest affinity for linoleic acid (- 8.0 kcal/mol), followed by oleic acid (- 7.8 kcal/mol) and palmitic acid (- 7.3 kcal/mol). These interactions were stabilized by hydrophobic interactions and hydrogen bonding, with key contributions from critical amino acid residues, particularly VAL250. The partially purified recombinant lipase (rLipase) exhibited a maximum activity of 320 U/mL at 80 °C and pH 9, demonstrating remarkable thermostability and alkaline tolerance. Functional evaluation showed that rLipase improved the detergent efficiency for oil stain-removal from cotton fabrics. In addition, supplementation with 0.4% rLipase accelerated Ras cheese ripening by shortening the maturation period from 120 to 90 days with maintaining the desired ripening process.
Conclusions: The recombinant lipase from Lysinibacillus fusiformis demonstrated high thermal stability, alkaline tolerance, and strong catalytic efficiency. Its effectiveness in detergent formulations and cheese ripening highlights its potential as a versatile industrial biocatalyst for lipid bioconversion and related applications.
(© 2026. The Author(s).)
Competing Interests: Declarations. Ethics approval and consent to participate: Not applicable. Competing interests: The authors declare no competing interests.
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Contributed Indexing: Keywords: Lycinibacillus fusiformis; Enzyme characterization; Gene cloning; Heterologous expression; Ras cheese ripening; Recombinant lipase A
Substance Nomenclature: EC 3.1.1.3 (Lipase)
0 (Detergents)
0 (Recombinant Proteins)
0 (Bacterial Proteins)
Entry Date(s): Date Created: 20260829 Date Completed: 20260829 Latest Revision: 20260901
Update Code: 20260901
PubMed Central ID: PMC13526305
DOI: 10.1186/s12934-026-03084-w
PMID: 42668381
Database: MEDLINE
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Items – Name: Title
  Label: Title
  Group: Ti
  Data: Recombinant thermotolerant alkaline lipase from Lysinibacillus fusiformis for detergent and hard (Ras) cheese applications: cloning, expression, molecular docking, and characterization.
– Name: Author
  Label: Authors
  Group: Au
  Data: <searchLink fieldCode="AU" term="%22El-Sayed+GM%22">El-Sayed GM</searchLink>; Microbial Genetic Department, National Research Centre, Dokki, Giza, 12622, Egypt.<br /><searchLink fieldCode="AU" term="%22Wehaidy+HR%22">Wehaidy HR</searchLink>; Chemistry of Natural and Microbial Products Department, National Research Centre, Dokki, Giza, 12622, Egypt. halolty2009@yahoo.com.<br /><searchLink fieldCode="AU" term="%22Kholif+AMM%22">Kholif AMM</searchLink>; Dairy Sciences Department, National Research Centre, Dokki, Giza, 12622, Egypt.<br /><searchLink fieldCode="AU" term="%22Salama+WH%22">Salama WH</searchLink>; Molecular Biology Department, National Research Centre, Dokki, Giza, 12622, Egypt.<br /><searchLink fieldCode="AU" term="%22Salim+RG%22">Salim RG</searchLink>; Microbial Genetic Department, National Research Centre, Dokki, Giza, 12622, Egypt.
– Name: TitleSource
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  Data: <searchLink fieldCode="JN" term="%22101139812%22">Microbial cell factories</searchLink> [Microb Cell Fact] 2026 Aug 29; Vol. 25 (1). <i>Date of Electronic Publication: </i>2026 Aug 29.
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  Data: Journal Article
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  Data: English
– Name: TitleSource
  Label: Journal Info
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  Data: <i>Publisher: </i><searchLink fieldCode="PB" term="%22BioMed+Central%22">BioMed Central </searchLink><i>Country of Publication: </i>England <i>NLM ID: </i>101139812 <i>Publication Model: </i>Electronic <i>Cited Medium: </i>Internet <i>ISSN: </i>1475-2859 (Electronic) <i>Linking ISSN: </i><searchLink fieldCode="IS" term="%2214752859%22">14752859 </searchLink><i>NLM ISO Abbreviation: </i>Microb Cell Fact <i>Subsets: </i>MEDLINE
– Name: PublisherInfo
  Label: Imprint Name(s)
  Group: PubInfo
  Data: <i>Original Publication</i>: London : BioMed Central, [2002-
– Name: SubjectMESH
  Label: MeSH Terms
  Group: Su
  Data: <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+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Lipase%22">Lipase*</searchLink>/<searchLink fieldCode="MM" term="%22Lipase+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+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Bacillaceae%22">Bacillaceae*</searchLink>/<searchLink fieldCode="MM" term="%22Bacillaceae+enzymology%22">enzymology</searchLink> <br /><searchLink fieldCode="MM" term="%22Bacillaceae%22">Bacillaceae*</searchLink>/<searchLink fieldCode="MM" term="%22Bacillaceae+genetics%22">genetics</searchLink> <br /><searchLink fieldCode="MM" term="%22Bacterial+Proteins%22">Bacterial Proteins*</searchLink>/<searchLink fieldCode="MM" term="%22Bacterial+Proteins+genetics%22">genetics</searchLink> <br /><searchLink fieldCode="MM" term="%22Bacterial+Proteins%22">Bacterial Proteins*</searchLink>/<searchLink fieldCode="MM" term="%22Bacterial+Proteins+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Bacterial+Proteins%22">Bacterial Proteins*</searchLink>/<searchLink fieldCode="MM" term="%22Bacterial+Proteins+chemistry%22">chemistry</searchLink> <br /><searchLink fieldCode="MM" term="%22Cheese%22">Cheese*</searchLink><br /><searchLink fieldCode="MH" term="%22Recombinant+Proteins%22">Recombinant Proteins</searchLink>/<searchLink fieldCode="MH" term="%22Recombinant+Proteins+metabolism%22">metabolism</searchLink> ; <searchLink fieldCode="MH" term="%22Recombinant+Proteins%22">Recombinant Proteins</searchLink>/<searchLink fieldCode="MH" term="%22Recombinant+Proteins+genetics%22">genetics</searchLink> ; <searchLink fieldCode="MH" term="%22Recombinant+Proteins%22">Recombinant Proteins</searchLink>/<searchLink fieldCode="MH" term="%22Recombinant+Proteins+chemistry%22">chemistry</searchLink> ; <searchLink fieldCode="MH" term="%22Cloning%2C+Molecular%22">Cloning, Molecular</searchLink> ; <searchLink fieldCode="MH" term="%22Molecular+Docking+Simulation%22">Molecular Docking Simulation</searchLink> ; <searchLink fieldCode="MH" term="%22Enzyme+Stability%22">Enzyme Stability</searchLink> ; <searchLink fieldCode="MH" term="%22Hydrogen-Ion+Concentration%22">Hydrogen-Ion Concentration</searchLink> ; <searchLink fieldCode="MH" term="%22Substrate+Specificity%22">Substrate Specificity</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Background: Thermostable and alkaline lipases are of significant interest for industrial applications, particularly in detergents and food processing. This study aimed to isolate, clone, and express lipase-encoding genes from a potent bacterial source to produce a thermo-tolerant alkaline lipase with enhanced catalytic efficiency and practical applicability.<br />Results: Among several bacterial isolates, the most potent lipase producer was identified as Lysinibacillus fusiformis, and its 16 S rRNA sequence was deposited in GenBank (PP757498). Three lipase-encoding genes (est, est2, and lipA) were successfully isolated, cloned, and heterologously expressed in Escherichia coli BL21 (DE3). Their sequences were submitted to GenBank under accession numbers PX136937.1, PX136938.1, and PX136936.1, respectively. The recombinant lipase encoded by lipA (rLipase) exhibited the highest activity (150 U/mL) compared with the native enzyme (56.2 U/mL). Molecular docking analysis demonstrated strong binding affinity of rLipase toward major fatty acid derivatives in olive oil, with the highest affinity for linoleic acid (- 8.0 kcal/mol), followed by oleic acid (- 7.8 kcal/mol) and palmitic acid (- 7.3 kcal/mol). These interactions were stabilized by hydrophobic interactions and hydrogen bonding, with key contributions from critical amino acid residues, particularly VAL250. The partially purified recombinant lipase (rLipase) exhibited a maximum activity of 320 U/mL at 80 °C and pH 9, demonstrating remarkable thermostability and alkaline tolerance. Functional evaluation showed that rLipase improved the detergent efficiency for oil stain-removal from cotton fabrics. In addition, supplementation with 0.4% rLipase accelerated Ras cheese ripening by shortening the maturation period from 120 to 90 days with maintaining the desired ripening process.<br />Conclusions: The recombinant lipase from Lysinibacillus fusiformis demonstrated high thermal stability, alkaline tolerance, and strong catalytic efficiency. Its effectiveness in detergent formulations and cheese ripening highlights its potential as a versatile industrial biocatalyst for lipid bioconversion and related applications.<br /> (© 2026. The Author(s).)
– Name: Abstract
  Label: Competing Interests
  Group: Ab
  Data: Declarations. Ethics approval and consent to participate: Not applicable. Competing interests: The authors declare no competing interests.
– Name: Ref
  Label: References
  Group: RefInfo
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– Name: SubjectMinor
  Label: Contributed Indexing
  Group:
  Data: <i>Keywords: </i>Lycinibacillus fusiformis; Enzyme characterization; Gene cloning; Heterologous expression; Ras cheese ripening; Recombinant lipase A
– Name: NumberCAS
  Label: Substance Nomenclature
  Group: ID
  Data: EC 3.1.1.3 (Lipase)<br />0 (Detergents)<br />0 (Recombinant Proteins)<br />0 (Bacterial Proteins)
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  Label: Entry Date(s)
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  Data: <i>Date Created: </i>20260829 <i>Date Completed: </i>20260829 <i>Latest Revision: </i>20260901
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  Data: 20260901
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  Data: 10.1186/s12934-026-03084-w
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  Data: 42668381
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=cmedm&AN=42668381
RecordInfo BibRecord:
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        Value: 10.1186/s12934-026-03084-w
    Languages:
      – Code: eng
        Text: English
    Subjects:
      – SubjectFull: Recombinant Proteins metabolism
        Type: general
      – SubjectFull: Recombinant Proteins genetics
        Type: general
      – SubjectFull: Recombinant Proteins chemistry
        Type: general
      – SubjectFull: Cloning, Molecular
        Type: general
      – SubjectFull: Molecular Docking Simulation
        Type: general
      – SubjectFull: Enzyme Stability
        Type: general
      – SubjectFull: Hydrogen-Ion Concentration
        Type: general
      – SubjectFull: Substrate Specificity
        Type: general
      – SubjectFull: Lipase genetics
        Type: general
      – SubjectFull: Lipase metabolism
        Type: general
      – SubjectFull: Lipase chemistry
        Type: general
      – SubjectFull: Detergents chemistry
        Type: general
      – SubjectFull: Detergents metabolism
        Type: general
      – SubjectFull: Bacillaceae enzymology
        Type: general
      – SubjectFull: Bacillaceae genetics
        Type: general
      – SubjectFull: Bacterial Proteins genetics
        Type: general
      – SubjectFull: Bacterial Proteins metabolism
        Type: general
      – SubjectFull: Bacterial Proteins chemistry
        Type: general
      – SubjectFull: Cheese
        Type: general
    Titles:
      – TitleFull: Recombinant thermotolerant alkaline lipase from Lysinibacillus fusiformis for detergent and hard (Ras) cheese applications: cloning, expression, molecular docking, and characterization.
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            – D: 29
              M: 08
              Text: 2026 Aug 29
              Type: published
              Y: 2026
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              Value: 1475-2859
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