A lipase from Lacticaseibacillus rhamnosus IDCC 3201 with thermostability and pH resistance for use as a detergent additive

Mi Dan Kang, Go Eun Choi, Jeong Hwa Jang, Sung Chul Hong, Hee Soo Park, Dong Hyun Kim, Won Chan Kim, Natasha P. Murphy, Young Hoon Jung

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

Abstract: Lipases are important biocatalysts and ubiquitous in plants, animals, and microorganisms. The high growth rates of microorganisms with low production costs have enabled the wide application of microbial lipases in detergent, food, and cosmetic industries. Herein, a novel lipase from Lacticaseibacillus rhamnosus IDCC 3201 (Lac-Rh) was isolated and its activity analyzed under a range of reaction conditions to evaluate its potential industrial application. The isolated Lac-Rh showed a molecular weight of 24 kDa and a maximum activity of 3438.5 ± 1.8 U/mg protein at 60 °C and pH 8. Additionally, Lac-Rh retained activity in alkaline conditions and in 10% v/v concentrations of organic solvents, including glycerol and acetone. Interestingly, after pre-incubation in the presence of multiple commercial detergents, Lac-Rh maintained over 80% of its activity and the stains from cotton were successfully removed under a simulated laundry setting. Overall, the purified lipase from L. rhamnosus IDCC 3201 has potential for use as a detergent in industrial applications.

Original languageEnglish
Article number365
JournalApplied Microbiology and Biotechnology
Volume108
Issue number1
DOIs
StatePublished - Dec 2024

Keywords

  • Detergent additive
  • Lipase
  • Recombinant enzyme
  • Thermostability
  • pH resistance

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