Evidence map›Paper›PMID 38842543›Full record

ArticleApplied microbiology and biotechnology2024

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

Abstract read
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In one paragraph

Article in Applied microbiology and biotechnology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

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

2 citing papers in PubMed.

  1. Article
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4 · The record

Corrections and comments

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

9 authors.

Mi Dan Kang *School of Food Science and Biotechnology, Kyungpook National University, Daegu, 41566, Republic of Korea.
Go Eun Choi *School of Food Science and Biotechnology, Kyungpook National University, Daegu, 41566, Republic of Korea.
Jeong Hwa Jang *School of Food Science and Biotechnology, Kyungpook National University, Daegu, 41566, Republic of Korea.
Sung-Chul HongDepartment of Food Science and Biotechnology, Kunsan National University, Gunsan, 54150, Republic of Korea.
Hee-Soo ParkSchool of Food Science and Biotechnology, Kyungpook National University, Daegu, 41566, Republic of Korea.
Dong Hyun KimSchool of Food Science and Biotechnology, Kyungpook National University, Daegu, 41566, Republic of Korea.
Won Chan KimDepartment of Applied Biosciences, Department of Integrative Biology, Kyungpook National University, Daegu, 41566, Republic of Korea.
Natasha P MurphyRenewable Resources and Enabling Sciences Center, National Renewable Energy Laboratory, Golden, CO, 80401, USA. Natasha.murphy@nrel.gov.
Young Hoon JungSchool of Food Science and Biotechnology, Kyungpook National University, Daegu, 41566, Republic of Korea. younghoonjung@knu.ac.kr.ORCID http://orcid.org/0000-0002-0781-3608

Funding

National Research Foundation of Korea 2020R1C1C1005251
6 · The paper itself

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. KEY POINTS: • A novel lipase (Lac-Rh) was isolated from Lacticaseibacillus rhamnosus IDCC 3201 • Purified Lac-Rh exhibited its highest activity at a temperature of 60 °C and a pH of 8, respectively • Lac-Rh remains stable in commercial laundry detergent and enhances washing performance.

Indexed as

DetergentsEnzyme StabilityLacticaseibacillus rhamnosusLipaseBacterial ProteinsHydrogen-Ion ConcentrationMolecular WeightTemperatureBacterial ProteinsDetergentsLipaseDetergent additiveLipasepH resistanceRecombinant enzymeThermostability

Identifiers

PMID38842543
PMCPMC11156721

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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.