Evidence map›Paper›PMID 40694201›Full record

ArticleBiotechnology letters2025

Optimization and characterization of collagenase KU665299 and its application in effective in-vitro clot digestion.

Shikha Chauhan, Kriti Kanwar, Deepika Sharma, Harjodh Singh, Deepak Sharma, Vishal Ahuja, Wamik Azmi

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Article in Biotechnology letters, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

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2citing papers in PubMed
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1 · What the graph read from it

What it found

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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

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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.

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4 · The record

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5 · Who and what money

Authors and funding

7 authors.

Shikha Chauhan *Department of Biotechnology, Himachal Pradesh University, Summerhill Shimla, Shimla, Himachal Pradesh, 171005, India.
Kriti Kanwar *Department of Biotechnology, Himachal Pradesh University, Summerhill Shimla, Shimla, Himachal Pradesh, 171005, India.ORCID http://orcid.org/0000-0002-3774-0024
Deepika SharmaDepartment of Biotechnology, Chandigarh College of Technology CGC, Landran, Mohali, Punjab, 140307, India.
Harjodh SinghDepartment of Biotechnology, Chandigarh College of Technology CGC, Landran, Mohali, Punjab, 140307, India.
Deepak SharmaDepartment of General Surgery, Saveetha Medical College and Hospital, Saveetha Institute of Medical and Technical Sciences (SIMATS), Thandalam, Chennai, Tamil Nadu, 602105, India.
Vishal AhujaUniversity Institute of Biotechnology, Chandigarh University, Mohali, Punjab, 140413, India.
Wamik AzmiDepartment of Biotechnology, Himachal Pradesh University, Summerhill Shimla, Shimla, Himachal Pradesh, 171005, India. wamikazmi@rediffmail.com.ORCID http://orcid.org/0000-0003-2689-4359

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

objectiveThe study employed response surface methodology (RSM) to optimize physicochemical variables for extracellular collagenase production by gram negative bacterial strain Chryseobacterium contaminans KU665299 under submerged fermentation. It is also revealing the ability of collagenase to degrade collagen, main structural protein in human blood.

resultThe study successfully enhanced collagenase activity by 1.2 folds through Response Surface Methodology (RSM) and 5.33 folds through purification of enzyme using ammonium sulfate precipitation and DEAE-Sepharose chromatography (specific activity with 538.0 U/mg). SDS-PAGE analysis identified its molecular weight as 32 kDa. Optimal conditions for the enzyme's activity were pH 7.5 and 40 °C. Kinetic studies of collagenase KU665299 revealed specificity for collagen, with K

conclusionThe study successfully optimized and characterized a novel collagenase from C. contaminans KU665299, revealing its high specificity, stability, and efficiency in degrading collagen and its promising ability to rapidly digest blood clots for potential thrombolytic properties.

Indexed as

CollagenasesFibrinolytic AgentsCollagenEnzyme StabilityHumansHydrogen-Ion ConcentrationKineticsSubstrate SpecificityTemperatureCollagenCollagenasesFibrinolytic AgentsChryseobacterium contaminansCollagenase KU665299Thrombolytic agent

Identifiers

PMID40694201

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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.