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Related Concept Videos

Green Algae01:21

Green Algae

Green algae, also referred to as chlorophytes, are different from red algae in having the chloroplasts containing chlorophylls a and b, which give them their distinct green hue. However, they lack phycobiliproteins, preventing them from developing the red or blue-green pigmentation seen in red algae. In terms of photosynthetic pigment composition, green algae closely resemble plants and share a close evolutionary relationship with them. Taxonomically Green algae belong to Phylum Chlorophyta in...

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Related Experiment Video

Updated: Jun 5, 2026

Preparation of Keratin Hydrolysate from Chicken Feathers and Its Application in Cosmetics
08:29

Preparation of Keratin Hydrolysate from Chicken Feathers and Its Application in Cosmetics

Published on: November 27, 2017

Bioprospecting keratinous materials.

L N Jones1, R D Sinclair, J Carver

  • 1Department of Medicine, University of Melbourne, St Vincent's Hospital, Melbourne 3065, Australia 5005.

International Journal of Trichology
|December 29, 2010
PubMed
Summary
This summary is machine-generated.

Bioprospecting keratinous materials like feathers and wool yielded bioactive peptides. These novel peptides show promise for functional foods and nutraceuticals, particularly in inhibiting amyloid aggregation.

Keywords:
Bioactive peptidesbioprospectingkeratin

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Area of Science:

  • Bioprospecting and Peptide Discovery
  • Nutraceuticals and Functional Foods
  • Biochemistry and Protein Science

Background:

  • Keratin-containing materials (wool, hair, feathers) are abundant natural protein sources.
  • Proline-rich peptides are known for bioactivity in disease models (cancer, hypertension, Alzheimer's).
  • The bioactivity of keratin-derived peptides remains largely unexplored.

Purpose of the Study:

  • To investigate the potential of bioprospecting keratinous materials for novel bioactive peptides.
  • To screen peptide libraries from avian and mammalian keratin sources for bioactivity.
  • To evaluate the inhibitory effect of these peptides on amyloid fibril formation.

Main Methods:

  • Enzymatic hydrolysis of mammalian (cow epidermis, sheep wool) and avian (chicken feather) keratin.
  • Development and validation of a bio-assay using reduced and carboxymethylated bovine K-casein (RCMk-CN) and Thioflavin T (ThT) to quantify amyloid fibril inhibition.
  • Screening of 27 peptide products (9 from each source) in the validated fibril inhibition assay.

Main Results:

  • Three out of 27 tested peptide products exhibited significant bioactivity in inhibiting K-casein fibril formation.
  • High-Performance Liquid Chromatography (HPLC) profiles indicated the complexity of the active peptide mixtures.
  • The findings demonstrate the potential of keratin sources for discovering functional peptides.

Conclusions:

  • Bioprospecting keratinous materials is a promising strategy for identifying novel bioactive peptides.
  • Keratin-derived peptides show potential as functional food ingredients and nutraceuticals.
  • Further research is warranted to isolate and characterize the specific bioactive peptides from these sources.