Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Glycosaminoglycans01:23

Glycosaminoglycans

8.0K
Glycosaminoglycans (GAGs), also known as mucopolysaccharides, are long and linear polymers comprising of specific repeating disaccharides - the amino sugar that can be N-acetylglucosamine or N-acetylgalactosamine, and a uronic acid that is usually glucuronic acid or iduronic acid.
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
8.0K
Collagens are the Major Structural Proteins of ECM01:13

Collagens are the Major Structural Proteins of ECM

6.5K
Three main types of fibers are secreted by fibroblasts: collagen fibers, elastic fibers, and reticular fibers. Collagen fiber is made from fibrous protein subunits linked together to form a long, straight fiber. Collagen fibers, while flexible, have great tensile strength, resist stretching, and give ligaments and tendons their characteristic resilience and strength. These fibers hold connective tissues together, even during the body's movement.
Connective tissue proper includes loose...
6.5K
Type IV Collagen of Basal Lamina01:05

Type IV Collagen of Basal Lamina

3.4K
Type IV collagen is a 400 nm long, network-forming collagen that acts as a barrier between the epithelial and endothelial cells. Type IV collagen  forms the backbone of the basement membrane by scaffolding with laminin, entactin, proteoglycans, and fibronectin. Apart from rendering structural support to the basement membrane, it also helps entail signaling potentials necessary for both pathological and physiological functions.
A type IV collagen molecule has six alpha chains which can...
3.4K
Connective Tissue Fibers and Ground Substance01:17

Connective Tissue Fibers and Ground Substance

42.7K
One of the significant functions of connective tissue is connecting tissues and organs. Unlike epithelial tissue that is composed of cells closely packed with little or no extracellular space in between, connective tissue cells are dispersed in a matrix. The matrix usually includes a large amount of extracellular material produced by the connective tissue cells that are embedded within it. It plays a significant role in the functioning of this tissue. The major component of the matrix is a...
42.7K
Reticular Dermis01:15

Reticular Dermis

5.5K
The papillary and reticular dermis are the two layers of the dermis. They are made of connective tissue with fibers of collagen extending from one to the other, making the border between the two somewhat indistinct. The dermal papillae extending into the epidermis belong to the papillary layer, whereas the dense collagen fiber bundles below belong to the reticular layer.
Reticular Layer
Underlying the papillary layer is the much thicker reticular layer, composed of dense, irregular connective...
5.5K
Fibrous Proteins00:55

Fibrous Proteins

5.3K
Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...
5.3K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Production of hydrolytic enzymes from crop waste for bioconversion of lignocellulosic biomass to ethanol.

3 Biotech·2026
Same author

Production of squalene and fatty acids by Thraustochytrium sp. RT2316-16: effects of dissolved oxygen and the medium composition.

Bioresources and bioprocessing·2025
Same author

Ce, Gd and Yb accumulation in microalgae: an L-edge XAS study.

Acta crystallographica. Section C, Structural chemistry·2025
Same author

Editorial: Microalgae as sustainable food resources: prospects, novel species, bioactive compounds, cultivation process and food processing.

Frontiers in nutrition·2025
Same author

Thermal degradation kinetics and purification of C-phycocyanin from thermophilic and mesophilic cyanobacteria.

Journal of biotechnology·2024
Same author

Infrared Spectroscopy of Synovial Fluid Shows Accuracy as an Early Biomarker in an Equine Model of Traumatic Osteoarthritis.

Animals : an open access journal from MDPI·2024

Related Experiment Video

Updated: Apr 11, 2026

In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen
07:54

In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen

Published on: September 20, 2012

13.8K

Gelatin and Collagen from Sheepskin.

Andrea Marie E Matinong1, Kim L Pickering2, Mark R Waterland1

  • 1School of Food and Natural Sciences, Massey University, Palmerston North 4442, New Zealand.

Polymers
|June 19, 2024
PubMed
Summary

Sheepskins, often discarded as waste, can be a valuable source of collagen and gelatin. Acid-based extraction methods yield purer collagen and gelatin compared to alkali methods, offering a sustainable alternative.

Keywords:
collagenextractiongelatinsheepskin

More Related Videos

An Improved Method for the Preparation of Type I Collagen From Skin
05:17

An Improved Method for the Preparation of Type I Collagen From Skin

Published on: January 21, 2014

22.9K
Three-dimensional Biomimetic Technology: Novel Biorubber Creates Defined Micro- and Macro-scale Architectures in Collagen Hydrogels
12:07

Three-dimensional Biomimetic Technology: Novel Biorubber Creates Defined Micro- and Macro-scale Architectures in Collagen Hydrogels

Published on: February 12, 2016

9.2K

Related Experiment Videos

Last Updated: Apr 11, 2026

In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen
07:54

In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen

Published on: September 20, 2012

13.8K
An Improved Method for the Preparation of Type I Collagen From Skin
05:17

An Improved Method for the Preparation of Type I Collagen From Skin

Published on: January 21, 2014

22.9K
Three-dimensional Biomimetic Technology: Novel Biorubber Creates Defined Micro- and Macro-scale Architectures in Collagen Hydrogels
12:07

Three-dimensional Biomimetic Technology: Novel Biorubber Creates Defined Micro- and Macro-scale Architectures in Collagen Hydrogels

Published on: February 12, 2016

9.2K

Area of Science:

  • Biomaterials Science
  • Waste Valorization
  • Protein Chemistry

Background:

  • Sheepskins are typically disposed of as solid waste due to low demand for leather.
  • Sheepskins represent a potential source of valuable proteins like collagen and its derivative, gelatin.
  • Sustainable utilization of abattoir by-products is an ongoing area of research.

Purpose of the Study:

  • To investigate sheepskins as a viable source for collagen and gelatin extraction.
  • To compare the efficacy of different extraction methods (acid, acid-enzyme, alkali) for collagen recovery.
  • To characterize the extracted collagen and gelatin products.

Main Methods:

  • Sheepskins were processed using acid extraction, acid extraction with enzymes, and alkali extraction.
  • Characterization involved Scanning Electron Microscopy (SEM), Fourier-Transform Infrared Spectroscopy (FTIR), Small Angle X-ray Scattering (SAXS), and Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis (SDS-PAGE).
  • Hydroxyproline content was measured to determine product purity.

Main Results:

  • Extraction yields ranged from 3.1% to 4.8%.
  • Product purity, indicated by hydroxyproline content, was significantly higher in acid (59%) and acid-enzyme (68%) extracts compared to alkali (7.8%).
  • SDS-PAGE revealed different molecular weight fragments depending on the extraction method, with acid-enzyme yielding smaller fragments.

Conclusions:

  • Sheepskin is a promising source for collagen-gelatin materials.
  • Acid-based extraction methods are more effective for obtaining purer collagen and gelatin.
  • The study demonstrates a sustainable approach to utilizing abattoir by-products for valuable biomaterials.