Abstract
Type I collagen is commonly used in medical materials and cosmetics. While it can be extracted from the skin and bones of mammals, marine collagen has attracted attention recently, since the use of mammalian collagen could result in zoonosis, and products containing mammalian collagen are avoided due to some religious beliefs. Chemical extractions using strong acids and alkalis, thermal extractions, and other nonconventional methods have been used for collagen extraction. However, there are few reports on environmentally friendly methods. Although heat extractions provide higher yields of collagen, they often cause collagen denaturation. Therefore, dilute acetic acid and ultrafine bubbles of oxygen, carbon dioxide, and ozone were used to extract type I collagen from tilapia scales. The extraction performance of the different conditions employed was qualitatively analyzed by SDS-PAGE electrophoresis, and the collagen concentration was quantified using circular dichroism spectroscopy by monitoring the peak intensity at 221 nm, which is specific to the triple helix of type I collagen. Collagen was extracted from tilapia scales with a yield of 1.58% by the aeration of ultrafine bubbles of carbon dioxide gas in a 0.1 M acetic acid solution for 5 h.
Highlights
Using Acetic Acid and UltrafineThe extracellular matrix is commonly defined as noncellular component tissue that provides both biochemical and essential structural support to its cellular constituents [1].Collagen is an extracellular protein that accounts for 25–30% of the total protein content within the human body [2]
Type I collagen was extracted from tilapia scales by bubbling ultrafine bubbles of three separate gases (O2, CO2, and O3 ) into an acetic acid solution
SDS-PAGE analysis of the extracted samples displayed bands indicating the presence of three chains of type I collagen, namely α1, α2, and β, when O2 and CO2 were used
Summary
Using Acetic Acid and UltrafineThe extracellular matrix is commonly defined as noncellular component tissue that provides both biochemical and essential structural support to its cellular constituents [1].Collagen is an extracellular protein that accounts for 25–30% of the total protein content within the human body [2]. Type I collagen is present in tendons and ligaments [8,9], while the majority type found in human cartilage is type II collagen [10]. Based on the organism of origin, collagen is classified as either mammalian or marine; the triple-helix structure consisting of three polypeptide chains containing repeating units of three amino acids—(Gly-Pro-Xaa)n —is common to both mammalian and marine collagen [11]. The levels of proline and hydroxyproline in the collagen of different fish species vary significantly depending on the environmental temperature in which the fish lives, as the amounts of these amino acids affect the thermal stability of the collagen [12,13].
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