Characterization of Collagen from Three Genetic Lines (Gray, Red and F1) of Oreochromis niloticus (Tilapia) Skin in Young and Old Adults

Abstract

From tilapia (Oreochromis niloticus) farming, the by-products have been identified as a source of collagen that could be used for the development of dermocosmetics or pharmaceutical products. However, the characteristics of collagen related to a specific strain or culture must be well defined prior to its application. Collagen was extracted from the skin of three strains of tilapia: red YY males (YY: two Y-type sex chromosomes), XX gray females, and the F1: offspring of crossing red YY males with XX gray females; at different ages in the adult phase, using acetic acid and pepsin enzyme. The characteristics of acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) were shown by SDS-PAGE band profiles to be similar to bovine collagen type I (SIGMA), the PSC of gray tilapia being more fragile to temperature changes, consistent with the results of fractional viscosity. The characteristics of the F1 progeny were prioritized for being a commercially productive and sustainable source for the extraction of collagen, and the ASC form, being the one with the greatest stability and advantage over PSC, of importance to our investigations, leads to a controlled digestion as in the case of peptide induction, and also in the development of natural products in the pharmaceutical and/or dermocosmetic industry. Evaluations of the triple helix structure by FT-IR, X-ray diffraction and UV–visible spectroscopy give similar results between the strains: red, gray, and F1, and between ages in the adult form F1 (15, 24, and 36 months of age). Consequently, the skin of tilapia in adult form is recommended sustainably for up to 24 months of age where the collagen is obtained with the use of acetic acid without enzymatic treatment.

Physicochemical and Microstructural Analyses of Pepsin-Soluble Collagens Derived from Lizardfish (Saurida tumbil Bloch, 1795) Skin, Bone and Scales

“…The differences in the peaks might be due to sample preparation that was arranged in a random order. Moreover, our previous reports on acid-extracted collagens also exhibited two diffraction peaks [ 25 , 26 , 27 ] and other previous reports of carp ( C. carpio ) scale collagen [ 52 ], golden pompano ( T. blochii ) skin and bone collagen [ 7 ] and tilapia ( O. niloticus ) skin collagen [ 53 ]. Furthermore, d(Å) was used to predict the minimum value of repeated spacing d (Å).…”

Comparison of Physicochemical and Structural Properties of Acid-Soluble and Pepsin-Soluble Collagens from Blacktip Reef Shark Skin

“…The maximum absorbance of collagen at 234 nm was due to higher amounts of glycine (which absorbs maxima at 216.8 nm) and peptide bonds (at 230 nm) [23]. In addition, the liberation of more peptides (which tend to absorb UV maxima at 230 nm) by pepsin treatment might be the actual reason for the higher absorption of PSC at 234 nm than ASC.…”

Construction of antibacterial nano-silver embedded bioactive hydrogel to repair infectious skin defects

“…The lyophilized tissue was ground into powder. Then, 20 mg mL − 1 of the powder was digested using pepsin in a dilute hydrochloric acid solution (pH 2-3) for 10 min [21], and a ⌀5-nm Ag NP solution was added dropwise, and the mixture was stirred rapidly. Subsequently, this mixture was digested for 2 h until the gel was translucent and viscous and was stored in a refrigerator at 4 °C.…”

“…Day and night were alternated for 12 h. According to the National Institute of Health publication No. [18][19][20][21][22][23]1985, which is typically referenced for the care and use of laboratory animals, great care should be taken with rats. The rats were anesthetized using ketamine (30.0 mg kg − 1 ), their dorsal hair was removed, and their skin was rinsed using 70% ethanol.…”