{"title":"Characterization of biochemical and optical properties of Nile tilapia (Oreochromis niloticus) corneal collagen","authors":"Hatem Hassan Abd-Elrahman, Wael Abdel-Moneim Omar, Hazem Abdallah Elnashar","doi":"10.1186/s43094-024-00597-2","DOIUrl":null,"url":null,"abstract":"<div><h3>Background</h3><p>Collagen extracted from fish body parts is a promising biological material. It has an important role in many pharmaceutical, medical applications and tissue engineering such as corneal regeneration and stromal replacement. The present work investigates a new trend to extract collagen from the fish cornea, as a prospected substituent of human corneal collagen by characterizing some biochemical and optical properties of the fish corneal collagen.</p><h3>Results</h3><p>Examination of the corneal tissue of Nile tilapia; <i>Oreochromis niloticus</i> was conducted using electron microscopy, Fourier transform infrared (FTIR) spectroscopy, UV–visible spectrophotometry, optical properties, and thermal properties. The fish were divided into 10 groups each of which consisted of 5 fish. 2 groups of fish were examined for each technique. Results indicated that the corneal layers of <i>O. niloticus</i> are thin at the center and thicker at the periphery with the stroma consisting of a triple helical structure collagen type I. The fish cornea showed very weak transmission at the UV regions (190 nm) and maximum transmission at the visible regions. The values of transmission (<i>T</i>), reflected light (<i>R</i>) and scattered light (<i>S</i>) were 2.685 mw, 100 × 10<sup>−3</sup> mw at 45° and 40 × 10<sup>−3</sup> mw, respectively. Consequently, the percentage of absorbed light is 21.76%. The denaturation temperature of the fish corneal stroma is 22.27 °C.</p><h3>Conclusions</h3><p>The method for obtaining fish collagen affects the specific properties of collagen and consequently its further uses as a potential biomedical substituent for mammalian collagen. Specification of the fish species and tissue type is crucial in identifying the quality as well as the physical and functional properties of the extracted collagen.</p></div>","PeriodicalId":577,"journal":{"name":"Future Journal of Pharmaceutical Sciences","volume":null,"pages":null},"PeriodicalIF":3.4000,"publicationDate":"2024-03-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://fjps.springeropen.com/counter/pdf/10.1186/s43094-024-00597-2","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Future Journal of Pharmaceutical Sciences","FirstCategoryId":"1085","ListUrlMain":"https://link.springer.com/article/10.1186/s43094-024-00597-2","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"PHARMACOLOGY & PHARMACY","Score":null,"Total":0}
引用次数: 0
Abstract
Background
Collagen extracted from fish body parts is a promising biological material. It has an important role in many pharmaceutical, medical applications and tissue engineering such as corneal regeneration and stromal replacement. The present work investigates a new trend to extract collagen from the fish cornea, as a prospected substituent of human corneal collagen by characterizing some biochemical and optical properties of the fish corneal collagen.
Results
Examination of the corneal tissue of Nile tilapia; Oreochromis niloticus was conducted using electron microscopy, Fourier transform infrared (FTIR) spectroscopy, UV–visible spectrophotometry, optical properties, and thermal properties. The fish were divided into 10 groups each of which consisted of 5 fish. 2 groups of fish were examined for each technique. Results indicated that the corneal layers of O. niloticus are thin at the center and thicker at the periphery with the stroma consisting of a triple helical structure collagen type I. The fish cornea showed very weak transmission at the UV regions (190 nm) and maximum transmission at the visible regions. The values of transmission (T), reflected light (R) and scattered light (S) were 2.685 mw, 100 × 10−3 mw at 45° and 40 × 10−3 mw, respectively. Consequently, the percentage of absorbed light is 21.76%. The denaturation temperature of the fish corneal stroma is 22.27 °C.
Conclusions
The method for obtaining fish collagen affects the specific properties of collagen and consequently its further uses as a potential biomedical substituent for mammalian collagen. Specification of the fish species and tissue type is crucial in identifying the quality as well as the physical and functional properties of the extracted collagen.
期刊介绍:
Future Journal of Pharmaceutical Sciences (FJPS) is the official journal of the Future University in Egypt. It is a peer-reviewed, open access journal which publishes original research articles, review articles and case studies on all aspects of pharmaceutical sciences and technologies, pharmacy practice and related clinical aspects, and pharmacy education. The journal publishes articles covering developments in drug absorption and metabolism, pharmacokinetics and dynamics, drug delivery systems, drug targeting and nano-technology. It also covers development of new systems, methods and techniques in pharmacy education and practice. The scope of the journal also extends to cover advancements in toxicology, cell and molecular biology, biomedical research, clinical and pharmaceutical microbiology, pharmaceutical biotechnology, medicinal chemistry, phytochemistry and nutraceuticals.