Page | 1 AROC in Pharmaceutical and Biotechnology, 2021, 1(2);01-10 https://doi.org/10.53858/arocpb01020110 Extraction and characterization of type 1 collagen from the skin and scales of Heterotis niloticus and Lates niloticus Victoria Ifeoluwa Ayo 1* , Dickson Achimugu Musa 2 and Evans Chidi Egwim 3 1 Department of Biochemistry, Federal University Wukari, Taraba state, Nigeria. 2 Department of Biochemistry, Ibrahim Badamasi Babangida University, Lapai, Niger state, Nigeria. 3 Department of Biochemistry, Federal University of Technology, Minna, Niger state Nigeria. ABSTRACT The study is aimed to extract and characterize collagens from the skin and scale of two selected Nigerian freshwater fish species (Heterotis niloticus and Lates niloticus) using either pepsin (PSC) or acid-soluble (ASC) extraction. The collagen was extracted using 0.5M acetic acid and pepsin. The collagen yield was determined and characterized by SDS PAGE, and FTIR. Collagen extraction yields varied with the extraction process; the yield was significantly higher in the skin (5.08±0.34–33.97±1.78 %) than in the scale (1.76–8.05 %). The absorption peaks of the extracted collagen using acetic acid and pepsin show that only ASC of skin (3344.27 cm -1 ) and scale (3495.85 cm -1 ) of H. niloticus shows the peaks characteristic of Amide A, while Amide B peaks of collagen extracted from the skin and scale of H. niloticus and L. niloticus were found at 2974.46 cm -1 and 2925.7 cm -1 , representing an asymmetrical stretch of CH 2 . Similarly, ASC on the skin (1558.36 cm -1 ) and scale (1576.46 cm -1 ) of H. niloticus shows the absorption peak characteristics of amide II. ASC on the skin of H. niloticus (1671.05 cm -1 ), PSC on scale of H. niloticus (1658.55 cm -1 ), and on scale of H. niloticus (1678.65 cm - 1 ) shows absorption peaks in range characteristic of amide 1. There were no differences in the skin and scale collagen profiles among the two fish species when characterized by SDS-PAGE. Our data revealed that the skin and scale of Lates niloticus and Heterotis niloticus could be a good alternative source of high-quality collagen for industries. Keywords: Collagen; Skin; Scales; Characterization; Lates niloticus; Heterotis niloticus Received: 22 July 2021, Revised: 21 July 2021, Published: 22 July 2021 Citation: Ayo, V.I., Musa, D.A., and Egwim, E.C. (2021). Extraction and characterization of type 1 collagen from the skin and scales of Heterotis niloticus and Lates niloticus. AROC in Pharmaceutical and Biotechnology, 1(2);01-10, https://doi.org/10.53858/arocpb01020110 1.0 Introduction Structural proteins such as collagens are mostly found abundantly in the extracellular matrix of several connective tissues which comprises about 30% of the entire proteins in the vertebrate’s body including bones, ligaments, tendons and cartilage [1, 2]. Collagen plays a crucial function to assist and protect the body when dispersed in a wide range of vertebrate connective tissues [3]. Collagen also has emulsification properties, gel qua lity, low viscosity, biological compatibility, water int ake and saturation effects as biological natural ass ets that can be widely used in pharmaceutical, food beauty care products and biomedical materials [4]. In addition, several biological activities of collagen including anti-hypertensive, antioxidant, and antimicrobial properties have been reported [5-9]. Fish scales and skins are known to contain biocomposites with highly ordered type 1 collagen fibres and hydroxyapatite [10, 11]. Although there are many reports about collagen from the skin of marine organisms, there are few studies of fish scales like the studies of Kimura et al. [12] and those of Shao et al. [13]. Collagens from these sources are mainly the type I collagen with lower denaturation temperature than the collagen from porcine dermis [14]. H. niloticus and L. niloticus are freshwater species AROC in Pharmaceutical and Biotechnology 2021, 1(2);01-10 https://doi.org/10.53858/arocpb01020110 Arocjournal.com RESEARCH ARTICLE *Corresponding author Victoria I. Ayo Email: oluwavicky7@gmail.com