Recovery of gelatin from bovine skin with the aid of pepsin and its effects on the characteristics of the extracted gelatin

• Main Authors: Ahmad, S.A (Author), Ahmad, T. (Author), Akhtar, M.T (Author), Awad, E.A (Author), Ismail, A. (Author), Khalil, K.A (Author), Sazili, A.Q (Author)
• Format: Article
• Language: English
• Published: MDPI AG 2021
• Series: Polymers
• Subjects: Alpha helix; Amides; Bovine skin; Electrophoresis; Enzymes; Fourier transform infrared spectroscopy; Free amino acid; FTIR; Functional properties; Gel electrophoresis; Gel strengths; Gelatin; High yield; Mammals; NMR; Nuclear magnetic resonance; Pepsin; Protein chains; Protein patterns; Recovery
• Online Access: View Fulltext in Publisher; View in Scopus

 Pepsin enzyme was used to pretreat the bovine skin at the rate of 5, 15, and 25 units of enzyme/g of skin to recover gelatin, and the recovered gelatins were referred to as Pe5, Pe15, and Pe25, respectively. The gelatin yield increased significantly (p < 0.05) from 18.17% for Pe5 to 24.67% for Pe25 as the level of pepsin increased, but the corresponding gel strength and viscosity decreased significantly (p < 0.05) from 215.49 to 56.06 g and 9.17 to 8.17 mPa.s for Pe5 and Pe25, re-spectively. β-and α1-and α2-chains were degraded entirely in all the gelatins samples as observed in protein pattern elaborated by gel electrophoresis.1H nuclear magnetic resonance (1H NMR) analysis indicated the coiled structure of gelatin protein chains. The lowest amide III amplitude of Pe25 as found by Fourier transform infrared (FTIR) spectroscopy indicated that α-helix structure of protein chains were lost to more irregular coiled structure. Thus, it could be summarized that pepsin might be used at the lower level (5 units/g of wet skin) to extract gelatin from bovine skin with good functional properties and at higher level (15/25 units/g of wet skin) to obtain gelatin of industrial grade with high yield. © 2021 by the authors. Licensee MDPI, Basel, Switzerland.