Optimisation and characterisation of acid soluble collagen from japanese sea bass scales using ultrasonic assisted extraction /
Arthi Srinivasan
- xiv, 98 pages : Illustration ; 30 cm.+ 1 CD ROM
Faculty of Chemical and Process Engineering Technology
Thesis (Master of Science) -- Universiti Malaysia Pahang – 2022
Includes bibliographical references
Collagen is the most abundant protein in vertebrates and invertebrates and is the major structural protein comprising about 30% of the total protein in the human body. Due to its unique biodegradability characteristics, natural abundance, good mechanical features, low density, hydrophobic behaviour, biocompatibility, environmentally friendly, and low-cost applications, collagen has been used extensively in many applications. The objective of this research aimed to extract the collagen from fish scales using acidic, pepsin hydrolysis, and ultra-sonication assisted acid and pepsin extraction methods; To optimize the ultrasonication process and to characterize the extracted collagen. Conventional collagen extraction process has been time-consuming and produced low yields. The use of ultrasound can relatively improve the extraction efficiency. This research investigated the potential of ultrasound for the extraction of collagen from seabass scales and compared yields and purities to the conventional extraction method to find an advanced method for collagen extraction. For extraction of acid-soluble collagen using ultrasound, the acetic acid concentration, time, temperature, ultrasonication time parameters were investigated to optimise performance. ANOVA demonstrated the model is significant and has a p-value less than 0.05, with the R2 was 0.91. The collagen yield for the conventional method of acid soluble and pepsin soluble collagen extraction 12.86% and 14.23%. The ultrasound-assisted extraction shows increased yield of acid soluble and pepsin soluble collagen extraction up to 13.58% and 15.36%. The characterization of the collagen is done using Fourier transforms infrared spectroscopy (FTIR) revealed that the extracted collagens with functional groups amide A, II, III represent a fingerprint for collagen structure. Thermogravimetric analysis, (TGA) showed that the weight loss occurred in two different stages. Scanning electron microscopy (SEM) was used to examine the surface morphology for collagen molecule. UV visible spectroscopy was used to determine the purity of the collagen. Additionally, the properties of collagen like solubility, viscosity, denaturation temperature have been studied. Collagens have higher solubilisation at the acid pH ranges, and PSC is more soluble than ASC and there is a decrease in solubility with the increase in NaCl concentration. The denaturation temperature (Td) of ASC, PSC, UASC, UPSC was estimated to be 30°C and 34.56°C, 33.2°C, 37.2°C, respectively. It is concluded that fish scales can be an alternative source of collagen with high purity for application in various field.
THE0009455(Local)
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