Ultrasonic Collagen Extraction from Jellyfish
- Jellyfish collagen is a high-quality collagen, which is unique but exhibits similar properties to type I, II, III and type V collagen.
- Ultrasonic extraction is a purely mechanical technique, that increases yield, accelerates the process and produces high molecular weight collagen.
Ultrasonic Jellyfish Extraction
Jellyfish is rich in minerals and proteins, and collagen is a major protein in these gelatinous marine creatures. Jellyfish is an almost abundant source found in the oceans. Often seen as a plague, the use of jellyfish for collagen extraction is beneficial in both ways, producing excellent collagen, using a sustainable natural source, and removing jellyfish blooms.
Ultrasonic extraction is mechanical extraction method, which can be precisely controlled and adapted to the raw material treated. Ultrasonic extraction has been successfully applied to isolate collagen, glycoproteins and other proteins from jellyfish.
In general, proteins isolated from jellyfish exhibit strong antioxidant activity and are therefore valuable active compounds for the food, supplement, and pharmaceutical industries.
For extraction, the whole jellyfish, the mesoglea (= major part of jellyfish umbrella), or the oral-arms can be used.
- food / pharma grade collagen
- high molecular weight
- amino acid composition
- increased yields
- rapid processing
Ultrasonic-Acid & Ultrasonic-Enzymatic Extraction
Ultrasonic extraction can be used in combination with various acid solutions to release the acid soluble collagen (ASC) from the jellyfish. Ultrasonic cavitation promotes the mass transfer between the jellyfish substrate and the acid solution by breaking cell structures and flushing the acids into the substrate. Thereby, the collagen as well as other targeted proteins are transferred into the liquid.
In a subsequent step, the remaining jellyfish substrate is treated with enzymes (i.e. pepsin) under ultrasonication to isolate the pepsin soluble collagen (PSC). Sonication is known for its capability to increase enzyme activity. This effect is based on the ultrasonic dispersion and deagglomeration of the pepsin aggregates. Homogeneously dispersed enzymes offer an increased surface for mass transfer, which is correlated to higher enzyme activity. Furthermore, the powerful ultrasound waves opens up the collagen fibrils so that the collagen is released.
Research has shown that an ultrasonically assisted enzymatic (pepsin) extraction results in higher yields and a shorter extraction process.
High Performance Ultrasonicators for Collagen Production
Hielscher Ultrasonics supplies powerful ultrasonic systems from lab to bench-top and industrial scale. To ensure optimum extraction output, reliable sonication under demanding conditions can be performed continuously. All industrial ultrasonic processors can deliver very high amplitudes. Amplitudes of up to 200µm can be easily continuously run in 24/7 operation. For even higher amplitudes, customized ultrasonic sonotrodes are available. The robustness of Hielscher’s ultrasonic equipment allows for 24/7 operation at heavy duty and in demanding environments.
The table below gives you an indication of the approximate processing capacity of our ultrasonicators:
|Batch Volume||Flow Rate||Recommended Devices|
|0.5 to 1.5mL||n.a.||VialTweeter|
|1 to 500mL||10 to 200mL/min||UP100H|
|10 to 2000mL||20 to 400mL/min||UP200Ht, UP400St|
|0.1 to 20L||0.2 to 4L/min||UIP2000hdT|
|10 to 100L||2 to 10L/min||UIP4000hdT|
|n.a.||10 to 100L/min||UIP16000|
|n.a.||larger||cluster of UIP16000|
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- Nicholas M.H. Khonga, Fatimah Md. Yusoff, B. Jamilah, Mahiran Basri, I. Maznah, Kim Wei Chan, Nurdin Armania, Jun Nishikawa (2018): Improved collagen extraction from jellyfish (Acromitus hardenbergi) with increased physical-induced solubilization processes. Food Chemistry Vol. 251, 15 June 2018. 41-50.
- Guoyan Ren, Bafang Li, Xue Zhao, Yongliang Zhuang, Mingyan Yan (2008): Ultrasound-assisted extraction technology for the extraction of glycoprotein from jellyfish (Rhopilema esculentum) oral-arms. Transactions of the Chinese Society of Agricultural Engineering 2008-02.
- Guoyan Ren, Bafang Li, Xue Zhao, Yongliang Zhuang, Mingyan Yan, Hu Hou, Xiukun Zhang, Li Chen (2009): Screening of extraction methods for glycoproteins from jellyfish (Rhopilema esculentum) oral-arms by high performance liquid chromatography. Journal of Ocean University of China 2009, Volume 8, Issue 1. 83–88.
Facts Worth Knowing
Collagen is fibrous protein with triple helix structure and the major insoluble fibrous protein in the extracellular matrix and in connective tissue.There are at least 16 types of collagens but most of them are (approx. 90%) belong to type I, type II, and type III. Collagen is the most abundant protein in the human body found in bones, muscles, skin and tendons. In mammals, it contributes 25-35% of the whole body protein. The following list gives examples of tissues where collagen types are the most abundant: Type I—bone, dermis, tendon, ligaments, cornea; Type II—cartilage, vitreous body, nucleus pulposus; Type III—skin, vessel wall, reticular fibers of most tissues (lungs, liver, spleen, etc.); Type IV—basement membranes, Type V—often co-distributes with Type I collagen, especially in the cornea. This naturally favored the commercial exploitation of the standard abundant collagens (collagens I–V), by isolating and purifying them, mostly from human, bovine and porcine tissues, by conventional, high yield manufacturing processes, leading to high quality collagen batches. (Silva et al., Mar. Drugs 2014, 12)
Endogenous collagen is a natural collagen synthesised by the body, whilst exogenous collagen is synthetic and may come from an external source such as supplements. Collagen occurs in the body, especially in the skin, bones and connective tissues. The collagen production in an organism decreases with age and exposure to factors such as smoking and UV light. In medicine, collagen can be used in collagen wound dressings to attract new skin cells to wound sites.
Collagen is widely used in supplements and pharmaceuticals since it can be resorbed. This means that it can be broken down, transformed, and taken back into the body. It can also be formed into compressed solids or lattice-like gels. Its wide range of functions and its natural occurrence makes it clinically versatile and suitable for a variety of medical purposes. For medical use, collagen may be obtained from bovine, porcine, sheep, an marine organisms.
There are four major methods to isolate collagen from animals: the salting-out, alkaline, acid, and enzyme method.
The acid and enzymatic methods are most commonly used in combination for the production of high-quality collagen. Since parts of the collagen is acid-soluble collagen (ASC) and other parts are pepsin-soluble collagen (PSC), the acid treatment is followed by an enzymatic pepsin extraction. The acid collagen extraction is carried out using organic acids such as chloracetic, citric, or lactic acid. To release pepsin-soluble collagen (PSC) from the remaining material of the acid collagen extraction process, the undissolved matter is treated with the enzyme pepsin, to isolate the pepsin soluble collagen (PSC). PSC is commonly applied in combination with 0.5M of acetic acid. Pepsin is a common enzyme as it is able to maintain a collagen structure by cleaving to the N-terminal of the protein chain and non-helix peptide.
Collagen is used in nutritional supplements (nutraceuticals), cosmetic products and medicine. Mammalian and marine (fish) collagen is available on the market and can be bought in any quantities. Jellyfish collagen is a new form of collagen, which is human biocompatible and non-mammalian (desease-free). Jellyfish collagen does not match any particular type of collagen (type I-V), but it exhibits the various properties of the collagen types I, II and V.
Glycoproteins are found in many organisms from bacteria to humans and have different functions. These proteins with short oligosaccharide chains are involved in cell surface recognition by hormones, viruses and other substances in many cellular events. In addition, cell surface antigens serve as mucin secretion of the extracellular matrix element, gastrointestinal and urogenital tract. Almost all of the globular proteins in plasma except albumin, secreted enzymes and proteins have glycoprotein structure. The cell membrane is composed of protein, lipid and carbohydrate molecules. The role of glycoproteins in the cell membrane, on the other hand, affects the number and distribution of proteins. These proteins are involved in the transition from membrane to substance. The number and distribution of glycolipids and glycoproteins give cell specificity.
Glycoproteins are responsible for the recognition of cells, the selective permeability of the cell membrane and the uptake of hormones. There are 7 main types of monosaccharides in the carbohydrate part of glycoproteins. These monosaccharides combine with different sequencing and different bond structures, resulting in a large number of carbohydrate chain structures. A glycoprotein may contain a single N-linked oligosaccharide structure or may contain more than one type of oligosaccharide. The N-linked oligosaccharides may be of the same or different structures or may also be present in O-linked oligosaccharides. The number of oligosaccharide chains varies depending on protein and function.
Sialic acids in glycoproteins, an element of glycocalyx, play an important role in the recognition of cells. If the sialic acids are destroyed for any reason, the glycocalyx structure of the membrane is disrupted and the cell cannot perform most of the specified tasks. Also, there are some structural glycoproteins. They are fibronectins, laminins, fetal fibronectins and they all have different missions in the body. Also in eukaryotic glycoproteins, there are some monosaccharides mostly in hexose and aminohexose type. They can assist in protein folding, improve protein’s stability and are involved in cell signalling.