We have heard a number of benefits Collagen has to offer to a human body. From anti-aging to stronger muscles, bones, and better joint health to beautiful and flawless skin; collagen is a super supplement that contributes a lot to overall health. Though it is made in the body naturally, its production is affected by aging.
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That is why experts suggest adding collagen supplements in your diet to make up for the decreasing collagen and to keep your body in good health. But how exactly is this wonder supplement made? Of course, the process his highly scientific, but the curiosity surrounding as to how it is made has always remained to a common consumer.
Today, we will be discussing the manufacturing of collagen on an industrial and scientific basis to develop a better understanding of where it comes from.
Collagen in itself is not a single substance but rather, a family of protein that is found in the connective tissues, muscles, bones, and skin of all animals in abundance. When collagen is used in the form of supplements (i.e. ingested from an outside source) the protein needs to be first broken down into hydrolyzed collagen (which is a polypeptide). It is hydrolyzed when denatured or gelatin collagen is subjected to the process of 'hydrolysis'. This makes it easier to be digested and absorbed by the body, this means it does not turn to gel while retaining its surface-active properties.
Processing of raw collagen to hydrolyzed collagen that is good for consumption involves the following steps:
· Demineralization.
· Extraction of collagen to form gelatin.
· Obtaining hydrolyzed collagen from enzymatic hydrolysis.
· Ion exchange.
· Filtration.
· Evaporation.
· Sterilization.
· Drying.
·
Hydrolyzed collagen is usually manufactured from the hydrolysis process of type 1 collagen (or its gelatin). Hydrolyzed collagen is a polypeptide composite that is manufactured from further hydrolysis of gelatin or denatured collagen.
This collagen can easily get dissolved in water and has no secondary displeasing taste. With hydrolyzed protein, very few bitter peptides are produced.
Bovine collagen is primarily harvested from bovine resources (cows and pigs). It is extracted from the hide of the animals which is made into a flavorless powder; other ingredients are added to it for taste. The obtained proteins are hydrolyzed to break them down into more easily digestible amino acids. The main constituents of collagen obtained from bovine resources include type 1 and 3 collagens.
Aside from bovine resources, type 1 collagen can also be obtained from marine resources. It is present in the skin and scales of fish. Marine collagen has additional benefits to it that vary from collagen obtained from bovine sources.
As type 1 and 3 are harvested from bovine and marine sources, type 2 collagen can be harvested from other animal sources that are beside the ones for type 1 and 3. Type 2 collagen is commonly derived from chicken sternum cartilage. Type 2 collagen is made differently from type 1 and 3 collagens.
Collagen-based on animal extracts has been rejected y vegans along with collagen made from cow and pig rejected by different people for religious and region-based reasons. That is why new alternatives are being discovered to manufacture collagen that will be accepted without prejudice.
· By chemical hydrolysis.
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· By enzymatic hydrolysis
Both methods are gaining traction on the industrial level due to feasibility and widespread acceptance without any judgment. But no matter the resources, consumption of collagen should be integrated into daily life to keep bones and muscles strong along with retaining a youthful glow in the skin.
Collagen is the most abundant protein in vertebrates and constitutes about 25% of vertebrate total proteins (Ogawa et al., ). To date, some 27 different types of collagen have been identified. Type I collagen occurs widely, primary in connective tissue such as skin, bone and tendons. Type II collagen occurs practically exclusively in cartilage tissue. Type III collagen is strongly dependent on age. For example, very young skin can contain up to 50%, but in the course of time is reduced 5-10%. The other collagen types are present in very low amounts only and are mostly organ-specific (Schrieber and Gareis, ). From that different kinds of collagen, type I collagen is the most widely occurring collagen in connective tissue. The collagen molecule is formed by three chains building a triple helix. The triple helical collagen molecule consists of about 1,000 glycine, 360 prolines and 300 hydroxyprolines (Gelita Group, ). Because of its spatial structure and high molecular weights, native collagen naturally insoluble in water. In order to be separated from the other constituents of animal tissues, it is made soluble through an extraction process which includes partial and controlled hydrolysis of the protein chain and then a warm water extraction. This yields hydrolysed collagen.
Normally, hydrolysed collagen is made by hydrolysis process of type I collagen or gelatine. Hydrolysed collagen is a polypeptide composite made by further hydrolysis of denatured collagen (Zhang et al., ) or gelatine. It is also called collagen hydrolysate, collagen peptide, hydrolysedgelatine or gelatinehydrolysate. The molecular weights of hydrolysed collagen are within the range of approximately 500-25 000 Da (Schrieber and Gareis, ). The hydrolysed collagen will dissolved in cold water and have no bitter taste due to the high glycine content of gelatine. During the manufacturer of hydrolysed collagen, very little bitter peptide is produced compared to the amount formed with other hydrolyzed proteins, so that it is more neutral in taste (Schrieber and Gareis, ).
The importance of hydrolysed collagen today cannot be denied since it is safe to be consumed by all human beings. The organoleptic characteristic of hydrolysed collagen makes it a suitable ingredient to be used in food, drinks and dietary supplements. Hydrolysed collagen has been broken down by hydrolysis process, so that it can be more easily digested when used in dietary supplements and food. It is also easy to be digested since it can be absorbed in small peptides in the blood (Iwai et al., ). For joint and bone health, it has been proven that the oral ingestion of 10 g of collagen hydrolysate daily decreases the joint pain (Moskowitz, ) and increases the bone mass density after 4-24 weeks (Nomura et al., ; Wu et al., ). Besides that, it is also widely used for weight management diet, nutraceuticals and cosmetics.
The objectives of this study are to briefly describe the process design, application and market demand, existing process technology, research and development work and potential future research development for the production of hydrolysed collagen.
APPLICATION AND MARKET DEMAND OF HYDROLYSED COLLAGEN
The principal technological property of hydrolysed collagen is its attractive molecular profile. This contributes to its wide range of application. The molecular profile is dependent on the raw materials and especially the manufacturing process used. By employing precisely controlled enzymatic hydrolysis, a product can be obtained with a mean molecular weight within a specified range (Schrieber and Gareis, ).
The demand for hydrolysed collagen has increased considerably in recent years, not only in Europe but also in United Stated and Asia. Hydrolysed collagen has become valuable ingredients in functional foods, pharmaceutical application, cosmetics and dietary food. With the advancement of science and technology, the application of hydrolysed collagen become broader, especially after its curative effect has been discovered (Huang et al., ). The various surface functionality of the hydrolysed collagen resulted in various applications within the food industry as shown in Table 1.
Collagen is a group of naturally occurring proteins found in animals, especially in the flesh and connective tissues of mammals. Thus it can be sourced out from pigs, cows, fish and chickens. In , the world Halal market for gelatin reached 278 300 tons; consisting of 42.4% from pig skin origin, 29.3% bovine hides, 27.6% bones and 0.7% from other sources (GEA, ). It is obvious that for gelatine industry, the major source of gelatine is from pig skin origin. Thus it can be correlated that the main source of hydrolysed collagen will also be the same because hydrolysed collagen is manufactured by using the same raw materials that are used for producing gelatine. Since Malaysia has positioned itself as one of the major producer of halal products, the market for hydrolysed collagen is tremendous not only in Malaysia but also in other parts of the world where halal hydrolysed collagen is urgently needed.
EXISTING PROCESS TECHNOLOGY AND RESEARCH and DEVELOPMENT WORK FOR PRODUCTION OF HYDROLYSED COLLAGEN
Hydrolysed collagen is manufactured using the same raw materials that are used for standard gelatine (Schrieber and Gareis, ) which is manufactured by denaturising and partial hydrolysis of the collagen. Usually, collagen and hydrolysed collagen have been produced from pig skin or bovine hide (Jia et al., ). However, outbreaks of mad cow disease and the banning of collagen from pig skin and bone in some regions for religious reasons have made it necessary to find a new marine or poultry source, that are safer and healthier for consumers.
Hydrolysed collagen can be obtained in two ways, by chemical hydrolysis or enzymatic hydrolysis. Although chemical hydrolysis is always used by a few manufacturers, enzymatic hydrolysis by protease is the preferred method because it is much better to control than chemical hydrolysis.
Table 1: Typical application areas for hydrolysed collagen (Schrieber and Gareis, )Hydrolysate could be manufactured directly from pure or nearly pure collagen. However, this is seldom done because collagen is very resistant. Collagen is resistant to most proteases and requires special collagenases for its enzymatic hydrolysis. This method probably is quite expensive. The collagenous domain is hardly digested by enzymes due to its stable triple helix but the denatured products such as gelatine are easily attacked by proteinase (Zhang et al., ). Frequently, a combination of enzymatic and chemical hydrolysis method is used. In a first step the manufacturer produces gelatine using chemical hydrolysis and then hydrolyzed with enzymes until the desired molecular weight is achieved (Schrieber and Gareis, ). Recently, the new method applied in order to produce hydrolysed collagen in less time is by using commercial gelatine as the raw material.
Enzymatic hydrolysis is widely applied to improve and upgrade the functional and nutritional properties of food proteins (Zhu et al., ). There are many classes of enzyme. For hydrolysis of gelatin into hydrolysed collagen, the suitable enzyme is protease class enzyme. Proteases from different sources are commonly used to obtain more selective hydrolysis since there are specific for peptide bonds adjacent to certain amino acid residues (Peterson and Johnson, ). This class of enzyme can hydrolyze the peptide bonds of proteins. Proteases sources are usually from animal, plant and microbial (Adler-Nissen, ). From previous study, a number of commercial proteases have been used for the production of hydrolysate, including trypsin, chymotrypsin, pepsin, pancreatin, bromelain, papain, alcalase, propase E, Neutrase, Flavourzyme and Protamex (Aleman et al., ; Huang et al., ; Jia et al., ; Lin and Li, ; Mendis et al., ; Yang et al., ). From all these commercial enzyme, Alcalase from microbial source, has been used in numerous studies dealing with hydrolysate because of its broad specificity as well as the high degree of hydrolysis that can be achieved in a relatively short time under moderate conditions (Benjakul and Morrissey, ).
Referring to Adler-Nissen (), any hydrolysis experiment carried out with a given substrate and a given enzyme is not adequately described unless at least the so-called hydrolysis parameters are specified. These hydrolysis parameters are substrate concentration, the enzyme-substrate ratio, pH and temperature. These four hydrolysis parameters are quite generally the primary determinants for how fast the enzyme reaction proceeds, as well as for other characteristic of the hydrolysis process. Figure 1 shows the overall process for production of hydrolysed collagen by using a combined method of chemical and enzymatic hydrolysis while Fig. 2 shows the overall process by using commercial gelatine as raw material for production of hydrolysed collagen.
The molecular weight of hydrolysed collagen is one of the most important factors in producing hydolysed collagen with desired functional properties. The process can also utilize advanced membrane filtration technique to fractionate the hydrolysed collagen molecules during the separation process. The use of membranes reduces the energy requirement with a possible saving of water through recycling.
Fig. 1: Overall process for production of hydrolysed collagen by using combined methodUse of ultrafiltration system could be a useful and industrially advantageous method for obtaining hydrolysate fractions with a desired molecular size (Gomez-Gullen et al., ). This system has been successfully applied in the fractionation and functional characterization of gelatin hydrolysates from squid or cobia skins (Lin and Li, ; Yang et al., ).
POTENTIAL FUTURE RESEARCH DEVELOPMENT
Batch reactors are conventionally used for enzymatic hydrolysis to produce hydrolysed collagen with pH and temperature controlled. However, batch reactors have some disadvantageous, such as low productivity because the enzyme is used only once, variability in product characteristics and quality due to batch-to-batch differences, the long times needed which also leads to low productivity, large space requirements and inability to obtain the final product instantly and continuously. The development of the Enzymatic Membrane Reactor (EMR) overcame many of these problems. The use of EMR will allow fractionation of hydrolysed collagen to obtain different fractions with different molecular weight distributions which will contribute to its wide range application.
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