Source Of Gelatin Research Articles

Preliminary Characterization on Physical Properties of Selected Marine Fish Skins as Alternative Sources of Halal Gelatin

Preliminary Characterization on Physical Properties of Selected Marine Fish Skins as Alternative Sources of Halal Gelatin

Extraction and Characterization of Gelatin from Bovine Lung

Gelatin is extracted from animal tissues using heat usually with low yields, but pepsin may increase high quality gelatin yield per unit of tissue. Gelatin from bovine lungs was extracted using heat and pepsin and the resulting gelatins were characterized. Pepsin increased gelatin yield by about 9-fold that of heat extraction alone. All bovine lung gelatin contained protein as the major proximate component, with little ash and non-detectable fat. Bovine lung gelatin had pH, moisture and protein comparable to or less than that of commercial bovine gelatin and decreased ash. Transmittance of bovine lung gelatin was substantially reduced compared to that of commercial bovine gelatin but had increased water and fat-binding capacity, and comparable or increased gelling and melting temperature. Gel strengths of bovine lung gelatin were comparable to or lower than and foam stability and emulsifying activity were lower than commercial bovine gelatin. Increased imino acid (proline and hydroxyproline) content was associated with increased gelling and melting temperatures and was comparable to commercial bovine gelatin. Heat-extracted bovine lung gelatin contained predominantly collagen γ– chains, β– chains and α– chains (α1(I) and α2(I)), with some low molecular weight peptides, while the pepsin-extracted lung gelatins were characterized by comparatively decreased β– and α– chains and increased low molecular weight peptides. The gel strength of heat-extracted bovine lung gelatin was higher than that of pepsin-extracted gelatins, indicating that additional yield was associated with reduced gelatin quality. Bovine lung is a potential source of gelatin for application in diversified industrial fields and use of pepsin is a viable method for extracting additional gelatin after heat extraction of high quality (increased gel strength) gelatin from bovine lung.

New acidic proteases from Liza aurata viscera: Characterization and application in gelatin production

The present study reports the extraction and characterisation of acidic protease from the viscera of golden grey mullet (LACAP), and its use in gelatin preparation. The optimum pH for the crude extract activity was 3.0, with high stability over a pH range from 3.0 to 7.0. The enzymatic extract lost about 79% of its activity by pepstatin A. Due to its high activity under acidic conditions, gelatin was extracted from the skin of L. aurata using different levels of LACAP (0, 5 and 10U/g of skin, named GGSG0, GGSG5 and GGSG10). The extraction yield of GGSG0 was only 3.3% and the addition of acidic proteases increased the yields, which reached 5% and 8.2% at 5 and 10U/g of skin, respectively. In addition, Fourier transform infrared (FT-IR) and SDS-page profiles of gelatins indicated that the structure was affected by enzymatic pre-treatment. The results of functional properties showed that the emulsion stability and activity indexes (ESI and EAI) of GGSG0 were higher than those of GGSG5 and GGSG10. Furthermore, foam expansion (FE) and foam stability (FS) increased as the concentration of gelatin increased. The results showed that L. aurata by-products can be a potential source of gelatin and protease.

Alterations in juvenile diploid and triploid African catfish skin gelatin yield and amino acid composition: Effects of chlorpyrifos and butachlor exposures

Skin is a major by-product of the fisheries and aquaculture industries and is a valuable source of gelatin. This study examined the effect of triploidization on gelatin yield and proximate composition of the skin of African catfish (Clarias gariepinus). We further investigated the effects of two commonly used pesticides, chlorpyrifos (CPF) and butachlor (BUC), on the skin gelatin yield and amino acid composition in juvenile full-sibling diploid and triploid African catfish. In two separate experiments, diploid and triploid C. gariepinus were exposed for 21 days to graded CPF [mean measured: 10, 16, or 31 μg/L] or BUC concentrations [Mean measured: 22, 44, or 60 μg/L]. No differences in skin gelatin yield, amino acid or proximate compositions were observed between diploid and triploid control groups. None of the pesticide treatments affected the measured parameters in diploid fish. In triploids, however, gelatin yield was affected by CPF treatments while amino acid composition remained unchanged. Butachlor treatments did not alter any of the measured variables in triploid fish. To our knowledge, this study is the first to investigate changes in the skin gelatin yield and amino acid composition in any animal as a response to polyploidization and/or contaminant exposure.

Comparison of oil yield and quality obtained by different extraction procedures from salmon (Salmo salar) processing byproducts

The content and composition of lipids in different byproducts (skins, heads, and backbones) from mechanically processed farmed Atlantic salmon were determined and compared with that obtained from wild salmon. Three different procedures were used to establish the optimal conditions of oil extraction (at high temperature −95°C, “cold” extraction at temperature not exceeding 15°C and enzyme assisted with Alcalase). “Cold” extraction at temperature not exceeding 15°C was very efficient, yielding almost 95% of the oil from skins. In the case of heads the obtained yield of about 71% was not lower than that from extraction performed at 95 °C or extraction supported by enzyme treatment. The peroxide value of oil isolated from the heads using “cold” extraction was at the same level as in oil of the enzyme assisted process, but four times lower than in oil extracted at high temperature. The results showed that the content of lipids from in the farmed salmon byproducts the content of lipids was about 45–55% higher than in byproducts of wild salmon, however the EPA + DHA content was 10–33% lower.Practical applications: With “cold” extraction heating which is commonly used for oil recovery in the fish industry could be eliminated and thus the cost of the process would be lower and oxidative changes in the oil reduced. Furthermore, this method based on rules of “green chemistry” can be more attractive and alternative procedure of oil isolation from fatty fish byproducts than those using organic solvents. The fatty fish byproducts such as heads, skins, and backbones may be used as a source of valuable oils rich in PUFA. The remaining material after oil isolation can be a source of collagen and gelatin used in the food, pharmaceutical, and cosmetic industries and finally of minerals preparation (in the case of heads and backbones) used for enriching animal feed.The oil was extracted from salmon byproducts: heads, backbones, and skins by using different methods. Conventional extraction of the oil at high temperatures ensures high yield but leads to low quality of the product. Enzymatic extraction is more preserving to oils rich in polyunsaturated fatty acids, but has special requirements. An attractive solution can be the “cold” extraction. This procedure allows achieving the oil from fatty fish byproducts with high yield and quality in a simple and cheap way.

Effects of Pre-Treatment Durations on Properties of Black Tilapia <i>(Oreochromis mossambicus)</i> Skin Gelatin

Black tilapia (Oreochromis mossambicus) fish skins are good alternatives sources of gelatin. Vast variations in extraction procedures affect the properties of fish gelatin such as yield and gel strength. Thus, this study explores the effect of pretreatment durations on the properties of black tilapia skin gelatin. Gelling properties such as gel strength (bloom value) of the gelatin samples had been determined. Highest gel strength had been detected for gelatin treated at 24 h (390.1 g), followed by 16 h (287.1 g) and 8 h (141.2 g). In contrast, gelatin treated at 24 h indicates lower yield on wet weight basis (14.12 %) than those treated at 16 h (14.96 %) and 8 h (16.90 %). The possible interactions and characteristics between the functional groups in the gelatin samples have also been perceived via Fourier Transform Infrared Spectroscopy (FTIR) analysis.

Identification of bioactive peptide from Oreochromis niloticus skin gelatin.

Fish skin, one type of wastes generated from Nile tilapia processing, is still a good source of collagen and gelatin. Bioactive peptides can be obtained from Nile tilapia skin gelatin by trypsin digestion. Trypsin hydrolysate was subsequently purified by gel filtration chromatography. Trypsin A fraction showed the greatest reducing power (5.138±1.060μM trolox/mg peptide) among all hydrolysate fractions, while trypsin B fraction from gel filtration column was found to exhibit the best radical scavenging and angiotensin-I-converting enzyme (ACE) inhibitory activities 8.16±2.18μg trolox/mg peptide and 59.32±9.97% inhibition, respectively. The most active fraction was subjected to MALDI-TOF/TOF MS/MS. After annotation by Mascot sequence matching software (Matrix Science) with Ludwig NR Database, two peptide sequences were identified; GPEGPAGAR (MW 810.87Da) and GETGPAGPAGAAGPAGPR (MW 1490.61Da). The docking analysis suggested that the shape of the shorter peptide may be slightly more proper, to fit into the binding cleft of the ACE. However, the binding affinities calculated from the docking showed no significant difference between the two peptides. In good agreement with the in silico data, results from the in vitro ACE inhibitory activity with synthetic peptides also showed no significant difference. Both peptides are thus interesting novel candidates suitable for further development as ACE inhibitory and antioxidant agents from the natural source.

Behaviorally-selective chemoreceptor lesions reveal two different chemically mediated orientation strategies in the rusty crayfish, Orconectes rusticus

Information from environmental stimuli is essential for animals to make behaviorally and ecologically relevant decisions. We sought to determine by studying Orconectes rusticus (Girard, 1852), the relative importance of mechanical and chemical information during orientation of crayfish to food and the type of orientation strategy crayfish employ to locate attractive odor sources. This was achieved through selectively lesioning chemoreceptors, leaving mechanoreceptors intact. Chemoreceptors were lesioned by placing the olfactory appendages in 50 ppt saltwater for two hours, then a deionized water bath for 10 minutes. Crayfish were subsequently used in orientation trials with a food source of fish gelatin. Orientation videos were digitized and orientation parameters (walking speed, heading angles and turning angles) were analyzed at a population level using a polynomial regression to determine how parameters changed as a function of distance from source and experimental treatment. Through the lesioning of chemoreceptors, we determined whether crayfish were orienting using chemotaxis or odor-gated rheotaxis. Lesioned crayfish oriented to the source with significantly decreased upstream heading angles compared to controls. Regression analysis revealed that lesioned crayfish had significantly altered orientation parameters demonstrating a change in orientation strategy. Results suggest that intact crayfish are using chemical information to guide search behavior while lesioned crayfish are performing a rheotactic-type of search.

Effects of Pre-Treatment Conditions on Black Tilapia Fish Scales for Gelatin Extraction

Black tilapia (Oreochromis mossambicus) fish scales are good sources of gelatin. Fish scales needs to undergo adequate demineralization (pre-treatment) process in order to be a suitable medium for gelatin extraction. The effect of hydrochloric acid (HCl) concentrations (1-5 %) and pre-treatment time (4-20 h) on the raw tilapia scales have been determined. Scanning Electron Microscopy (SEM) analysis was done on the raw scales before and after pre-treatment process. SEM images reveal the pattern of ridges on the scales that fades away at different treatment conditions. Energy Dispersive X-ray Spectroscopy (EDX) results indicate that 3% of HCl with 12 h of treatment time is adequate for demineralization of the fish scales. These were further proved by Fourier Transform Infrared Spectroscopy (FTIR) analysis, where no any inorganic components been detected in the pre-treated scales in comparison to raw scales.

Aplikasi Metode SDS-PAGE (Sodium Dodecyl Sulphate Poly Acrylamide Gel Electrophoresis) untuk Mengidentifikasi Sumber Asal Gelatin pada Kapsul Keras

Gelatin as the main ingredient of capsules is still a problem for a moslem. Most of gelatin production remains largely derived from non-halal materials. One of gelatin source is came from collagen of the skin and bones of bovine or pork. The main of study is determine the source of gelatin used in hard capsules by using SDS-PAGE (Sodium Dodecyl Sulphate Gel electrophoresis Poly Acrylamide) method. In the early stages, optimization of standards bovine and pork gelatin were hydrolyzed by pepsin at pH 4.5 and 60°C for 1 hour, 2 hours, and 3 hours. Gelatin hydrolyzateswere analyzed by SDS-PAGE to determine the optimal hydrolysis time. Identification of gelatin hydrolyzate fragments were carried by molecular weight. Hydrolysis time optimization throught applied to identify the source of hard gelatin capsules in the samples obtained from market and compared with the simulation of hard gelatin capsules. The results showed there were of specific bands of bovine gelatin with a molecular weight of 11,4 kDa; 34 kDa; 47kDa and specific bands of pork gelatin with a molecular weight of 24.7 kDa; 28 kDa; and 60 kDa. Similar results were obtained on a sample of hard capsules with bands of protein fragments that were identical to bovine gelatinstandard. Based on the results,each of the samples were tested contain of bovine gelatin respectively. DOI :http://dx.doi.org/10.15408/jkv.v0i0.3150

Pulsed electromembrane extraction for analysis of derivatized amino acids: A powerful technique for determination of animal source of gelatin samples

Differentiation of animal sources of gelatin is required for many reasons such as some anxieties about bovine spongiform encephalopathy or a ban on consuming porcine gelatin in some religions. In the present work, an efficient method is introduced for determination of animal origin of gelatin samples. The basis of this procedure is the application of pulsed electric field for extraction, preconcentration, and analysis of derivatized amino acids in gelatin. To this end, after derivatization of amino acids of interest by means of o-phthalaldehyde (OPA) for enhancing their ultraviolet (UV) absorbance as well as increasing their lipophilicities, a 137V electric field was applied for 20min with 10min−1 frequency to make the analytes migrate through a 200µm organic liquid membrane into an aqueous acceptor phase. Finally, the acceptor phase was analyzed by HPLC-UV. The proposed technique offered a high efficiency for analysis of amino acids, regarding 43% and 79% as extraction recoveries and 25ngmL−1 and 50ngmL−1 as limits of detection (LODs) for asparagine and glutamine, respectively. Therefore, due to sample cleanup ability of the proposed method and obtained preconcentration factors (29 and 53 for asparagine and glutamine, respectively), it could be carried out for differentiation of animal origins of gelatin samples, even if only small amounts of samples are available or in complicated media of foodstuffs and medicament.

Structural Characteristics of Tilapia (Oreochromis mossambicus) Bone Gelatin: Effects of Different Liming Methods

Fish bone is a good source of gelatin. In this study, gelatins were prepared from tilapia bone after the bone was pretreated with alkali protease, desalted immediately by 0.6 mol L−1 HCl, and hydrolyzed by papain or limed by Ca(OH)2. Gelatins extracted from papain-treated tilapia bone exhibited space structures similar to those of alkali-treated tilapia bone. Despite this similarity, many differences were observed between these gelatin samples. Compared with alkali-treated gelatin, papain-treated gelatins showed higher values for imino residue content, molecular weight proportion, bloom strength, and viscosity. The bloom strengths of the second and third papain-treated gelatins were 163 and 94 bloom, respectively, which were lower than the bloom strength of the first papain-treated gelatin (189 bloom). The viscosities of the three papain-treated gelatin samples were 4.18, 2.81, and 0.51 mPa.s−1. The first papain-treated gelatin achieved the highest gelling (16 °C) and melting points (23.9 °C). The yields of the first (5.40%) and second (6.71%) papain-treated gelatins were higher than those of the alkali-treated gelatins (3.33 and 5.76%, respectively). However, the yield of the third papain-treated gelatin (2.27%) was lower than that of the third alkali-treated gelatin (5.42%). More importantly, papain hydrolysis can prevent destruction by Ca(OH)2 in the bone structure and effectively reduce the denaturation temperature of tilapia bone collagen. Moreover, papain hydrolysis can dramatically reduce the time required for liming (0.8% of traditional liming process spent). Papain hydrolysis is a clean production method that can replace traditional liming.

Biomedical and Pharmaceutical Application of Fish Collagen and Gelatin: A Review

In last decade, more research has been conducted in order to find the better way for utilizing the wastes product generated from food processing industries. The increasing demand of industrial by-products is one of the main reasons for the conversion of these wastes into valuable products. Among the different valuable products from the waste, the extraction of collagen and gelatin could be a better way of utilizing the wastes, due to their effective applications in biomedical and pharmaceutical industries. The most abundant source of collagen and gelatin are land-based animals, such as cow and pig. However, the extraction of collagen and gelatin from non-mammalian sources such as fish has been high influences in current society due to some religious and disease transmission issues. Many studies have dealt with the extraction and functional properties of collagen and gelatin from fish wastes. The present work is a compilation of information on biomedical and pharmaceutical application of collagen and gelatin from fish processing wastes.

Sea bream bones and scales as a source of gelatin and ACE inhibitory peptides

Sea bream scales and bones were used as sources of gelatin. Scales gave a higher gelatin yield than bones pretreated with HCl or Alcalase. Demineralization with EDTA was effective especially in the case of scale gelatin that showed the lowest ash content. The pretreatment of bones with HCl led to an increase in the removal of minerals. The gel strength and viscoelastic properties of sea bream scale gelatins were higher than those of bone gelatins, and only slight differences were found between gelatin extracted from bones pretreated with HCl or Alcalase, although the amino acid profile was similar in the three gelatins. The gel strength of scale gelatins was higher than that of a commercial bovine gelatin used for comparative purpose (Bloom 200–220). When the scales gelatin was hydrolyzed with Esperase, a high ACE-inhibitory activity was found in the peptide fraction below 3 kDa, and the amount of this peptide fraction required to inhibit 50% of the ACE activity (IC50) was around 60 μg/mL.

Characterization of the gelatin of the flying gurnard (Dactylopterus volitans) and its interaction with starch

Gelatin extracted from the skin of the flying gurnard (Dactylopterus volitans L,) was characterised and its interaction with cassava starch mixtures of different ratio concentrations was investigated by rheology and differential scanning calorimetry (DSC). Protein and moisture were the main proximate composition, whilst glycine was the main amino acid. The gelatin had high bloom (275 g) strength with high imino acids, proline and hydroxyproline, content of 217/1000 residues. Gelation temperatures increased as more starch is used in the mixtures, ranging from 19.0°C for gelatin to starch ratio 4:1 to 70.1°C for mixture 1:4. Inclusion of cassava starch also increased the elastic modulus of the gelatin phase. Therefore, gelatin from flying gurnard skin has a potential to serve as an alternative source of non-bovine or porcine gelatin for food applications.

Optimisation of gelatin extraction from Unicorn leatherjacket (Aluterus monoceros) skin waste: response surface approach.

Physical properties of gelatin extracted from Unicorn leatherjacket (Aluterus monoceros) skin, which is generated as a waste from fish processing industries, were optimised using Response Surface Methodology (RSM). A Box-Behnken design was used to study the combined effects of three independent variables, namely phosphoric acid (H3PO4) concentration (0.15-0.25M), extraction temperature (40-50°C) and extraction time (4-12h) on different responses like yield, gel strength and melting point of gelatin. The optimum conditions derived by RSM for the yield (10.58%) were 0.2M H3PO4 for 9.01h of extraction time and hot water extraction of 45.83°C. The maximum achieved gel strength and melting point was 138.54g and 22.61°C respectively. Extraction time was found to be most influencing variable and had a positive coefficient on yield and negative coefficient on gel strength and melting point. The results indicated that Unicorn leatherjacket skins can be a source of gelatin having mild gel strength and melting point.

Effects of Various Extraction Methods on Quality Characteristics of Duck Feet Gelatin

We determined the optimum pretreatment conditions such as pH and time for swelling duck feet and investigated the effects of the extracting method, such as water bath (WB), pressure cooker (PC), and microwave oven (MO), on quality characteristics of the duck feet gelatin for improving utilization of duck feet as a novel source of gelatin. The soaking solution of pH 1 among pH 1-14 with unit intervals was selected due to the highest yield. The quality characteristics of the gelatin tested were color, pH, gel strength, viscosity, and melting point. For the extracted gelatin with different methods, the CIE L*, a* and b* values were in the following order: MO>PC>WB (p PC>MO (p MO>WB (p 0.05). The quality characteristic of duck feet gelatin was affected by extracting methods, and MO extraction can be one of the effective methods for duck feet gelatin.

A comparative study on the physical, chemical and functional properties of carp skin and mammalian gelatins.

Carp species forms the bulk of the aquaculture production in India and studies have shown that the filleting waste of these species, particularly skin can be a good source of gelatin. This study is a comparison of the gelatins from these unexploited sources with that of mammalian gelatins to get a better understanding of their physicochemical and functional properties with respect to mammalian gelatins. The study showed that mammalian gelatins had significantly superior physical properties viz., higher viscosity, melting & setting temperature and faster setting time. The odour scores were significantly higher (P < 0.05) for bovine and porcine skin gelatins (3.1-3.12), indicating that they had a distinguishable odour and hence can be considered as inferior to fish skin gelatins in organoleptic qualities. The gel strengths of rohu and common carp skin gelatins were significantly lower than mammalian gelatins. Among the carp skin gelatins, grass carp skin gelatin was found to have better compatibility with gelatin from bovine and porcine skins.

Analytical Methods for Gelatin Differentiation from Bovine and Porcine Origins and Food Products

Usage of gelatin in food products has been widely debated for several years, which is about the source of gelatin that has been used, religion, and health. As an impact, various analytical methods have been introduced and developed to differentiate gelatin whether it is made from porcine or bovine sources. The analytical methods comprise a diverse range of equipment and techniques including spectroscopy, chemical precipitation, chromatography, and immunochemical. Each technique can differentiate gelatins for certain extent with advantages and limitations. This review is focused on overview of the analytical methods available for differentiation of bovine and porcine gelatin and gelatin in food products so that new method development can be established.

Functional characteristics of gelatin extracted from skin and bone of Tiger-toothed croaker (Otolithes ruber) and Pink perch (Nemipterus japonicus)

The utilization of waste from fish processing industry for production of value added products has attracted substantial attention. Tiger-toothed croaker (Otolithes ruber) and Pink perch (Nemipterus japonicus) are used for surimi production and have the potential of abundant supply of raw skins and bones. In order to evaluate the waste from Tiger-toothed croaker and Pink perch as a source of gelatin, the gelatin was extracted from skin and bones and its rheological and functional properties were examined. The skins of Tiger-toothed croaker and Pink perch yielded 7.56% and 5.57% gelatin, whereas their bones yielded 4.57% and 3.55% respectively indicating skin as an important source for gelatin production. The gel strength of gelatins from the skins and bones of Tiger-toothed croaker (170g and 140g respectively) were found higher than Pink perch skin and bone gelatins (150g and 130g respectively). Similarly, the viscosity, melting point, emulsifying capacity and stability, foaming capacity and stability, and water holding capacity of gelatin extracted from Tiger-toothed croaker were in general greater than those of the gelatin from Pink perch and the values of skin gelatin were higher compared to bone gelatin in both the species. Hydroxyproline contents in skin and bone of Tiger-toothed croaker were 7.77 and 7.51mg/g and in Pink perch they were 7.63 and 7.41mg/g respectively. It can be concluded from the present study that Tiger-toothed croaker skin is a prospective source to produce gelatin in good yield with desirable functional properties comparable to commercially available mammalian gelatins.