Journal articles on the topic 'Gelatin'
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1
Charoenchokpanich, Wiriya, Pratchaya Muangrod, Sittiruk Roytrakul, Vilai Rungsardthong, Savitri Vatanyoopaisarn, Benjamaporn Wonganu, and Benjawan Thumthanaruk. "Influence of extraction times on physical and functional properties of gelatin from salted jellyfish by-products." E3S Web of Conferences 355 (2022): 02014. http://dx.doi.org/10.1051/e3sconf/202235502014.
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By-products of the marine industry have gained attention for producing valuable food ingredients like gelatin, which might benefit food applications and decrease food waste. Gelatin is the only protein-based food hydrocolloid, mainly used for gelling, viscosity, or emulsifying in the food industry. So far, a number of researchers have reported that by-products of salted jellyfish can produce jellyfish gelatin. The quality of jellyfish gelatin gel depends on several factors including hydrochloric acid pretreatment, extraction temperature, and extraction time. However, the functional properties such as foaming and emulsifying of jellyfish gelatin are not well understood. This research was aimed at investigating the hydrochloric acid pretreatment effect of extraction times (12, 24, and 48 h) at 60 °C on the resulting gelatin's yield, physical, and functional properties. Results showed that jellyfish gelatin's yield, gel strength, and viscosity significantly increased with increasing extraction times. Jellyfish gelatin yields were 2.74-14.07%. The gel strength of jellyfish gelatin extracted for 48 h (325.97±2.84 g) was higher than that of jellyfish gelatins extracted for 12 h (210.46±3.97 g) and 24 h (261.60±3.25 g). All jellyfish gelatins can form gels at 4 °C. Viscosity values of jellyfish gelatin were 23.00-24.50 centipoise. The foaming capacity and foaming stability of jellyfish gelatin were 12.28-17.54% and 10.52-15.78%, respectively. The emulsification activity index of jellyfish gelatin was 13.11-13.30 m2/g, and the emulsification stability index was 39.19-56.42%. As a result, varied gelatin extraction periods influenced jellyfish gelatin's physical and functional properties, indicating that the extended extraction time of 48 h delivered the jellyfish gelatin that can be used as a foaming and emulsifying agent. Therefore, turning the jellyfish by-products into food ingredients like gelatin would increase product values and potential uses in the food and medical applications.
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Li, Yi, Yunchao Xiao, Man Xi, Guibin Li, and Yang Jiang. "One-Step Preparation of Adhesive Composite Hydrogels through Fast and Simultaneous In Situ Formation of Silver Nanoparticles and Crosslinking." Gels 8, no. 5 (April 21, 2022): 256. http://dx.doi.org/10.3390/gels8050256.
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In this study, a series of gelatin/silver nanoparticles (AgNPs) composite hydrogels are prepared for the first time through the facile in situ formation of AgNPs. AgNPs, which are formed by reducing Ag+ using dopamine-conjugated gelatins. These can simultaneously crosslink gelatin molecules, thus generating three-dimentional and porous hydrogels. The gelation time and pore sizes of these composite hydrogels can be controlled by controlling the feeding concentration of AgNO3 and weight content of gelatin in water, respectively. The feeding concentration of AgNO3 also has an effect on the equilibrium swelling ratio of the hydrogels. Moreover, these composite hydrogels, with a controllable gelation time and in situ forming ability, exhibit good adhesive properties and can be used as drug-release depots.
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Padilla, Cristina, Franck Quero, Marzena Pępczyńska, Paulo Díaz-Calderon, Juan Pablo Acevedo, Nicholas Byres, Jonny J. Blaker, William MacNaughtan, Huw E. L. Williams, and Javier Enrione. "Understanding the Molecular Conformation and Viscoelasticity of Low Sol-Gel Transition Temperature Gelatin Methacryloyl Suspensions." International Journal of Molecular Sciences 24, no. 8 (April 19, 2023): 7489. http://dx.doi.org/10.3390/ijms24087489.
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For biomedical applications, gelatin is usually modified with methacryloyl groups to obtain gelatin methacryloyl (GelMA), which can be crosslinked by a radical reaction induced by low wavelength light to form mechanically stable hydrogels. The potential of GelMA hydrogels for tissue engineering has been well established, however, one of the main disadvantages of mammalian-origin gelatins is that their sol-gel transitions are close to room temperature, resulting in significant variations in viscosity that can be a problem for biofabrication applications. For these applications, cold-water fish-derived gelatins, such as salmon gelatin, are a good alternative due to their lower viscosity, viscoelastic and mechanical properties, as well as lower sol-gel transition temperatures, when compared with mammalian gelatins. However, information regarding GelMA (with special focus on salmon GelMA as a model for cold-water species) molecular conformation and the effect of pH prior to crosslinking, which is key for fabrication purposes since it will determine final hydrogel’s structure, remains scarce. The aim of this work is to characterize salmon gelatin (SGel) and salmon methacryloyl gelatin (SGelMA) molecular configuration at two different acidic pHs (3.6 and 4.8) and to compare them to commercial porcine gelatin (PGel) and methacryloyl porcine gelatin (PGelMA), usually used for biomedical applications. Specifically, we evaluated gelatin and GelMA samples’ molecular weight, isoelectric point (IEP), their molecular configuration by circular dichroism (CD), and determined their rheological and thermophysical properties. Results showed that functionalization affected gelatin molecular weight and IEP. Additionally, functionalization and pH affected gelatin molecular structure and rheological and thermal properties. Interestingly, the SGel and SGelMA molecular structure was more sensitive to pH changes, showing differences in gelation temperatures and triple helix formation than PGelMA. This work suggests that SGelMA presents high tunability as a biomaterial for biofabrication, highlighting the importance of a proper GelMA molecular configuration characterization prior to hydrogel fabrication.
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Reza, Muhammad, and Devi Annissa. "Fish-based gelatin: exploring a sustainable and halal alternative." Journal of Halal Science and Research 4, no. 2 (September 29, 2023): 55–67. http://dx.doi.org/10.12928/jhsr.v4i2.8596.
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Gelatin derived from fish has emerged as a promising alternative to traditional gelatin derived from mammals, primarily due to its potential to meet the rising demand for halal-certified products. This article provides a comprehensive overview of the utilization and extraction of gelatin derived from fish as a halal-compliant substitute. This study gathered information regarding the source, extraction method, and contribution to physicochemical properties and applications by reviewing the relevant literature. It discusses the most frequently consumed fish species, such as tilapia, mackerel, and catfish, which are halal and possess outstanding gel-forming properties. Type A gelatine (pre-treated acid) is distinguished from type B gelatine (pre-treated alkaline) based on the solvent used for pre-treatment. Seventy-five percent of the twenty gelatin extraction studies utilized alkaline pre-treatment (i.e., NaOH), where the base solution can eliminate non-collagen from the skin or bone of fish, thereby obtaining pure collagen. All extraction processes are conducted using the hot water extraction method at temperatures ranging from 45 to 70 °C. This method is time-efficient, accelerates collagen decomposition and gelatin solubility, and increases gelatin yield (from 5.33 to 68.75%). The effects of various procedures, including acid and alkaline extraction, on gelatin gel strength, moisture content, ash content, protein content, and fat content are investigated. According to SNI, gelatine has a gel strength between 50 and 300, a moisture content that does not exceed 16%, a lipid content that does not exceed 5%, and an average protein content that does not exceed 87.65%. However, ash concentrations typically persist above 3.25%, presumably due to using bases in pre-treatment processes that do not perfectly dissolve minerals compared to acids. In conclusion, the source and method of extraction will impact the gelatin's characteristics and applications. Keywords: Gelatin, Fish-based gelatin, Physicochemical properties, Traditional gelatin, SNI
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Takahashi, Kazuhiro, Tomoaki Takamoto, and Yasuhiko Tabata. "Preparation of Gelatin Grafted with Lactic Acid Oligomers." Key Engineering Materials 288-289 (June 2005): 441–44. http://dx.doi.org/10.4028/www.scientific.net/kem.288-289.441.
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The objective of this study is to synthesize gelatins grafted with lactic acid oligomer (LAo) and lactic acid oligomer-poly(ethylene glycol)-lactic acid oligomer (LAo-PEG-LAo) triblock copolymers and to examine their gelation behavior. The grafting ratio of LAo-grafted gelatins could be changed by the feed ratio of LAo to the amino groups of gelatin for grafting reaction, while triblock copolymers with different molecular weights of LAo were prepared. The turbidity of LAo-grafted gelatin solution increased with the increased grafting ratio, although the turbidity increase was suppressed by adding guanidine hydrochloride in a dose-dependent manner. The turbidity of LAo-grafted gelatin solution further enhanced by mixing with the solution of triblock copolymers, while the enhanced extent increased with an increase in the LAo molecular weight. A mechanically firm hydrogel was formed by mixing the LAo-grafted gelatin and triblock copolymer at the higher solution concentrations, while the compression strength of the hydrogel became higher as the grafting ratio increased. No hydrogel formation was observed in the presence of guanidine hydrochloride.
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Sugihartono, Sugihartono. "Kemampuan Gelatin Kulit Ikan Menggantikan Gelatin Mamalia Berdasarkan Sifat Fisika-Kimianya untuk Industri Pangan." Jurnal Riset Teknologi Industri 8, no. 16 (August 21, 2016): 156–67. http://dx.doi.org/10.26578/jrti.v8i16.1631.
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The major source of gelatin in the world is derived from pigskin, bovine hide and also pigs and cattle bone, of which 29,4% from bovine hides, 46% from pigskin, 23,1% from bones, and 1,5 % from others. Fish gelatin is one of the alternative sources of food gelatine, which can be accepted for various religious groups such as muslims, jews and hindus. The yield of gelatin from fish skin are varies, depending on the species and its processing method, able to match and even exceed the yield of mammalian gelatin. Physico-chemical properties of fish gelatin varies among species. Protein content of fish gelatin is lower than mammalian gelatin. The number of amino acids of fish gelatin and mammalian gelatin were similar, but defferent composition especially for glisine, proline and arginine. Fish gelatin melting point is lower than mammalian gelatin, some types of which has a gel strength and viscosity are able to match and even exceed the mammalian gelatine. Specifically of fish gelatine could replace the role of the mammalian gelatin as food gelatine, after considering suitability innate characteristic of fish gelatin for food product,ABSTRAKSumber Utama gelatin dunia berasal dari kulit dan tulang sapi serta babi; dimana dari kulit sapi (29,4%), kulit babi (46%), tulang (23,1%), dan sisanya dari bahan lain (1,5%). Gelatin dari kulit ikan merupakan salah satu sumber alternatif gelatin pangan, yang dapat diterima oleh berbagai kelompok religi, seperti muslim, jews dan hindu. Rendemen gelatin kulit ikan bervariasi, tergantung spesies dan cara pengolahannya, mampu menyamai dan bahkan melebihi rendemen gelatin mamalia. Sifat fisik-kimia gelatin ikan bervariasi diantara species ikan. Kandungan proteinnya lebih rendah dibanding protein gelatin mamalia. Jenis asam amino penyusun gelatin ikan mirip dengan gelatin mamalia, namun komposisinya berbeda terutama kandungan glisine, proline dan arginin. Titik leleh gelatin ikan lebih rendah, beberapa jenis diantaranya memiliki kekuatan gel dan viskositas yang mampu menyamai dan bahkan melebihi gelatin mamalia. Secara spesifik gelatin ikan mampu menggantikan peran gelatin mamalia sebagai gelatin pangan setelah mempertimbangkan karakteristik innate dari gelatin ikan dengan kesesuaian produk pangan. Kata kunci : gelatin, ikan, mamalia, pangan
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Gaidau, Carmen, Maria Râpă, Gabriela Ionita, Ioana Rodica Stanculescu, Traian Zaharescu, Rodica-Roxana Constantinescu, Andrada Lazea-Stoyanova, and Maria Stanca. "The Influence of Gamma Radiation on Different Gelatin Nanofibers and Gelatins." Gels 10, no. 4 (March 26, 2024): 226. http://dx.doi.org/10.3390/gels10040226.
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Gelatin nanofibers are known as wound-healing biomaterials due to their high biocompatible, biodegradable, and non-antigenic properties compared to synthetic-polymer-fabricated nanofibers. The influence of gamma radiation doses on the structure of gelatin nanofiber dressings compared to gelatin of their origin is little known, although it is very important for the production of stable bioactive products. Different-origin gelatins were extracted from bovine and donkey hides, rabbit skins, and fish scales and used for fabrication of nanofibers through electrospinning of gelatin solutions in acetic acid. Nanofibers with sizes ranging from 73.50 nm to 230.46 nm were successfully prepared, thus showing the potential of different-origin gelatin by-products valorization as a lower-cost alternative to native collagen. The gelatin nanofibers together with their origin gelatins were treated with 10, 20, and 25 kGy gamma radiation doses and investigated for their structural stability through chemiluminescence and FTIR spectroscopy. Chemiluminescence analysis showed a stable behavior of gelatin nanofibers and gelatins up to 200 °C and increased chemiluminescent emission intensities for nanofibers treated with gamma radiation, at temperatures above 200 °C, compared to irradiated gelatins and non-irradiated nanofibers and gelatins. The electron paramagnetic (EPR) signals of DMPO adduct allowed for the identification of long-life HO● radicals only for bovine and donkey gelatin nanofibers treated with a 20 kGy gamma radiation dose. Microbial contamination with aerobic microorganisms, yeasts, filamentous fungi, Staphylococcus aureus, Escherichia coli, and Candida albicans of gelatin nanofibers treated with 10 kGy gamma radiation was under the limits required for pharmaceutical and topic formulations. Minor shifts of FTIR bands were observed at irradiation, indicating the preservation of secondary structure and stable properties of different-origin gelatin nanofibers.
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Yanar, Yasemen, and Mehmet Gökçin. "Uskumru (Scomber scombrus) ve Levrek (Dicentrarchus labrax ) Kemiklerinden Jelatin Ekstraksiyonu ve Karakterizasyonu." Turkish Journal of Agriculture - Food Science and Technology 4, no. 9 (September 15, 2016): 728. http://dx.doi.org/10.24925/turjaf.v4i9.728-733.776.
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The aims of this study were to determine the physicochemical properties of extracted gelatins from mackerel (Scomber scombrus) and sea bass (Dicentrarchus labrax) bones and compare with those of commercial fish and bovine gelatins. The yield of gelatin obtained from the bone of mackerel and sea bass were 5.98 and 6.20%, respectively. Two extracted gelatins showed higher protein content, lower moisture content compared to both commercial gelatins, indicates that the gelatin has considerably high purity. Melting temperatures of mackerel and sea bass bone gelatins were 25.5 and 23°C, respectively. Mackerel bone gelatin was yellow in appearance and higher L* value than both commercial gelatins. It can be concluded from the present study that mackerel and sea bass bone are a prospective source to produce gelatin in good yield with desirable functional properties comparable to commercially available mammalian and fish gelatins.
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Pichayakorn, Wiwat, Suchipha Wannaphatchaiyong, and Wanlapha Saisin. "Preparation Process and Properties of Crosslinked Gelatin Beads for Drug Loading." Advanced Materials Research 1060 (December 2014): 74–78. http://dx.doi.org/10.4028/www.scientific.net/amr.1060.74.
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This study aimed to develop the preparation process of stable gelatin beads for drug loading. Gelatin beads were prepared by either ionotropic gelation or emulsification techniques. Hardening of gelatin beads were done by both cooling and chemical treatments. For ionotropic gelation techniques, aqueous gelatin solution was continuously dropped into cool calcium chloride (CaCl2) or sodium tripolyphosphate (TPP) solution. However, the stable bead particles could not be formed. For emulsification techniques, water in oil (w/o) system was performed using aqueous gelatin solution as dispersed phase and cool soybean oil as dispersion medium, and glutaraldehyde (GAL) might also be used as chemical crosslinking agent. Gelatin type, amount of GAL, and crosslinking time slightly affected the characters of beads formation. Propranolol HCl could be loaded in gelatin beads.
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Jiang, Yu, Jun Yu, and Cheng Chu Liu. "Comparison of Physicochemical Properties of Gelatins Prepared from Different Fish Skins through Hot Water Extraction at Mild Temperature Condition." Advanced Materials Research 887-888 (February 2014): 557–61. http://dx.doi.org/10.4028/www.scientific.net/amr.887-888.557.
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Gelatins were prepared from tilapia, salmon and halibut skin through hot water extraction (60°C, 180 min) and their physiochemical properties were compared with commercial gelatins from porcine and bovine sources. Tilapia gelatin contained highest hydroxyproline content (8.45%) and had highest gel strength (376.6 g), followed by salmon gelatin. Halibut gelatin had the lowest hydroxyproline content (24.72% in average) and gel strength (47.56 g in average). Gelatin prepared from tilapia had much higher gel strength and viscosity than commercial pharmaceutical gelatins of porcine and bovine sources and showed a great potential to be utilized in pharmaceutical industry.
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Nuamsrinuan, Nisakorn, Noppadon Suttisiri, Ekachai Hoonnivathana, Pichet Limsuwan, and Kittisakchai Naemchanthara. "Characterization and Gel Properties of Gelatin Extracted from Waste Fish Scales." Applied Mechanics and Materials 804 (October 2015): 187–90. http://dx.doi.org/10.4028/www.scientific.net/amm.804.187.
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The objective of this research is to compare the characteristic of gelatin prepared from waste fish scales. White perch, java barb, red tilapia and nile tilapia scales were cleaned and treated with 1.0 M NaOHfor 2 h at room temperature to remove fat and then treated 0.8 M acetic acid to restructure of fish scales. Gelatin from waste fish scales were exacted using heating the cleaned fish scales in the distilled water at 70 °C for 2 h. Gelatins were characterization by UV-vis spectrometer, viscometer, X-ray diffraction (XRD), fourier transform infrared spectrophotometer (FT-IR) and scanning electron microscopy (SEM). The results shown the amount of gelatin and percent transmittance of light of gelatin from white perch was more than that of other waste fish scales. The viscosities of all gelatins decreased with increasing temperature. The gelatin from java bard was more viscosity than that from other fish scales due to more amounts of aspartic and glutamic acid. The XRD intensity of gelatin from white perch scales and java barb scales had higher than that from other fish scales confirming the higher crystallinity of gelatin. The FT-IR resultsindicated the same function groupsof all gelatins. SEM results revealed the porous structure of all gelatins. The all results concluded that gelatin property of nile tilapia scales had less than that of other fish scales which could be used in different industry.
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Bai, Yun, Shuai Peng, Yi Qun Huang, and Ke Qiang Lai. "Physicochemical and Rheological Properties of Gelatin Extracted from Tilapia (Oreochromis niloticus) Skin and Concentration Effect." Advanced Materials Research 941-944 (June 2014): 1128–32. http://dx.doi.org/10.4028/www.scientific.net/amr.941-944.1128.
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Tilapia skin gelatins were extracted with optimal acetic or citric acid concentrations which provide similar optimum protein yield (22g/100 wet weight), and rheological properties of gelatin solutions with various concentrations were measured and characterized. Commercial valued properties including bloom strength, gelling and melting point, viscosity were measured to compare the samples of the two gelatins. Liner viscoelastic range (LVR) of gelatin preparations with increasing concentration and decreasing temperature were determined. Temperature sweep was conducted for comparison and characterization the relationships between concentration and gelling/melting point of gelatin extracted by citric acid or acetic acid. The results showed that the melting and gelling point varying with concentration followed exponential curve (R2 as high as 0.99), and there were rarely molecular fractions in extracted gelatins. Elastic modulus (G′) of gelatin gels was mainly a function of cold temperature and time, while the discrepancy between the melting behaviors of gelatin extracted by two acids may stem from the composition and molecular weight of gelatin chains. In conclusion, the tilapia skin gelatin extracted in our study is of high qualities and rheological analysis is a critical tool for material of gelatin differentiation from varied molecular properties.
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Purwanti, Tutiek, Rico Andre Satriawan, and Dewi Melani Hariyadi. "The Effect of the Comparison of Sodium Alginate-Gelatin Levels on Microspheres Characteristics (Produced by Ionic Gelation Method Aerosolized Technique)." International Journal of Drug Delivery Technology 10, no. 02 (June 25, 2020): 301–6. http://dx.doi.org/10.25258/ijddt.10.2.19.
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The aim of this research is to investigate the effect of concentration ratio of sodium alginate-gelatin on the characteristics of microspheres. Microspheres were prepared with ionotropic gelation methods aerosolization technique with sodium alginate and gelatin as polymer matrixes, and calcium chloride (1.5 M) as the cross-linker, and then dried using freeze dryer. The concentration ratio of sodium alginate-gelatin that was used to make microsphere was divided into F1: 2.25:0.25%, F2: 1.75:0.75%, and F3: 1.25:1.25%. Resulting microspheres were characterized in terms of characteristics (yield, particle size, and swelling index). The result showed that there was an increase in yield and particle size, as sodium alginate concentration increased on formula. The statistical test showed the concentration ratio of sodium alginate-gelatine showed a significant meaning different from the yield and particle size. The swelling index shows that the swelling peak of microspheres became more quickly with increased sodium alginate concentration.
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Minami, M., K. Sakata, M. Takigami, T. Nagaoka, and T. Nakamura. "Ultrafiltration Pretreatment for 14C Dating of Fossil Bones from Archaeological Sites in Japan." Radiocarbon 55, no. 2 (2013): 481–90. http://dx.doi.org/10.1017/s0033822200057611.
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To study the effect of ultrafiltration on the radiocarbon ages of relatively poorly preserved bones in Japan, we analyzed the 14C dates of high-molecular-weight (HMW) gelatin samples and compared them with those of other extracted organic fractions, unfiltered gelatin samples extracted from NaOH-treated or NaOH-untreated collagen, and XAD-purified hydrolysates of animal fossil bones (∼4600 BP; gelatin yield of 2–4%) from the Awazu underwater archaeological site, Shiga, Japan. NaOH-treated, unfiltered gelatins and XAD-purified hydrolysates showed statistically similar 14C ages to those of HMW gelatins. The 14C ages of the HMW gelatins were the oldest and similar to those of wood collected from the same layer as the bones, and the NaOH-treated, unfiltered gelatins gave 14C ages within the acceptable margins of error; therefore, ultrafiltration was effective for accurate 14C dating, while NaOH-treated gelatin without ultrafiltration was also sufficient to obtain accurate 14C dates on the animal bones. The 14C ages of human skeletons (∼750 BP; gelatin yield of 2–11%) from 5 individuals excavated from an archaeological site in Yuigahama, Kamakura, Japan, showed statistically the same 14C ages as NaOH-treated, unfiltered gelatins and HMW gelatins within the margins of error, although HMW gelatins were likely to give slightly older ages than unfiltered gelatin with a yield of less than ∼3%. These results indicate that unfiltered gelatins extracted from fossil bones of gelatin yield more than ∼3% can produce accurate 14C ages without the need for ultrafiltration. Ten bone fragments from 3 humans showed the same 14C ages for each individual, suggesting that any bone part from an individual can be used to obtain a representative age. The 14C ages of tooth enamels of 2 individuals were 35 and 70 yr older than their bone ages. Death dates obtained from these age gaps agreed with those determined by morphology.
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Gaspar-Pintiliescu, Stefan, Anton, Berger, Matei, Negreanu-Pirjol, and Moldovan. "Physicochemical and Biological Properties of Gelatin Extracted from Marine Snail Rapana venosa." Marine Drugs 17, no. 10 (October 17, 2019): 589. http://dx.doi.org/10.3390/md17100589.
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In this study, we aimed to obtain gelatin from the marine snail Rapana venosa using acidic and enzymatic extraction methods and to characterize these natural products for cosmetic and pharmaceutical applications. Marine gelatins presented protein values and hydroxyproline content similar to those of commercial mammalian gelatin, but with higher melting temperatures. Their electrophoretic profile and Fourier transform infrared (FTIR) spectra revealed protein and absorption bands situated in the amide region, specific for gelatin molecule. Scanning electron microscopy (SEM) analysis showed significant differences in the structure of the lyophilized samples, depending on the type of gelatin. In vitro studies performed on human keratinocytes showed no cytotoxic effect of acid-extracted gelatin at all tested concentrations and moderate cytotoxicity of enzymatic extracted gelatin at concentrations higher than 0.5 mg/mL. Also, both marine gelatins favored keratinocyte cell adhesion. No irritant potential was recorded as the level of IL-1α and IL-6 proinflammatory cytokines released by HaCaT cells cultivated in the presence of marine gelatins was significantly reduced. Together, these data suggest that marine snails are an alternative source of gelatins with potential use in pharmaceutical and skincare products.
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Barman, Liton Chandra, Md Belal Hossain Sikder, Iftekhar Ahmad, Jahid Hasan Shourove, Shah Samiur Rashid, and Aizi Nor Mazila Ramli. "Gelatin Extraction from the Bangladeshi Pangas Catfish (Pangasius pangasius) Waste and Comparative Study of Their Physicochemical Properties with a Commercial Gelatin." International Journal of Engineering Technology and Sciences 7, no. 2 (April 19, 2021): 13–23. http://dx.doi.org/10.15282/10.15282/ijets.7.2.2020.1002.
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Abstract- Production of gelatin from the aquatic source is gradually replacing the mammalian sources because of some socio-cultural and religious issues. The Pangasius pangasius catfish is a native species and very popular in Bangladesh due to their availability and cheap price. The perspective of this study was to extract the gelatin from the skin and bones of this catfish and compare them with commercial gelatin. Gelatin was extracted by applying the acid-base extraction process and the resultant gelatins were evaluated based on some physical properties. The gelatin yield was found significantly higher from the skin sample (10.85±0.93%) than the bone (5.23±0.39%) of Pangasius. The extracted skin gelatin had higher moisture and fat content than the bone and Commercial gelatin, while the ash content was significantly higher in bone gelatin. Protein content was noted in skin gelatin (81.34±3.45%), bone gelatin (73.44±2.58%), Where commercial gelatin (92.38±3.89%). Skin gelatin exerted significantly higher (p<0.05) viscosity (4.62±0.3 mPa.s) than the extracted bone gelatin (3.11±.24 mPa.s) and lower than the commercial gelatin (5.76±0.34 mPa.s). The melting and setting temperature of this catfish skin and bone gelatin were very near to each other and significantly lower than the commercial gelatin. Skin gelatin had exerted higher water holding capacity (2.36±0.11 ml/g), fat binding capacity (3.23±0.05 ml/g), foaming capacity ratio (1.88±0.07), and foam stability (1.51±0.04). Both the skin and bone gelatins were acidic. In this comparative study, it was noticed that the skin gelatin had better physical properties than the bone gelatin of native Pangasius catfish. Pangasius skin may be recognized as a potential aquatic source of edible gelatin with good yield and desirable physical properties comparing with commercial gelatin.
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Chen, Xi Liang, and Qing Nan Shi. "Research on Sol-Gel Transition Process of Gelatin." Advanced Materials Research 683 (April 2013): 474–78. http://dx.doi.org/10.4028/www.scientific.net/amr.683.474.
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As a kind of functional material, gelatin gel is widely used in controlled drug release, biological tissue engineering, photographic and food industries. Plenty of studies on the gelatin gel have been carried out by researchers, which include gelation mechanisms, gelation kinetics, analysis on the crosslinked structure and macroscopic performance during the gelation process. Numerical simulation is a new method used in the study of gelatin sol-gel transition process, which can make up for the deficiency of the experimental research. E.g., the dynamic gelation process makes it difficult to measure the structural and performance parameters in time and space scales in experiments. However, these problems have been solved by numerical simulation method in our previous work. The experimental, theoretical and numerical simulation research on sol-gel transition of gelatin is reviewed, and the progress and difficulties in this field are discussed.
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Martin Torrejon, Virginia, Yanqiu Deng, Guidong Luo, Bingjie Wu, Jim Song, Song Hang, and Dongmei Wang. "Role of Sodium Dodecyl Sulfate in Tailoring the Rheological Properties of High-Strength Gelatin Hydrogels." Gels 7, no. 4 (December 16, 2021): 271. http://dx.doi.org/10.3390/gels7040271.
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Gelatin hydrogels are widely used materials that may require surfactants to adjust their solution’s surface tension for cell attachment, surface adsorption enhancement, or foaming. However, gelatin is a highly surface-active polymer, and its concentrated solutions usually do not require surfactants to achieve low surface tension. However, anionic surfactants, such as sodium dodecyl sulfate (SDS), interact strongly with gelatin to form complexes that impact its hydrogels’ rheological properties, influencing processability and functionality. Nevertheless, there is a lack of systematic research on the impact of these complexes on high gelatin content (i.e., high strength) hydrogels’ rheological properties. In this work, the SDS/gelatin ratio-dependent viscoelastic properties (e.g., gel strength, gelation kinetics, and melting/gelling temperature) of high-strength gelatin hydrogels were investigated using rheology and correlated to surface tension, viscometry, FTIR, and UV-Vis spectrophotometry. SDS–gelatin ratio was proved to be an important factor in tailoring the rheological properties of gelatin hydrogels. The gel strength, gelation kinetics, and melting/gelling temperature of the gelatin hydrogels linearly increased with SDS incorporation up to a maximum value, from which they started to decline. The findings of this work have wide applicability in tailoring the properties of gelatin–SDS solutions and hydrogels during their processing.
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Ab Rahim, Halimah, Hasan Ahmad, and Mohd Hasbi Ab Rahim. "Extraction of Gelatin from Different Parts of Gallus Gallus Domesticus." Current Science and Technology 1, no. 1 (May 12, 2021): 50–55. http://dx.doi.org/10.15282/cst.v1i1.6447.
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Gelatin is a mixture of protein obtained from animal parts (skin, bones, tendons, ligaments, and cartilages) by hydrolysis. Gelatin market demand is high especially in pharmaceutical, food, photographic, and cosmetics industries based on its gelling, foaming, and emulsifying properties. This preliminary study was focus on chicken head and feet gelatin extraction and their characterization in terms of percentage yield and physical properties (pH, color, melting point, and texture). Two different treatments (acid and alkali) were used. The percentage yield of chicken head (CHGac) and feet (CFGac) gelatins by using acid treatment were 32.10% and 33.65% while the chicken head (CHGal) and feet (CFGal) from alkali treatment were 20.06% and 22.18% respectively. All the gelatins indicated the same pH pattern range from 4.3 to 6.4. The melting point for gelatins from each treatment was a range from 30.4℃ to 35.9℃. The texture analysis is specifically into the gel strength of gelatin produce which ranges from 230 g to 356 g. All the gelatins also showed the same pattern of dl(lighter/darker), da(redder/greener), and db(yellower/bluer) which are positive value mean that the gelatins have lighter, redder and yellower color respectively. In conclusion, chicken head and feet can be an alternative that could replace the usage of porcine, bovine, and other mammals as a source of gelatin.
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Isseroff, Rebecca, Jerry Reyes, Roshan Reddy, Nicholas Williams, and Miriam Rafailovich. "The Effects of Graphene Oxide and Partially Reduced Graphene Oxide on the Enzymatic Activity of Microbial Transglutaminase in Gelatin." MRS Advances 4, no. 15 (2019): 879–87. http://dx.doi.org/10.1557/adv.2019.89.
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ABSTRACTA significant drawback of enzyme use in industrial applications is its lack of stability. Graphene oxide (GO) has previously been investigated for enzyme immobilization and enhancement of enzymatic catalysis. Microbial transglutaminase (MTG) is an enzyme that is used to modify food proteins, increase durability of textiles, and crosslink hydrogels for drug delivery. We tested the effects of adding GO and partially reduced GO (pRGO) to water solutions of gelatin and then crosslinking it with MTG, measuring both the resulting gelatin modulus and then the time it took for the onset of gelation. We found that the presence of pRGO in a gelatin-MTG-water mixture (when using 0.75 g MTG in 10 ml of gelatin solution) significantly increases the modulus by 60% more than the control. Using this same concentration of MTG, we measured the onset of gelation time and found that pRGO in gelatin solution reduces the onset of gelation time by nearly 50% while inducing a very large increase in viscosity by three orders of magnitude, whereas the addition of GO increases the onset of gelation time by 33% and decreases the viscosity of the gel by more than one order of magnitude. The very large enhancement by pRGO of the viscosity may be due to pRGO’s electron withdrawing ability and/or may also be due to adsorption of gelatin to the pRGO platelets which effectively increases the crosslinking density through non-enzymatic processes assisting the enzymatic activity.
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Gál, Robert, Pavel Mokrejš, Petr Mrázek, Jana Pavlačková, Dagmar Janáčová, and Jana Orsavová. "Chicken Heads as a Promising By-Product for Preparation of Food Gelatins." Molecules 25, no. 3 (January 23, 2020): 494. http://dx.doi.org/10.3390/molecules25030494.
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Every year, the poultry industry produces a large number of by-products such as chicken heads containing a considerable proportion of proteins, particularly collagen. To prepare gelatin is one of the possibilities to advantageously utilize these by-products as raw materials. The aim of the paper was to process chicken heads into gelatins. An innovative method for conditioning starting raw material was using the proteolytic enzyme. Three technological factors influencing the yield and properties of extracted gelatins were monitored including the amount of enzyme used in the conditioning of the raw material (0.4% and 1.6%), the time of the conditioning (18 and 48 h), and the first gelatin extraction time (1 and 4 h). The gelatin yield was between 20% and 36%. The gelatin gel strength ranged from 113 to 355 Bloom. The viscosity of the gelatin solution was determined between 1.4 and 9.5 mPa.s. The content of inorganic solids varied from 2.3% to 3.9% and the melting point of the gelatin gel was recorded between 34.5 and 42.2 °C. This study has shown that gelatin obtained from chicken heads has a promising potential with diverse possible applications in the food industry, pharmacy, and cosmetics.
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Ghafouri Azar, Mina, Lucie Wiesnerova, Jana Dvorakova, Petra Chocholata, Omid Moztarzadeh, Jiri Dejmek, and Vaclav Babuska. "Optimizing PCL/PLGA Scaffold Biocompatibility Using Gelatin from Bovine, Porcine, and Fish Origin." Gels 9, no. 11 (November 14, 2023): 900. http://dx.doi.org/10.3390/gels9110900.
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This research introduces a novel approach by incorporating various types of gelatins, including bovine, porcine, and fish skin, into polycaprolactone and poly (lactic-co-glycolic acid) using a solvent casting method. The films are evaluated for morphology, mechanical properties, thermal stability, biodegradability, hemocompatibility, cell adhesion, proliferation, and cytotoxicity. The results show that the incorporation of gelatins into the films alters their mechanical properties, with a decrease in tensile strength but an increase in elongation at break. This indicates that the films become more flexible with the addition of gelatin. Gelatin incorporation has a limited effect on the thermal stability of the films. The composites with the gelatin show higher biodegradability with the highest weight loss in the case of fish gelatin. The films exhibit high hemocompatibility with minimal hemolysis observed. The gelatin has a dynamic effect on cell behavior and promotes long-term cell proliferation. In addition, all composite films reveal exceptionally low levels of cytotoxicity. The combination of the evaluated parameters shows the appropriate level of biocompatibility for gelatin-based samples. These findings provide valuable insights for future studies involving gelatin incorporation in tissue engineering applications.
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Ding, Yan, Xiacong Zhang, Wen Li, and Afang Zhang. "Dendronized Gelatin-Mediated Synthesis of Gold Nanoparticles." Molecules 27, no. 18 (September 18, 2022): 6096. http://dx.doi.org/10.3390/molecules27186096.
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Thermoresponsive dendronized gelatins (GelG1) or gelatin methacrylates (GelG1MA) were used as precursors to modulate the efficient reduction of Au(III) to form stable gold nanoparticles (AuNPs) through UV irradiation. These dendronized gelatins were obtained through the amidation of gelatin or gelatin methacrylates with dendritic oligoethylene glycols (OEGs). Crowded OEG dendrons along the gelatin backbones create a hydrophobic microenvironment, which promotes the reduction of Au(III). Gelatin backbones act as ligands through the electron-rich groups to facilitate the reduction, while the dendritic OEGs provide shielding effects through crowding to form a hydrophobic microenvironment, which not only enhances the reduction but also stabilize the formed AuNPs through encapsulation. The effects of dendron coverage on the dendronized biomacromolecules and their thermoresponsiveness on the reduction kinetics were examined. Dendronized gelatin/AuNPs hydrogels were further prepared through the in situ photo-crosslinking of GelG1MA. The modification of natural macromolecules through dendronization presented in this report facilitates a novel platform for the environmentally friendly synthesis of noble metal nanoparticles, which may form a new strategy for developing smart nano-biosensors and nano-devices.
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Mokrejš, Pavel, Robert Gál, Jana Pavlačková, and Dagmar Janáčová. "Valorization of a By-Product from the Production of Mechanically Deboned Chicken Meat for Preparation of Gelatins." Molecules 26, no. 2 (January 12, 2021): 349. http://dx.doi.org/10.3390/molecules26020349.
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In recent decades, food waste management has become a key priority of industrial and food companies, state authorities and consumers as well. The paper describes the biotechnological processing of mechanically deboned chicken meat (MDCM) by-product, rich in collagen, into gelatins. A factorial design at two levels was used to study three selected process conditions (enzyme conditioning time, gelatin extraction temperature and gelatin extraction time). The efficiency of the technological process of valorization of MDCM by-product into gelatins was evaluated by % conversion of the by-product into gelatins and some qualitative parameters of gelatins (gel strength, viscosity and ash content). Under optimal processing conditions (48–72 h of enzyme conditioning time, 73–78 °C gelatin extraction temperature and 100–150 min gelatin extraction time), MDCM by-product can be processed with 30–32% efficiency into gelatins with a gel strength of 140 Bloom, a viscosity of 2.5 mPa.s and an ash content of 5.0% (which can be reduced by deionization using ion-exchange resins). MDCM is a promising food by-product for valorization into gelatins, which have potential applications in food-, pharmaceutical- and cosmetic fields. The presented technology contributes not only to food sustainability but also to the model of a circular economy.
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Zuev, Yuriy F., Svetlana R. Derkach, Liliya R. Bogdanova, Nikolai G. Voron’ko, Yulia A. Kuchina, Aidar T. Gubaidullin, Ivan V. Lunev, et al. "Underused Marine Resources: Sudden Properties of Cod Skin Gelatin Gel." Gels 9, no. 12 (December 18, 2023): 990. http://dx.doi.org/10.3390/gels9120990.
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The main object of this work was to characterize the structure and properties of laboratory-made fish gelatin from cod skin in comparison with known commercial gelatins of fish and mammalian origin. This is one way we can contribute to the World Food Program and characterize foodstuff resources from alternative natural sources. Our research was based on the combination of an expanded set of complementary physical–chemical methods to study the similarities and distinctions of hydrogels from traditional and novel gelatin sources from underused marine resources. In this work, we have compared the morphology, supramolecular structure and colloid properties of two commercial (mammalian and fish) gelatins with gelatin we extracted from cold-water cod skin in laboratory conditions. The obtained results are novel, showing that our laboratory-produced fish gelatin is much closer to the mammalian one in terms of such parameters as thermal stability and strength of structural network under temperature alterations. Especially interesting are our experimental observations comparing both fish gelatins: it was shown that the laboratory-extracted cod gelatin is essentially more thermally stable compared to its commercial analogue, being even closer in its rheological properties to the mammalian one.
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Okawa, Y., W. Komuro, H. Kobayashi, and T. Ohno. "Rheological Study on Gelatin Gelation." Imaging Science Journal 45, no. 3-4 (January 1997): 197–200. http://dx.doi.org/10.1080/13682199.1997.11736184.
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Abete, Tiziana, Emanuela Del Gado, and Lucilla de Arcangelis. "Gelation kinetics of crosslinked gelatin." Polymer Composites 34, no. 2 (January 8, 2013): 259–64. http://dx.doi.org/10.1002/pc.22399.
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Derkach, Svetlana R., Nikolay G. Voron’ko, Yuliya A. Kuchina, and Daria S. Kolotova. "Modified Fish Gelatin as an Alternative to Mammalian Gelatin in Modern Food Technologies." Polymers 12, no. 12 (December 19, 2020): 3051. http://dx.doi.org/10.3390/polym12123051.
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This review considers the main properties of fish gelatin that determine its use in food technologies. A comparative analysis of the amino acid composition of gelatin from cold-water and warm-water fish species, in comparison with gelatin from mammals, which is traditionally used in the food industry, is presented. Fish gelatin is characterized by a reduced content of proline and hydroxyproline which are responsible for the formation of collagen-like triple helices. For this reason, fish gelatin gels are less durable and have lower gelation and melting temperatures than mammalian gelatin. These properties impose significant restrictions on the use of fish gelatin in the technology of gelled food as an alternative to porcine and bovine gelatin. This problem can be solved by modifying the functional characteristics of fish gelatin by adding natural ionic polysaccharides, which, under certain conditions, are capable of forming polyelectrolyte complexes with gelatin, creating additional nodes in the spatial network of the gel.
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Yesiltas, Betül, Chloé Robert, Heidi Olander Petersen, Flemming Jessen, Fatemeh Ajalloueian, Mohammad Amin Mohammadifar, Charlotte Jacobsen, Jens J. Sloth, Greta Jakobsen, and Federico Casanova. "Gelatin from Saithe (Pollachius virens) Skin: Biochemical Characterization and Oxidative Stability in O/W Emulsions." Marine Drugs 20, no. 12 (November 25, 2022): 739. http://dx.doi.org/10.3390/md20120739.
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This study performed the extraction of gelatin from saithe (Pollachius virens) skin and compared it to commercial marine gelatin. As a first stage, we investigated the physicochemical and biochemical properties of the gelatin. SDS-PAGE analysis revealed the presence of α-chains, β-chains, and other high-molecular-weight aggregates. DSC thermograms showed typical gelatin behavior, while the FTIR spectra were mainly situated in the amide band region (amide A, amide B, amide I, amide II, and amide III). In the second stage, we produced O/W emulsions and analyzed their physical and oxidative stability over 9 days. Oil droplets stabilized with the gelatins obtained from saithe fish skin had a size of ~500 nm and a ζ-potential ~+25 mV, which is comparable to oil droplets stabilized with commercial gelatin products. Moreover, the oxidative stability of the emulsions stabilized with gelatin from saithe fish skin showed promising results in terms of preventing the formation of some volatile compounds towards the end of the storage period compared to when using the commercial gelatins. This study indicates the potential application of fish skin gelatin in the fields of food and cosmetics, as well as suggesting that further investigations of their techno-functional properties.
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Gál, Robert, Pavel Mokrejš, Jana Pavlačková, Ngo Thi Hong Linh, and Jiří Mlček. "Biotechnological Processing of Laying Hen Paw Collagen into Gelatins." Processes 8, no. 11 (November 6, 2020): 1415. http://dx.doi.org/10.3390/pr8111415.
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By-products of laying hens represent a promising raw material source with a high collagen content, which is currently not adequately used. The aim of the paper is to prepare gelatins from laying hen paws. The purified collagen raw material was processed by a biotechnological process using the food endoprotease Protamex®. After cleavage of the cross-links in the collagen structure, the gelatin was extracted by a batch process with a stirrer in two extraction steps. The influence of the extraction process on the yield of gelatins and on selected qualitative parameters of gelatins was monitored by two-level factor experiments with three selected process factors. The studied factors were: enzyme dosage (0.2–0.8%), enzyme processing time (24–72 h) and gelatin extraction time (30–120 min). After the first extraction step at 75 °C, gelatin was extracted with a yield of 8.2–21.4% and a gel strength of 275–380 Bloom. In the second extraction step at 80–100 °C, it is possible to obtain another portion (3.3–7.7%) of gelatin with a gel strength of 185–273 Bloom. Total extraction efficiency of gelatins prepared from laying hen collagen is almost 30%. The prepared gelatins are of high quality and, under proper extraction conditions, gelatins with a gel strength above 300 Bloom can be prepared, thus equaling commercial beef and pork gelatins of the highest quality. Biotechnological processing of laying hen collagen into gelatins is environmentally friendly.
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Sakai, Shinji, Hiromi Ohi, and Masahito Taya. "Gelatin/Hyaluronic Acid Content in Hydrogels Obtained through Blue Light-Induced Gelation Affects Hydrogel Properties and Adipose Stem Cell Behaviors." Biomolecules 9, no. 8 (August 5, 2019): 342. http://dx.doi.org/10.3390/biom9080342.
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Composite hydrogels of hyaluronic acid and gelatin attract great attention in biomedical fields. In particular, the composite hydrogels obtained through processes that are mild for cells are useful in tissue engineering. In this study, hyaluronic acid/gelatin composite hydrogels obtained through a blue light-induced gelation that is mild for mammalian cells were studied for the effect of the content of each polymer in the precursor solution on gelation, properties of resultant hydrogels, and behaviors of human adipose stem cells laden in the hydrogels. Control of the content enabled gelation in less than 20 s, and also enabled hydrogels to be obtained with 0.5–1.2 kPa Young’s modulus. Human adipose stem cells were more elongated in hydrogels with a higher rather than lower content of hyaluronic acid. Stem cell marker genes, Nanog, Oct4, and Sox2, were expressed more in the cells in the composite hydrogels with a higher content of hyaluronic acid compared with those in the hydrogel composed of gelatin alone and on tissue culture dishes. These results are useful for designing conditions for using gelatin/hyaluronic acid composite hydrogels obtained through blue light-induced gelation suitable for tissue engineering applications.
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Ahmad, Farhani, Musfirah Azmi, Nurhamieza Md Huzir, and Norhidayu Muhamad Zain. "Development of Gelatin from Halal and Alternative Sources: A Review." Nusantara Halal Journal (Halal awareness, opinion, research, and initiative) 2, no. 2 (December 28, 2021): 56–62. http://dx.doi.org/10.17977/um060.2021v2p056-062.
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Gelatin is a common ingredient used in various industrial sectors including food and beverage, cosmetic, pharmaceutical as well as biomedical. Due to inexpensive processing cost and shorter processing time, porcine becomes the main source of gelatin. Thus, the application of this ingredient creates several problems especially issues related to its halal status among Muslim community. The present study aims at reviewing the development of gelatin from halal sources and their potential as alternatives to substitute the sources of non-halal gelatins. The applications of gelatin in food industry and the current issues on halal gelatin have been discussed in detail. The halal source of gelatin required intense study due to prominent demand of it not only in food industry but also in pharmaceutical industry. The development of halal gelatin provides Muslim alternatives and choices to consume gelatin as food and pharmaceutical products and yet complying with Islamic obligations.
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Harikedua, Silvana Dinaintang. "PROTEIN GELS: A MINI REVIEW." MEDIA TEKNOLOGI HASIL PERIKANAN 7, no. 1 (December 13, 2018): 19. http://dx.doi.org/10.35800/mthp.7.1.2019.19523.
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The use of gelatin as food additive for gelling properties was discussed in this review. Three products (i.e. gel dessert, yoghurt, and surimi) were selected as the main focus of this mini review since they characterized 3 different protein gelation system. The mechanism of gelatin gelation in water system was described by gel dessert, the gelation of casein in dairy product was presented by yoghurt, and the gelation of sarcoplasmic protein in meat system was exemplify by surimi. Overall, the mechanism of gelation mainly contributed by the networking of protein-protein which is strengthen by the intermolecular bond and intramolecular bond.
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Matulessy, Dellen N., Yuni Erwanto, Nurliani Nurliani, and Edy Suryanto. "EKSTRAKSI DAN KARAKTERISASI GELATIN TULANG KAMBING KACANG MENGGUNAKAN NEUTRASE." Agrinimal Jurnal Ilmu Ternak dan Tanaman 8, no. 1 (August 6, 2020): 24–32. http://dx.doi.org/10.30598/ajitt.2020.8.1.24-32.
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This study aims was to evaluate the characteristics of the gelatine derivate from Kacang goat bone extracted enzymatically using neutrase at different enzyme concentrations. The neutrase treatments, namely GTK-N0 (gelatin with neutrase 0%), GTK-N1 (Gelatin with 0.25% neutrase), GTK-N2 (Gelatin with neutrase 0.5%) and GTK-N3 (Gelatin with neutrase 0,75%). The bones sample used the bones from local Kacang goat aged 6 to 12 months. The study used was a randomized complete design (Oneway ANOVA) with 4 enzyme concentration treatments with 5 replications each treatment. The parameters observed were gelatin yields, the proximate analysis was performed on goat bones and gelatin (water content, ash, fat, and crude protein), pH, gel strength, viscosity, and functional groups of gelatin FTIR. The results showed that the application of the neutrase enzyme at the 0.25% level had the significant effect on the characteristics of the gelatin produced. The conclusion of this study neutrase can be used for enzymatically extracting gelatin from the bones of local Kacang goat and produced the gelatin characteristics that can be used for food applications.
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Lou, Ching Wen, Po Ching Lu, Jin Jia Hu, and Jia Horng Lin. "Manufacturing Technique and Property Evaluations of PET/Gelatin Composite Tubular Braids." Advanced Materials Research 910 (March 2014): 157–60. http://dx.doi.org/10.4028/www.scientific.net/amr.910.157.
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This study examine the influence of gelatain with different concentrations on the physical property of the PET/Gelatin composite tubular braids. PET fibers are braided into tubular braids on a braider, and then immersed in gelatin solution with various concentrations to form PET/Gelatin composite tubular braids. The tensile strength and water contact angle of the braids are then tested to determine the their physical properties. The experiment results show that an increasing concentration of gelatin does not result in a significant varation in tensile strength, but a decreased displacement only.
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Chen, Jia, Xian-Long Cheng, Feng Wei, Qian-Qian Zhang, Ming-Hua Li, and Shuang-Cheng Ma. "Detection of Gelatin Adulteration in Traditional Chinese Medicine: Analysis of Deer-Horn Glue by Rapid-Resolution Liquid Chromatography-Triple Quadrupole Mass Spectrometry." Journal of Analytical Methods in Chemistry 2015 (2015): 1–9. http://dx.doi.org/10.1155/2015/259757.
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Simultaneous identification of donkey-hide gelatin and bovine-hide gelatin in deer-horn glue was established by rapid-resolution liquid chromatography-triple quadrupole mass spectrometry. Water containing 1% NH4HCO3was used for sample dissolution and trypsin was used for hydrolysis of the gelatins. After separation by a SB-C18 reversed-phase analytical column, collagen marker peptides were detected by mass spectrometry in positive electrospray ionization mode with multiple reaction monitoring. The method was specific, precise and reliable, and suitable for detection of adulterants derived from donkey-hide gelatin and bovine-hide gelatin in deer-horn glue.
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YULIANI, Yuliani, Bambang Tri AGUNG, Marwati MARWATI, and Krishna Purnawan CANDRA. "Physico-Chemical Characteristics of Giant Featherback (Chitala lopis) and Mackerel (Scomberomorus commerson) Bone Gelatins and Their Potential as Gelling agents in Gel Mixtures for Roselle (Hibiscus sabdariffa L.) Soft Jelly Candies." Walailak Journal of Science and Technology (WJST) 17, no. 7 (July 1, 2020): 678–85. http://dx.doi.org/10.48048/wjst.2020.4559.
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The gel strength of gelatin depends on its raw material. Fish gelatin shows a broad range of gel strengths. Giant featherback and mackerel bone gelatins have the gel strengths 220 and 38 Bloom, respectively. Here, we prepared roselle soft jelly candy using the single gelatin and mixtures gelatins from bovine, giant featherback, and mackerel sources. Roselle calyces extract has been used as a food additive to improve taste, aroma, and antioxidant content. The soft jelly candies (1.5 % w/v roselle extract and 12 % gelling agent) were prepared using three types of gelatin (giant featherback (GF), mackerel (M), and bovine (B)) in four mixtures (GF:B = 1:3, GF:B = 1:1, M:B = 1:3, and M:B = 1:1). This experiment was arranged in a completely randomized design with three replications for each treatment. Physico-chemical and sensory characteristics of the jelly candies were determined. The data were analyzed by ANOVA continued by the LSD test. The results showed that water content, pH, gel strength, hardness, rigidity, and hedonic quality (taste, color, texture, and overall performance) of the roselle soft jelly candies were affected by choice of gelatin, but not total reducing sugar. Roselle soft jelly candy made with giant featherback and bovine gelatin (1:3) mix was the most preferred by the panelists.
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Mohammed, Ameer A. "Studies of Some Physical Properties of the extracted gelatin from Cynoglossus bilineatus skin." Iraqi Journal of Aquaculture 13, no. 2 (December 1, 2021): 165–78. http://dx.doi.org/10.58629/ijaq.v13i2.107.
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The study included extracting of gelatin from the fish`s skin Cynoglossus bilineatus using acid and alkaline pretreatment the chemical analysis of the experiment fishes skin shows that the extracted gelatin was 11.7% for yield, 85.7% for protein, 0.84% for fat , 0.65% for ash and 12.81% moisture. The physical properties of extracted gelatin such as melting point was 25.3 °C, setting points 21.8°C and 112 Sc. While the relatively viscosity was 2.5 cP, the result shows that the extracted gelatin have an ability to gelation in all concentrations, the emulsifying property increased with increasing of the concentration of the sample, the extracted gelatin have a good sensory properties with a pale Yellow color and less fish smell acceptable.
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Yasmin, Rehana, Mohsin Shah, Saeed Ahmad Khan, and Roshan Ali. "Gelatin nanoparticles: a potential candidate for medical applications." Nanotechnology Reviews 6, no. 2 (April 1, 2017): 191–207. http://dx.doi.org/10.1515/ntrev-2016-0009.
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AbstractGelatin is a protein obtained from the hydrolysis of collagen. Gelatin is an attractive biodegradable material for use in nano-biotechnology and nano-pharmaceutics. Gelatin nanoparticles (NPs) have been widely used as drug and gene carrier to targeted sick tissues including cancer, tuberculosis, HIV infection along with the treatment of vasospasm and restenosis, due to its biocompatibility and biodegradability. For instance, coating with gelatin lowers the cytotoxicity of quantum dots. Moreover, gelatin NPs have the ability to cross the blood-brain barrier, hence proven as a promising candidate to target brain disorders. Macrophage targeting with gelatin NPs for remedy of different diseases is repeatedly reported in previous years. In tissue engineering gelatin is actively utilized for construction of biological and life-long 3D scaffolds for bio-artificial tissues and organ production. Gelatins have a wide range of potential applications which needs to be unraveled in more detail. This review is mainly focused on the applications of gelatin NPs in biomedical sciences.
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He, Jinmeng, Jian Zhang, Yingjie Xu, Yigang Ma, and Xiaobing Guo. "The Structural and Functional Differences between Three Species of Fish Scale Gelatin and Pigskin Gelatin." Foods 11, no. 24 (December 7, 2022): 3960. http://dx.doi.org/10.3390/foods11243960.
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In this paper, gelatin was extracted from the scales of Coregonus peled, Carp and Bighead carp by the acid method, and the structure and functional properties of the obtained scale gelatin and food-grade pigskin gelatin (FG) were compared. The results showed that all gelatins exhibited relatively high protein (86.81–93.61%), and low lipid (0.13–0.39%) and ash (0.37–1.99%) contents. FG had the highest gel strength, probably because of its high proline content (11.96%) and high average molecular weight distribution. Low β-antiparallel was beneficial to the stability of emulsion, which led FG to have the best emulsifying property. The high content of hydrophobic amino acids may be one of the reasons for the superior foaming property of Bighead carp scales gelatin (BCG). The gel strength of Carp scales gelatin (CG) and BCG, the ESI of Coregonus peled scales gelatin (CPG) and the foaming property of BCG indicate that fish gelatin has the potential to be used in food industry as a substitute for pig skin gelatin.
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Mokrejš, Pavel, Robert Gál, and Jana Pavlačková. "Enzyme Conditioning of Chicken Collagen and Taguchi Design of Experiments Enhancing the Yield and Quality of Prepared Gelatins." International Journal of Molecular Sciences 24, no. 4 (February 11, 2023): 3654. http://dx.doi.org/10.3390/ijms24043654.
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During the production of mechanically deboned chicken meat (MDCM), a by-product is created that has no adequate use and is mostly disposed of in rendering plants. Due to the high content of collagen, it is a suitable raw material for the production of gelatin and hydrolysates. The purpose of the paper was to process the MDCM by-product into gelatin by 3-step extraction. An innovative method was used to prepare the starting raw material for gelatin extraction, demineralization in HCl, and conditioning with a proteolytic enzyme. A Taguchi design with two process factors (extraction temperature and extraction time) was used at three levels (42, 46, and 50 °C; 20, 40, and 60 min) to optimize the processing of the MDCM by-product into gelatins. The gel-forming and surface properties of the prepared gelatins were analyzed in detail. Depending on the processing conditions, gelatins are prepared with a gel strength of up to 390 Bloom, a viscosity of 0.9–6.8 mPa·s, a melting point of 29.9–38.4 °C, a gelling point of 14.9–17.6 °C, excellent water- and fat-holding capacity, and good foaming and emulsifying capacity and stability. The advantage of MDCM by-product processing technology is a very high degree of conversion (up to 77%) of the starting collagen raw material to gelatins and the preparation of 3 qualitatively different gelatin fractions suitable for a wide range of food, pharmaceutical, and cosmetic applications. Gelatins prepared from MDCM by-product can expand the offer of gelatins from other than beef and pork tissues.
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Roman, Voroshilin, Prosekov Alexander, Kurbanova Marina, and Kolbina Anastasiya. "Rheological characteristics of gelatin obtained from secondary raw materials of poultry processing." Poultry and Chicken Products 24, no. 2 (2022): 54–58. http://dx.doi.org/10.30975/2073-4999-2022-24-2-54-58.
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The investigation purpose is to carry out analysis of physical and chemical traits and rheological characteristics for gelatin received from broiler paws with enzyme acid hydrolysis method. Experimental gelatin sample has been shown to surpass control one in dry matter content including protein mass fraction by 1.5% average. The rest physical and chemical traits of experimental sample was at control sample level. Experimental gelatin characteristic has shown significant enzyme acid hydrolysis influence at gelation and gel strength traits.
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Janowicz, Monika, Sabina Galus, Karolina Szulc, Agnieszka Ciurzyńska, and Małgorzata Nowacka. "Investigation of the Structure-Forming Potential of Protein Components in the Reformulation of the Composition of Edible Films." Materials 17, no. 4 (February 17, 2024): 937. http://dx.doi.org/10.3390/ma17040937.
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To optimize the functional properties of edible films or coatings, mixtures of several ingredients are used, including food processing by-products. In this way, pectin from fruit pomace, whey proteins from whey as a by-product of rennet cheese production, and gelatin from by-products of the processing of slaughtered animals can be obtained. The aim and scope of the investigation were to verify the hypothesis of the research, which assumes that the addition of beef broth to edible gelatin films will affect the gelation processes of the tested film-forming solutions and will allow for the modification of the edible properties of the films obtained based on these solutions. Measurements were carried out to determine the visual parameters, mechanical strengths, surface and cross-sectional structures, FTIR spectra, thermal degradation rates, and hydrophilicities of the prepared gelatin films. The water content, water vapor permeability, and course of water vapor sorption isotherms of the films were also examined, as well as the course of the gelation process for film-forming solutions. The addition of broth to film-forming solutions was found to increase their opacity and color saturation, especially for the ones that were yellow. The films with the addition of broth were more uneven on the surface and more resistant to stretching, and in the case of the selected types of gelatins, they also formed a more stable gel. The broth increased the hydrophilicity and permeability of the water vapor and reduced the water content of the films. The addition of broth enables the practical use of edible films, but it is necessary to modify some features.
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Mehdi-Sefiani, Hanaa, E. Chicardi, A. Romero, and Victor M. Perez-Puyana. "Unveiling the Impact of Gelation Temperature on the Rheological and Microstructural Properties of Type A Gelatin Hydrogels." Polymers 16, no. 13 (June 28, 2024): 1842. http://dx.doi.org/10.3390/polym16131842.
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Gelatin-based hydrogels have garnered significant attention in the fields of drug delivery systems and tissue engineering owing to their biodegradability, biocompatibility, elasticity, flexibility and nontoxic nature. However, there is a lack of information regarding type-A-gelatin-based hydrogels. In this sense, the main aim of this work was the evaluation of the properties of type-A-gelatin-based hydrogel achieved using two different gelation temperatures (4 °C and 20 °C). Thus, the main novelty of this study lies in the analysis of the impact of gelation time on the rheological and microstructural properties of type-A-gelatin-based hydrogels. Moreover, the addition of a drug was also analyzed in order to evaluate the hydrogels’ behavior as a drug delivery system. For this purpose, rheological (strain, frequency sweep tests and flow curves) and microstructural (SEM) characterizations were carried out. The results demonstrated that lowering the gelation temperature improved the rheological properties of the systems, obtaining hydrogels with an elastic modulus of 20 kPa when processing at 4 °C. On the other hand, the increase in the gelation temperature improved the critical strain of the systems at low temperatures. In conclusion, this work showed the feasibility of producing hydrogels with potential application in drug delivery with different properties, varying the testing temperature and incorporating tetracycline into their formulation.
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Miskiyah, Miskiyah, Juniawati Juniawati, Nur Afni Oktafia, and Siti Chairiyah Batubara. "THE EFFECT OF CHICKEN FEET GELATIN TO CHARACTERISTIC OF JELLY CANDY." Jurnal Penelitian Pascapanen Pertanian 18, no. 2 (August 19, 2021): 87. http://dx.doi.org/10.21082/jpasca.v18n2.2021.87-92.
Full textAbstract:
Jelly candy is a soft textured candy processed with hydrocolloid components such as gum, pectin, agar, starch, carrageenan, gelatin. These are used to modify the chewy texture. This study aimed was to determine the effect of the combination of chicken feet gelatin and agar on the quality of jelly candy. Processing of chicken feet gelatin jelly candy based on Caeccar et.al (2018) method by modification. The study used a completely randomized design (CRD) with one factor, five levels and three replications. The factors studied were the ratio of chicken feet gelatin and agar 80:20; 60:40; 40:60; 20:80; 0:100. Product quality characteristics observed in this study were water content, ash content, reducing sugar content, sucrose content, and organoleptic quality. The results showed that the combination of chicken feet gelatine and agar were significantly affected water, ash, reducing sucrose content. Jelly candy with a treatment combination of 80% chicken feet gelatine and 20% agar was the best treatment. The results of the analysis of the candy were water content of 11.02± 0.04%, ash content of 0.89± 0.00%, reducing sugar content of 10.83± 0.01%, sucrose content of 50.68± 0.28%. The organoleptic test results showed that chicken feet gelatine improved the texture and taste of jelly candy.
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Cui, Yuming, Min He, Rui Dai, Hui Chen, and Yanqing Wang. "Cross-linking of Gelatin with Epichlorohydrin in a Sodium-Acetate-Trihydrate/Urea Deep Eutectic Solvent System." Journal of the American Leather Chemists Association 118, no. 3 (March 1, 2023): 95–101. http://dx.doi.org/10.34314/jalca.v118i3.6810.
Full textAbstract:
To improve the cross-linking efficiency of gelatin molecules, sodium acetate trihydrate/urea deep eutectic solvent with 30% water (SAT/U-DES30W, based on DES weight) was proposed as the solvent of gelatin in this paper. The system could overcome the gelation effect of gelatin at low temperature and expose more active groups of gelatin molecules, resulting in better cross-linking effect. Firstly, the optimal reaction concentration of epichlorohydrin (ECH) was determined by boiling water solubility of cross-linking products, and the cross-linking efficiency of gelatin under two systems was judged together with the Glass transition temperature method. Secondly, the water resistance of the cross-linked product was investigated by swelling capacity and water contact angle. The water absorption rate of GEW and GEDES decreased from 4614% to 1500% and 929% at 12 h, respectively, and the water contact angle also obviously decreased, indicating that the cross-linking efficiency of gelatin under DES system was higher. Finally, the cross-linking mechanism of gelatin and ECH were discussed and it was found the thermal stability of GEDES was significantly improved, which would provide a theoretical basis for gelatin-based materials.
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Grijalva Garces, David, Carsten Philipp Radtke, and Jürgen Hubbuch. "A Novel Approach for the Manufacturing of Gelatin-Methacryloyl." Polymers 14, no. 24 (December 11, 2022): 5424. http://dx.doi.org/10.3390/polym14245424.
Full textAbstract:
Gelatin and its derivatives contain cell adhesion moieties as well as sites that enable proteolytic degradation, thus allowing cellular proliferation and migration. The processing of gelatin to its derivatives and/or gelatin-containing products is challenged by its gelation below 30 ∘C. In this study, a novel strategy was developed for the dissolution and subsequent modification of gelatin to its derivative gelatin-methacryloyl (GelMA). This approach was based on the presence of urea in the buffer media, which enabled the processing at room temperature, i.e., lower than the sol–gel transition point of the gelatin solutions. The degree of functionalization was controlled by the ratio of reactant volume to the gelatin concentration. Hydrogels with tailored mechanical properties were produced by variations of the GelMA concentration and its degree of functionalization. Moreover, the biocompatibility of hydrogels was assessed and compared to hydrogels formulated with GelMA produced by the conventional method. NIH 3T3 fibroblasts were seeded onto hydrogels and the viability showed no difference from the control after a three-day incubation period.
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Yuliani, Dewi, Dhienda Risa Awalsasi, and Akyunul Jannah. "Characterization of Gelatin Profile of Chicken Broiler (Gallus domestica) Bone Using SDS-PAGE Electrophoresis." ALCHEMY 7, no. 1 (July 23, 2019): 7. http://dx.doi.org/10.18860/al.v7i1.7437.
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<p>Gelatin, a proteinaceous additive, is obtained from hydrolysis of collagen in the bone, hide and skin of animals. As natural product, gelatin has been applied in many industries with various functions. This study attempt to characterize gelatin profile of broiler chicken (<em>Gallus domestica</em>) using SDS-PAGE electrophoresis. The chicken bone was pretreated using a strong base, sodium hydroxide, producing type B gelatin. The gelatin was purified through precipitation using the variation of ammonium sulfate concentrations (40-70%) and dialysis using cellophane membrane. The purified gelatin was characterized through SDS-PAGE electrophoresis. Based on electrophoresis visualization, reduction of band intensity by ammonium sulfate 40% showed removal of small peptide fragments. The remained gelatin showed two major bands, α-chains and a β-chain with the respective molecular weight of ~135 and ~245 kDa. The protein content of the unpurified gelatin (E1) was 71.65±0.60 mg/L. The purified E1 gelatins by 40-70% of ammonium sulfate addition contained 61.42±3.90, 60.45±1.36, 59.89±0.24, and 55.32±1.05 mg/L of protein concentration, respectively.</p><p> </p><p>Keywords: chicken bone, gelatin profile, protein electrophoresis</p>
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Irfanita, Nining, Widya Lestari, Mohamed Elwathig Saeed Mirghani, Irwandi Jaswir, Fitri Octavianti, and Muhammad Salahuddin Haris. "Attenuated Total Reflectance-Fourier Transform Infrared (ATR-FTIR) Spectroscopy Coupled with Principal Component Analysis and Polymerase Chain Reaction (PCR) Assay for the Detection of Porcine and Bovine Gelatins in Dental Materials." Tropical Life Sciences Research 33, no. 2 (July 15, 2022): 133–53. http://dx.doi.org/10.21315/tlsr2022.33.2.7.
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Muslims are prohibited from consuming products that contain pig products and their derivatives, including porcine gelatin. Medical and dental products are not exempt from the use of gelatin in their formulation. This study employs attenuated total reflectance- Fourier transform infrared spectroscopy (ATR-FTIR) coupled with principal component analysis (PCA) to detect and distinguish between porcine and bovine gelatins in dental materials. The results were further verified by polymerase chain reaction (PCR) assay. Species-specific primers targeting the 212 bp porcine cytochrome b and 271 bp bovine cytochrome b genes were used to amplify DNA in nine dental material samples. Detection and distinction of gelatin standards (bovine and porcine) against gelatin present in the dental materials was achieved using ATR-FTIR combined with PCA within wavenumber 1756 cm–1–1584 cm–1 (Amide I and Amide II). The detection limit for DNA was 0.001 ng/μL and 0.0001 ng/μL for bovine and porcine gelatins, respectively. Using PCR, one sample, BDM 01, was found to contain both porcine and bovine DNA, while one sample (BDM 14) was found to be positive for bovine DNA. The findings suggest that ATR-FTIR combined with PCA and conventional PCR are applicable for the identification of porcine and bovine gelatin in dental materials.
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Ahmad, Tanbir, Amin Ismail, Siti Aqlima Ahmad, Khalilah Abdul Khalil, Elmutaz Atta Awad, Muhammad Tayyab Akhtar, and Awis Qurni Sazili. "Recovery of Gelatin from Bovine Skin with the Aid of Pepsin and Its Effects on the Characteristics of the Extracted Gelatin." Polymers 13, no. 10 (May 12, 2021): 1554. http://dx.doi.org/10.3390/polym13101554.
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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, respectively. 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.