scholarly journals Functional Characteristics of Ultraviolet-Irradiated Tilapia Fish Skin Gelatin

Molecules ◽  
2019 ◽  
Vol 24 (2) ◽  
pp. 254
Author(s):  
Cheng-Kuo Wu ◽  
Jenn-Shou Tsai ◽  
Wen-Chieh Sung
Keyword(s):  
Molecular Structure ◽  
Raman Spectroscopy ◽  
Functional Properties ◽  
Uv Irradiation ◽  
Sodium Dodecyl ◽  
Gel Strength ◽  
Fish Gelatin ◽  
Fish Skin ◽  
Irradiation Treatment ◽  
Fish Skin Gelatin

Studies were undertaken to investigate the effects of ultraviolet (UV) irradiation on the gel strength, color, thermal properties, protein molecular masses, and functional groups of commercially available fish gelatin samples. Commercially available tilapia skin gelatin powder was used as the raw material to investigate the functional properties of fish skin gelatin powder treated with UV irradiation for different durations (0–6 h). The functional properties of fish gelatin and the optimum irradiation treatment conditions were determined through gel strength testing, color characterization, differential scanning calorimetry, sodium dodecyl sulfate polyacrylamide gel electrophoresis, Fourier transform infrared (FTIR) spectroscopy, and Raman spectroscopy. UV irradiation treatment increased gel strength and thermal stability, and significantly degraded the macromolecules. FTIR and Raman spectroscopy data indicated that UV irradiation treatment did not significantly change the molecular structure of fish gelatin powder, but these methods could discriminate the molecular structure of gelatin from various sources. Irradiation for 2 h yielded the highest gel strength and melting peak temperature, and the lowest chromatic aberration.

scholarly journals Quality of Cultured Wader Pari During Storage at Different Temperature

2017 ◽  
Vol 20 (2) ◽  
pp. 339 ◽  
Author(s):  
Mala Nurilmala ◽  
Agoes Mardiono Jacoeb ◽  
Rofi Ahmad Dzaky
Keyword(s):  
Molecular Weight ◽  
Functional Group ◽  
Gel Strength ◽  
Yellowfin Tuna ◽  
Fish Skin ◽  
Alternative Source ◽  
Food Industries ◽  
Sds Page ◽  
Fish Skin Gelatin

Gelatin is one of the products which become a necessity for various industries, i.e. food and non-food industries. The application of gelatin has been increasing year by year in Indonesia. However, there is no<br />gelatin industry in Indonesia so far. Thus, it is necessary to find an alternative source of gelatin, especially from fishery by products.Thus, the purpose of this research was to extract fish skin gelatin of yellowfin tuna with temperature treatments (55, 65 and 75oC). In addition, the properties of resulted gelatin were determined including yield, pH, gel strength, viscosity, functional groups, molecular weight profiles, and amino acid composition. The extraction at 75oC was chosen as the best result. The yield was 17%; pH 5.3; gel strength 1789.55 gf, viscosity 104.2 Cp, respectively. There was functional group amide A, I, II, dan III. SDS-PAGE showed β, α1 dan α2 bands for tuna skin gelatin. In addition, the main amino acids were glycine and proline.

scholarly journals Effects of Temperature on the FT NIR Raman Spectra of Fish Skin Collagen

2021 ◽  
Vol 11 (18) ◽  
pp. 8358
Author(s):  
Maria Połomska ◽  
Leszek Kubisz ◽  
Jacek Wolak ◽  
Dorota Hojan-Jezierska
Keyword(s):  
Molecular Structure ◽  
Raman Spectroscopy ◽  
Secondary Structure ◽  
Raman Spectra ◽  
Molecular Organization ◽  
Fish Skin ◽  
Temperature Range ◽  
Skin Collagen ◽  
Α Helix ◽  
Fish Skin Collagen

The development of regenerative medicine turns attention toward native collagen as a biocompatible material. Particularly interesting is fish skin collagen, which is relatively easy to extract comparing mammalian tissues and free of some pathogens that are dangerous to humans. The paper presents results of IR Raman spectroscopy studies of silver carp (Hypophthalmichthys molitrix) skin collagen. As collagen properties result from its structure and conformation, both sensitive to temperature, FT NIR Raman spectroscopy is an excellent tool to characterize the molecular structure of fish skin collagen, particularly in temperature range typical for the manufacturing processes of biomedical products. Therefore, the Raman spectra were recorded in a temperature range of 300 to 403 K. The analysis of Raman spectra of prepared collagen films, particularly in the range of the bands related to amide I and amide III entities, showed a high content of α-helix and α-helix type molecular organization in fish skin collagen. Additionally, the secondary structure of the studied fish skin collagen is stable up to ~358 K. Heating to 403 K leads to irreversible changes in the molecular structure of fish skin collagen. It was found that the Raman spectrum of fish skin collagen preheated in this manner becomes similar to the spectrum of the collagen obtained from bovine Achilles tendon, whose secondary structure does not change up to 403 K.

scholarly journals Enhancement of Hydrophobicity of Fish Skin Gelatin via Molecular Modification with Oxidized Linoleic Acid

2019 ◽  
Vol 2019 ◽  
pp. 1-11 ◽  
Author(s):  
Wipawee Theerawitayaart ◽  
Thummanoon Prodpran ◽  
Soottawat Benjakul
Keyword(s):  
Amino Acids ◽  
Linoleic Acid ◽  
Free Amino ◽  
Amino Group ◽  
Fish Gelatin ◽  
Fish Skin ◽  
Molar Ratios ◽  
Group Content ◽  
Amino Group Content ◽  
Fish Skin Gelatin

Fish gelatin possesses hydrophilicity in nature since it contains a few hydrophobic amino acids and a large portion of hydrophilic amino acids. Low hydrophobicity of fish gelatin results in poor water vapor barrier and water resistance of gelatin films. This can limit its usage as packaging material. To overcome this drawback, the molecular attachment of hydrophobic domains can effectively improve the hydrophobicity of fish gelatin. In this study, fish skin gelatin modified with oxidized linoleic acid (OLA) prepared under various conditions using different molar ratios of OLA/free amino group content was characterized. When OLA was prepared at 60 and 80°C for various oxidation times (0–24 h), the peroxide value (PV) increased continuously up to 9 and 12 h when reaction was performed at 80 and 60°C, respectively. Consequently, the PV decreased until the end of the reaction (24 h). Thiobarbituric acid reactive substances (TBARS) of OLA were increased sharply up to 12 h, regardless of reaction temperatures. Thus, primary and secondary lipid oxidation products mainly occurred within the first 12 h. As gelatin was modified with different OLA at various OLA/free amino group molar ratios, the one modified with OLA prepared at 60°C for 24 h at a molar ratio of 10 : 1 had the highest increases in surface hydrophobicity and carbonyl content with the coincidentally lowest free amino group content, compared with control gelatin (without OLA modification). Fourier transforms infrared (FTIR) spectra also reconfirmed the presence of fatty acid covalently attached to resulting gelatin. Therefore, OLA could be used to modify gelatin and increase its hydrophobicity.

Effects of Ultraviolet (UV) Treatment on the Properties of Black Tilapia Fish Skins Gelatin

2020 ◽  
Vol 1010 ◽  
pp. 465-470
Author(s):  
Norhasikin Ismail ◽  
Maizlinda Izwana Idris ◽  
Hasan Zuhudi Abdullah
Keyword(s):  
Contact Angle ◽  
Fourier Transform ◽  
Infrared Spectroscopy ◽  
Water Contact Angle ◽  
Uv Irradiation ◽  
Functional Group ◽  
Gel Strength ◽  
Fish Gelatin ◽  
Uv Treatment ◽  
Water Contact

The aim of the study is to investigate the effects of ultraviolet (UV) treatment on the properties of black tilapia fish skins gelatin. The fish gelatin were investigated in terms of gel strength, functional group and the water contact angle of the gelatin. The UV treatment were irradiated with UVA and UVC at different time (0.5, 1.0, 1.5 and 2.0 h). The gel strength of gelatin gel significantly increases after UV irradiation for both UVA and UVC sample. The water contact angle of the gelatin was categorized as hydrophobic for both gelatin that treated with UVA and UVC which the angle >65°. The interactions and characteristic of functional groups for gelatin that treated with UV were analyzed via Fourier Transform Infrared Spectroscopy (FTIR). Results indicated that employing UV irradiation as an alternative method to enhance some of the quality attributes of fish gelatin.

Kemampuan Gelatin Kulit Ikan Menggantikan Gelatin Mamalia Berdasarkan Sifat Fisika-Kimianya untuk Industri Pangan

2016 ◽  
Vol 8 (16) ◽  
pp. 156-167
Author(s):  
Sugihartono Sugihartono
Keyword(s):  
Chemical Properties ◽  
Food Product ◽  
Gel Strength ◽  
Fish Gelatin ◽  
Fish Skin ◽  
Religious Groups ◽  
Physico Chemical ◽  
Alternative Sources ◽  
Bovine Hide

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

scholarly journals The Effect of Gelatin from Different Fish Skin on Physical and Sensory Characteristics of Marsmallow

2019 ◽  
Vol 21 (1) ◽  
pp. 17
Author(s):  
Izmy Nur Aziza ◽  
Yudhomenggolo Sastro Darmanto ◽  
Retno Ayu Kurniasih
Keyword(s):  
Water Content ◽  
Gel Strength ◽  
Partial Hydrolysis ◽  
Fish Skin ◽  
Parametric Data ◽  
Randomized Design ◽  
Honestly Significant Difference ◽  
Significant Difference ◽  
Fish Skin Gelatin

Gelatin is one type of protein obtained from partial hydrolysis of natural collagen. Utilization of gelatin has been widely applied to food, especially in foods related to elastic texture, for example marshmallow. The purpose of this research was to determine the quality of various types of gelatin based on gel strength, elsticity, water content, hedonic and to know the best marshmallow. The experimental design was complete randomized design. The treatment was different fish skin gelatin, namely patin, payus, and cobia with concentration of 7.39%. The parameters consisted of gelatin tests (yield, gel strength, viscosity) and marshmallow tests (gel strength, elasticity, water content and hedonic). Parametric data were analyzed with Analysis of Varience test and continued with Honestly Significant Difference test. The results showed that the use of different skin had significantly different (P<0.05) on yield, gel strength and viscosity, with the result of patin (13.24%, 280.56 bloom, 2.05 cP), payus (15.47%, 328 bloom, 3.18 cP), cobia 17.88%, 392.24 bloom, 5.63, respectively. The use of gelatin from payus and cobia had significantly different (P<0.05) to marshmallow characteristic. Marshmallow with gelatin skin of cobia fish had gel strength 1564.19 g.cm, elasticity 95.16 mm, water content 14.41% and hedonic test with interval of of 7.52 < μ < 7.91 which was means liked by panelists.

scholarly journals The Effect of Different Types and Gelatin Concentrations on Ice Cream Quality

2020 ◽  
Vol 147 ◽  
pp. 03026
Author(s):  
Diah Lestari Ayudiarti ◽  
Suryanti ◽  
Devi Ambarwaty Oktavia
Keyword(s):  
Amino Acids ◽  
Sensory Evaluation ◽  
Ice Cream ◽  
Total Solid ◽  
Quality Parameters ◽  
Fish Gelatin ◽  
Fish Skin ◽  
Different Types ◽  
Fish Skin Gelatin ◽  
Animal Skin

Gelatin is a polymer of amino acids found in collagen in bone tissue and animal skin. It is commonly used gelatin as stabilizer on an ice cream. Research on the effect of different types and gelatin concentrations on ice cream quality has been done. Types of gelatin Types of gelatin were used are commercial gelatin and fish gelatin. Ice cream were made by adding commercial and fish skin gelatin at concentration 0.1%; 0.2%; 0.3%; 0.4% and 0.5%. Overrun, total solid, melting run and sensory evaluation were observed as quality parameters of ice cream. Based on sensory evaluation, panelists preferred the taste of ice cream using additional 0.1% fish gelatin because it has soft texture than others. The result showed that ice cream with additional 0.1% fish gelatin had 30.63% overrun, 40.77% total solid and 197s/g melting run.

Effects of Hydrochloric Acid Concentration on the Properties of Black Tilapia Fish Skin Gelatin

2016 ◽  
Vol 840 ◽  
pp. 165-169 ◽  
Author(s):  
Norhasikin Ismail ◽  
Hasan Zuhudi Abdullah
Keyword(s):  
Hydrochloric Acid ◽  
Acid Concentration ◽  
Storage Time ◽  
Gel Strength ◽  
Hydrochloric Acid Concentration ◽  
Fish Skin ◽  
Percentage Yield ◽  
Fish Skin Gelatin ◽  
Pre Treatment

Gelatin extractedfrom fish skin is an alternativeresource instead of mammalian animals. Theextraction process of gelatin from black tilapia skin was carried out throughthe use of hydrochloric acid (HCl) with different concentration (0.05 M – 1.0 M)and followed by a final extraction with water at 50°C for 4 hours and endedwith drying. Characterization of gel strength was done in accordance with BSI:1975while moisture content and percentage yield on wet basis with AOAC 1999. Theeffects of acid concentration used during pre-treatment process on yield andphysical properties of fish gelatin were measured. The yield of gelatin for0.05 M and 1.0 M were 10.45% to 22.25% respectively. The gel strength ofgelatin at 0.05 M is the highest (833 g) due to longer storage time. Gelatin whichtreated with high acid concentration gives lower in gel strength that suitableas an edible gelatin.

An immunocytochemical study of maternal immunoglobulin localization in the suckling pig intestine

1990 ◽  
Vol 48 (3) ◽  
pp. 922-923
Author(s):  
László G. Kömüves ◽  
Donna S. Turner ◽  
Kathy S. McKee ◽  
Buford L. Nichols ◽  
Julian P. Heath
Keyword(s):  
Sodium Ethoxide ◽  
Intracellular Localization ◽  
Protein A ◽  
Tween 20 ◽  
Intestinal Epithelial ◽  
Immunocytochemical Study ◽  
Fish Skin ◽  
Newborn Piglets ◽  
Rabbit Igg ◽  
Fish Skin Gelatin

In this study we used colloidal gold probes to detect the intracellular localization of colostral immunoglobulins in intestinal epithelial cells of newborn piglets.Tissues were obtained from non-suckled newborn and suckled piglets aged between 1 hour to 1 month. Samples were fixed in 2.5 % glutaraldehyde, osmicated and embedded into Spurr’s resin. Thin (80 nm) sections were etched with 5% sodium ethoxide for 5 min, washed and treated with 4 % sodium-m-periodate in distilled water for 30 min. The sections were then first incubated with blocking buffer (2 % BSA, 0.25 % fish skin gelatin, 0.5 % Tween 20 in 10 mM Trizma buffer, pH=7.4 containing 500 mM NaCl) for 30 min followed by the immunoreagents diluted in the same buffer, 1 hr each. For the detection of pig immunoglobulins a rabbit anti-pig IgG antiserum was used followed by goat anti-rabbit IgG-Au10 or protein A-Au15 probes.

scholarly journals COMPARATIVE STUDIES OF LIGHT MEROMYOSIN PARACRYSTALS DERIVED FROM RED, WHITE, AND CARDIAC MUSCLE MYOSINS

1971 ◽  
Vol 49 (3) ◽  
pp. 883-898 ◽  
Author(s):  
A. Nakamura ◽  
F. Sreter ◽  
J. Gergely
Keyword(s):  
Molecular Structure ◽  
Cardiac Muscle ◽  
Functional Properties ◽  
Comparative Studies ◽  
White Muscle ◽  
Staining Pattern ◽  
Uranyl Acetate ◽  
Positive Staining ◽  
Cardiac Muscles

Tryptic and chymotryptic light meromyosin paracrystals from red and cardiac muscles of rabbit show a negative and positive staining pattern with uranyl acetate and phosphotungstate that sharply differs from that of white muscle light meromyosin paracrystals. The main periodicity of about 430 A is the same regardless of the source of light meromyosin. The results are discussed in terms of the molecular structure and the functional properties of various myosins.

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