scholarly journals Effectiveness of Alkali and Acid to Produce Collagen from Fish Skin of Striped Catifish

2017 ◽  
Vol 20 (2) ◽  
pp. 255
Author(s):  
Hilda Lu’lu’in Nanda Alfira Devi ◽  
Pipih Suptijah ◽  
Mala Nurilmala
Keyword(s):  
Acetic Acid ◽  
Type I Collagen ◽  
Electrophoretic Analysis ◽  
Extraction Process ◽  
Skin Extract ◽  
Type I ◽  
Fish Skin ◽  
Soaking Time ◽  
Randomized Design ◽  
Striped Catfish

Fish skin is one of the alternative sources contained high protein  to isolate collagen. Fish skin generally extracted by the method of acid, alkali and enzymes. The study aim to determine the effectiveness of NaOH<br />and acetic acid on catfish (Pangasius sp.) skin extraction  process.  The concentrations of alkaline pretreatment were 0,05; 0,1; 0,15 and 0,2 M with the soaking time of 2, 4, 6, 8 and 10 h by NaOH replacement in every 2 h. The concentrations of acetic acid for hydrolisis process were 0.05; 0.1; 0.15 and 0.2 M with the soaking time of 1, 2, and 3 h. The experimental design used for pretreatment process is split splot, while for the hydrolysis process is factorial completely randomized design. The results showed that pretreatment with a concentration of 0.05 M NaOH for 4 h has a significant effect for eliminating non-collagen protein (p&lt;0.05). The acetic acid concentration of 0.15 M for 1 h also has a significant effect on fish skin swelling. The yield of striped catfish collagen was 17.272%, the protein content was 86%, and the viscosity was 12 cP. Fish skin extract was identified as type I collagen by functional groups and electrophoretic analysis. Collagen from striped catfish skin has α1 and α2 and protein structure with the molecular weight of α chain were 94 and 98 kDa, meanwhile the molecular wheight of β chain was 204 kD.

Sub‐ and Supramolecular X‐Ray Characterization of Engineered Tissues from Equine Tendon, Bovine Dermis, and Fish Skin Type‐I Collagen

2020 ◽  
Vol 20 (5) ◽  
pp. 2000017 ◽  
Author(s):  
Alberta Terzi ◽  
Nunzia Gallo ◽  
Simona Bettini ◽  
Teresa Sibillano ◽  
Davide Altamura ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Skin Type ◽  
Type I ◽  
Fish Skin ◽  
X Ray ◽  
Engineered Tissues

scholarly journals The Effect of Different pH in Extraction Process Against Physicochemical Properties of Refined Iota Carrageenan from Eucheuma spinosum Seaweed.

2020 ◽  
Vol 8 (1) ◽  
pp. 14
Author(s):  
Miftakhul Ulumiah ◽  
Mochammad Amin Alamsjah ◽  
Kustiawan Tri Pursetyo
Keyword(s):  
Acetic Acid ◽  
Ph Value ◽  
Chemical Properties ◽  
Extraction Process ◽  
Fish Bone ◽  
Weak Acid ◽  
Gel Strength ◽  
Partial Hydrolysis ◽  
Single Chain ◽  
Randomized Design

Gelatin is a simple protein obtained from the partial hydrolysis of collagen from the skin, bones, joints and connective tissue of animals. One potential material for the manufacture of gelatin is fish bone milkfish (Chanos chanos). Gelatin derived from fish bones with acid process is able to change the triple helix collagen fibers into a single chain, whereas the solvent base only produce double chain. Demineralization of bone or fish skin should use a weak acid is acetic acid, because when using strong acids will produce a strong scent and color gelatin becomes dark. This study aims to determine the effect of the use of acetic acid to the production of fish bone gelatin and the concentration of acetic acid is necessary to produce gelatin with physical and chemical properties of the best. This study uses a Completely Randomized Design (CRD) with four treatments and five replications. The treatments used in this study is the concentration of acetic acid 2%, 4%, 6% and 8%. Based on the research, it was found that the acetic acid solvent effect on the value of the yield and gel strength, but has no effect on the pH value and viscosity. Acetic acid concentration 8% give 4.102% yield value; pH value (acidity) 4.98; 134.313 bloom gel strength and viscosity of 3.6 cP. FTIR analysis results indicate that the fish bone gelatin produced from this research have the same functional group with commercial gelatin.

scholarly journals Profiling of Collagens from Swim Bladder of Catfish (Pangasius sp.) by Acid Extraction

2019 ◽  
Vol 22 (2) ◽  
pp. 327-339
Author(s):  
Gressty Sari Br Sitepu ◽  
Joko Santoso ◽  
Wini Trilaksani
Keyword(s):  
Amino Acids ◽  
Acetic Acid ◽  
Triple Helix ◽  
Extraction Process ◽  
Raw Material ◽  
Acid Extraction ◽  
Swim Bladder ◽  
Acid Pretreatment ◽  
Randomized Design ◽  
Completely Randomized Design

Swim bladders of catfish contain high protein, therefore it is can be used as a raw material for collagen. The study aims to determine the chemical characteristics of swim bladders, the pretreatment of non-collagen, extraction of collagen dissolves acid and to evaluate the characteristics of collagen. The method of this study is KOH pretreatment with a concentration of 0,05; 0,1; and 0,15 for 12 hours. The extraction process is done by soaking the sample in a solution of acetic acid with a concentration of 0,25; 0,5 and 0,75 M (ratio 1:10; b/v) and extraction time for 24; 48; and 72 hours at 4oC. The experimental design used for alkaline and acetic acid pretreatment were factorial completely randomized design. The result showed that the protein content of swim bladder was 85,26% (db), the profile of amino acids were dominated by three amino acids namely glycine (56,85 mg/g), prolyne (31,03 mg/g), and alanyne (23,85 mg/g). Using 0,05 M KOH for 8 h was selected as the best pretreatment method for collagen extraction. Extraction method using 0,50 M acetic for 48 h resulted he best collagen which revealed the existence of a triple helix structure and had Tg 84oC.

scholarly journals COLLAGEN EXTRACTION FROM YELLOWFIN TUNA (Thunnus albacares) SKIN AND ITS ANTIOXIDANT ACTIVITY

2019 ◽  
Vol 81 (2) ◽  
Author(s):  
Mala Nurilmala ◽  
Shita Fauzi ◽  
Dian Mayasari ◽  
Irmanida Batubara
Keyword(s):  
Antioxidant Activity ◽  
Acetic Acid ◽  
Sodium Hydroxide ◽  
Type I Collagen ◽  
Electrophoretic Pattern ◽  
Dry Weight ◽  
Butyl Alcohol ◽  
Type I ◽  
Acid Soluble Collagen ◽  
Skin Collagen

Tuna skin, a byproduct of the fish processing industry, is used as an alternative collagen source to replace bovine and porcine products. This study aimed to extract collagen from tuna skin with acetic acid, and investigated the antioxidant activity. Collagen extraction was carried out through a pretreatment process, defatted with butyl alcohol, and soaking in acetic acid to extract the Acid Soluble Collagen (ASC). The effect of concentration of sodium hydroxide and soaking time on the non-collagenous protein removed were measured, and evaluated. The yield and antioxidant activity of each sample were evaluated and the best result was determined by ANOVA. The highest yield of collagen was 3.18% based on dry weight reached at the treatment with sodium hydroxide 0.2 M and acetic acid 1 M. The different treatments did not result in any significant differences in the spectrum of amide A, B, I, II and III which are the characteristics spectra of collagen. Based on the electrophoretic pattern, tuna skin collagen has two  chains (1 and 2), and one β chain. Therefore, it is classified as type I collagen. The main amino acids were glycine and proline. In addition, the strongest antioxidant activity was found in the sample treated with sodium hydroxide 0.05 M and acetic acid 1 M treatment with IC50 value of 0.45 mg/mL. This study is the first to report on antioxidant activity from fish collagen (not hydrolysate or peptide products).

Sequential extracts of human bone show differing collagen synthetic rates

2002 ◽  
Vol 30 (2) ◽  
pp. 61-65 ◽  
Author(s):  
J. Babraj ◽  
D.J. Cuthbertson ◽  
P. Rickhuss ◽  
W. Meier-Augenstein ◽  
K. Smith ◽  
...  
Keyword(s):  
Acetic Acid ◽  
Collagen Synthesis ◽  
Type I Collagen ◽  
Human Bone ◽  
Bone Collagen ◽  
Type I ◽  
Human Beings ◽  
Collagen Turnover ◽  
Bone Collagen Synthesis

Type I collagen is the major bone protein. Little is known quantitatively about human bone collagen synthesis in vivo, despite its importance for the understanding of bone formation and turnover. Our aim was to develop a method that could be used for the physiological and pathophysiological investigation of human bone collagen synthesis. We have carried out preliminary studies in patients undergoing hip replacement and in pigs to validate the use of the flooding dose method using 13C- or 15N-labelled proline and we have now refined our techniques to allow them to be used in a normal clinical or physiological setting. The results show that the application of a flooding dose causes bone free-proline labelling to equilibrate with that of blood in pigs and human beings, so that only 150 mg of bone will provide enough sample to prepare and measure the labelling of three fractions of bone collagen (dissolved in NaCl, acetic acid and pepsin/acetic acid) which have the same relative labelling (1.0:0.43:0.1) as measured by GC-combustion-isotope ratio MS. The rates of incorporation were substantially faster than in skeletal muscle samples taken at the same time. The results suggest that different fractions of human bone collagen turnover at markedly higher rates than had been previously considered. This approach should allow us to discover how growth and development, food, activity and drugs affect bone collagen turnover and to measure the effects on it of ageing and bone disease.

scholarly journals Effectiveness of Alkaline Pretreatment and Acetic Acid Hydrolysis on the Characteristics of Collagen from Fish Skin of Snakehead

2015 ◽  
Vol 18 (3) ◽  
Author(s):  
Wulandari Wulandari ◽  
Pipih Suptijah
Keyword(s):  
Acetic Acid ◽  
Alkaline Pretreatment ◽  
Fish Skin ◽  
Acid Pretreatment ◽  
Alternative Source ◽  
Randomized Design ◽  
Collagen Protein ◽  
Sheet Structure ◽  
Completely Randomized Design ◽  
Β Sheet

<p>Fish skin is one of marine byproducts potential for alternative source of collagen. This study<br />investigated the effectiveness of alkaline and acetic acid pretreatment on the characteristics of<br />collagen from skin snakehead fish. The concentrations of alkaline pretreatment were 0.05; 0.1; 0.15<br />and 0.2 M for 2, 4, 6, 8, 10 and 12 hours, acetic acid concentrations were 0.05 M, 0.1 M, 0.15 M and<br />0.2 M for 1 and 2 hours. The experimental design used for alkaline and acetic acid pretreatment<br />was factorial completely randomized design. The result showed that the concentration of alkaline<br />0.05 M for 6 hours have significant effect on the elimination of non-collagen protein (p&lt;0.05),<br />whereas for the optimum acetic acid at a concentration 0.1 M for 2 hours significantly different<br />on solubility and swelling. Extraction yields of collagen was 16%, with characteristics of whiteness<br />66.67%, protein content 96.21%, viscosity 10 cP, Tmax 159.9oC and glass transition temperature<br />78.55oC. The dominant amino acid composition were glycine (27.11%), proline (13.87%) and<br />alanine (12.58%). Functional groups collagen from skin snakehead fish has β-sheet structure<br />which is a characteristic of collagen.</p>

scholarly journals Studies on type I collagen in skin fibroblasts cultured from twins with lethal osteogenesis imperfecta.

2003 ◽  
Vol 50 (2) ◽  
pp. 481-488 ◽  
Author(s):  
Anna Galicka ◽  
Sławomir Wołczyński ◽  
Andrzej Gindzieński
Keyword(s):  
Osteogenesis Imperfecta ◽  
Type I Collagen ◽  
Direct Sequencing ◽  
Electrophoretic Analysis ◽  
Skin Fibroblasts ◽  
Collagen Molecule ◽  
Molecular Defect ◽  
Type I ◽  
Single Nucleotide Change ◽  
Type I Procollagen

Studies on type I procollagen produced by skin fibroblasts cultured from twins with lethal type II of osteogenesis imperfecta (OI) showed that biosynthesis of collagen (measured by L-[5-(3)H]proline incorporation into proteins susceptible to the action of bacterial collagenase) was slightly increased as compared to the control healthy infant. SDS/PAGE showed that the fibroblasts synthesized and secreted only normal type I procollagen. Electrophoretic analysis of collagen chains and CNBr peptides showed the same pattern of electrophoretic migration as in the controls. The lack of posttranslational overmodification of the collagen molecule suggested a molecular defect near the amino terminus of the collagen helix. Digestion of OI type I collagen with trypsin at 30 degrees C for 5 min generated a shorter than normal alpha2 chain which melted at 36 degrees C. Direct sequencing of an asymmetric PCR product revealed a heterozygous single nucleotide change C-->G causing a substitution of histidine by aspartic acid in the alpha2 chain at position 92. Pericellular processing of type I procollagen by the twin's fibroblasts yielded a later appearance of the intermediate pC-alpha1(I) form as compared with control cells.

scholarly journals Effects of acetic acid on efficiency of collagen extraction from jellyfish \(\textit{Rhopilema hispdium}\) (Vanhöffen, 1888)

2021 ◽  
Vol 21 (1) ◽  
pp. 57-65
Author(s):  
Kha Pham Thi ◽  
Thu Pham The ◽  
Ha Tran Manh ◽  
Thuoc Chu Van ◽  
Hoang Hiep Le Ba
Keyword(s):  
Acetic Acid ◽  
Acid Solution ◽  
Disease Transmission ◽  
Type I Collagen ◽  
High Efficiency ◽  
Acetic Acid Solution ◽  
The Body ◽  
Type I ◽  
Marine Animals ◽  
Promising Alternative

Collagen is an extremely important fibrous protein in the body. It is the main structural material of all tissues: Skin, bones, ligaments, tendons, cartilage. The source of traditional collagen production is mainly from the skin and bones of animals. However, marine animals are currently a promising alternative source of materials with low risk of disease transmission, no religious barriers to consumption, abundant raw materials, and high-efficiency extraction. In present study, the effects of several factors: Acetic acid concentration, the ratio of jellyfish and acetic acid solution (w:v), as well as the time of extraction on efficiency of collagen extraction process from jellyfish (Rhopilema hispidum Vanhoffen, 1888) were investigated. The results showed that the collagen which was extracted from jellyfish in 0.1M acetic acid, with the ratio 1:3 between the jellyfish and acetic acid solution (w:v) in 5-day extraction had high extraction efficiency. Extracted collagen in present study was mainly type I collagen, consisting of 3 polypeptide chains: β chain (~ 250 kDa), α1 chain (~ 40 kDa) and α2 chain (~ 100 kDa).

scholarly journals Review Article: Fish Bone Collagen

2021 ◽  
pp. 33-39
Author(s):  
Andre Wijaya ◽  
. Junianto
Keyword(s):  
Type I Collagen ◽  
Ph Value ◽  
Amino Acid Content ◽  
Extraction Process ◽  
Fish Bone ◽  
Raw Material ◽  
Bone Collagen ◽  
Type I ◽  
Alternative Source ◽  
Salting Out

Fishbone collagen is an alternative source of bovine and pig collagen. The purpose of this article is to review the types, benefits, extraction methods and characterization of collagen from fish bones, especially freshwater fish. The result of the review shows that the collagen from tilapia bones is shaped like a sheet with a slight porous surface and is of type I. Collagen extraction begins with bone disease from the remaining fat, then degreasing and the next step is extraction. After the extraction process is complete, filtration is carried out to store the filtrate or residue, then the collagen is purified by salting-out with NaCl. Collagen yield and collagen pH value from collagen extraction were different for each type of fish bone. The difference in yield value and protein and amino acid content in the resulting collagen can be caused by differences in the extraction method, the concentration of the solution used, whether acid or alkaline, and the neutralization process and the type of raw material. Fishbone collagen has good benefits in the cosmetic and pharmaceutical fields.

Organoleptic Characteristics Of Cow Skin Cracker With Variety Of Skin Types And Souring Time

2021 ◽  
Vol 3 (2) ◽  
Author(s):  
Anita Mustika Ibrahim ◽  
Harapin Hafid ◽  
Ali Bain
Keyword(s):  
Immersion Time ◽  
Skin Extract ◽  
Factor B ◽  
Soaking Time ◽  
Organoleptic Characteristics ◽  
Randomized Design ◽  
Different Types ◽  
Completely Randomized Design ◽  
Difference Test

Skin crackers are snacks which made from cattle skin. In order to get a good quality of skin crackers, the immersion process is carried out in a mixture of whiting solution and pineapple skin extract. This study aimed to evaluate the organoleptic characteristics of cow skin crackers with different types of skin and soaking time. The material used in this study is cow leather, whiting and pineapple skin. The method used is a completely randomized design factorial pattern with 3 x 3 and 4 times repetition. Factor A is the type of skin part (head, foot and neck) and factor B is difference of immersion time (24, 48, 72 and 96 hours). Research variables included color, aroma, taste, joy, crispness and acceptance of the panelists. The data obtained were analyzed using SPSS 16.0 and the smallest real difference test (LSD). The results showed that the interaction between the type of skin and immersion time did not significantly influence (P> 0.05) on color, aroma, taste, crispness, panelist acceptance and preference. Independent skin immersion time significantly influence (P <0.05) on color, aroma, taste, crispness, panelist acceptance and preference. The best treatment is obtained at 96 hours of immersion time.

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