fish collagen
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Author(s):  
Sonali Jana ◽  
Pradyot Datta ◽  
Himanka Das ◽  
Prabal Ranjan Ghosh ◽  
Biswanath Kundu ◽  
...  

Author(s):  
Mouna Rahabi ◽  
Marie Salon ◽  
Christelle Bruno-Bonnet ◽  
Mélissa Prat ◽  
Godefroy Jacquemin ◽  
...  

Abstract Purpose Particular interest is now given to the potential of dietary supplements as alternative non-pharmacological approaches in intestinal inflammation handling. In this aim, this study evaluates the efficiency of fish collagen peptides, Naticol®Gut, on colonic inflammation. Methods Wild type and Mannose receptor-deficient in the myeloid lineage C57BL/6 mice were administered with Dextran Sodium Sulfate (DSS), Naticol®Gut, DSS, and Naticol®Gut or only water for 4 or 8 days. Inflammatory status was evaluated by establishing macroscopic and microscopic scores, by measuring cytokine and calprotectin production by ELISA and the myeloperoxidase activity by chemiluminescence. Colonic macrophages were phenotyped by measuring mRNA levels of specific markers of inflammation and oxidative status. Colonic immune populations and T-cell activation profiles were determined by flow cytometry. Mucosa-associated gut microbiota assessment was undertaken by qPCR. The phenotype of human blood monocytes from inflammatory bowel disease (IBD) subjects was characterized by RT-qPCR and flow cytometry and their oxidative activity by chemiluminescence. Results Naticol®Gut-treated DSS mice showed attenuated colonic inflammation compared to mice that were only exposed to DSS. Naticol®Gut activity was displayed through its ability to orient the polarization of colonic macrophage towards an anti-inflammatory and anti-oxidant phenotype after its recognition by the mannose receptor. Subsequently, Naticol®Gut delivery modulated CD4 T cells in favor of a Th2 response and dampened CD8 T-cell activation. This immunomodulation resulted in an intestinal eubiosis. In human monocytes from IBD subjects, the treatment with Naticol®Gut also restored an anti-inflammatory and anti-oxidant phenotype. Conclusion Naticol®Gut acts as a protective agent against colitis appearing as a new functional food and an innovative and complementary approach in gut health.


Author(s):  
C. Moya-Lopez ◽  
J. Valcarcel ◽  
José A. Vázquez ◽  
P. Bourson ◽  
D. Chapron ◽  
...  
Keyword(s):  

Author(s):  
Divya K. Vijayan ◽  
P. R. Sreerekha ◽  
Pavan Kumar Dara ◽  
B. Ganesan ◽  
Suseela Mathew ◽  
...  

2021 ◽  
Vol 924 (1) ◽  
pp. 012089
Author(s):  
Nurhayati ◽  
R Kusumawati ◽  
Suryanti

Abstract Research on fish collagen is now growing rapidly as the use of collagen in industry increases. Collagen extraction begins with the removal of non-collagen proteins using bases to maximize the extraction process. This research aims to determine the effect of differences in NaOH concentrations on the characteristics of tilapia skin collagen. NaOH in collagen extraction serves to remove alkaline soluble proteins to optimize the collagen extraction process. The bases used were NaOH with the concentration of 0.5, 1.0, and 1.5%. The extraction was carried out using the acid method. Using SEM, observation parameters for crude collagen from the tilapia skin include collagen yield, functional group analysis, lightness, and surface morphology. The results of functional groups analysis showed that the collagen obtained in all treatments had typical collagen characteristics, i.e., amide A, amide B, amide I, amide II, and amide III. The non-collagen deproteination treatment with 0.5% NaOH could produce better collagen than the 1.0 and 1.5% concentrations, as indicated by the highest yield (20.42%) and lightness (93.22). Morphological analysis showed that the collagen extracted has an irregular branched fiber structure.


Author(s):  
Naoshi Shimojo ◽  
Akiko Yagami ◽  
Fumiaki Ohno ◽  
Yuta Tsurumi ◽  
Masashi Nakamura ◽  
...  

Author(s):  
S M Nazmuz Sakib

More than 800 million tons of fish are utilizing in a year and 25-30% become waste. The waste amount is beneficial source for extraction of collagen. But procedure of extraction is still to be optimized. The current study was designed to extract collagen from fish through fish waste fermentation under various conditions. For collagen extraction we did lactic acid fermentation in which yogurt and Dough bacteria was added with fish sample and placed it in incubator at 30ºC for one month. In yogurt and dough culture have at least 10 type of lactic acid bacterial species. After every week we check PH of each sample and take soup of that sample. After centrifugation of that sample’s TCA (Trichloroacetic acid) precipitation was done of yogurt and dough sample and kept at -20ºC. then did SDS-PAGE) using 6% resolving and 5% stacking gel of already stored sample. Then HaCaT cells (1 × 104 cells/well) were cultured in 96-well flat-bottom culture plates and treated with appropriate doses of FFCP (fermented fish collagen peptide) for 24 and 48 hours.The SDS-PAGE revealed that the collagen protein of fish had doublet pattern for α1 and α2 chains at corresponding to 145 kDa and 132 kDa respectively. The density for α1 twice as compared to α2. Our result agrees that The fish collagen consists mostly of α-chain as well as little amount of inter and intra molecular cross-linked components of α-chains; b (dimmer) and c (trimer). Different biochemical tests were done for identification of lactic acid bacteria catalase positive, citrate positive, urease negative. Our fermented fish collagen and peptides mixture were test for cellular cytotoxicity and proliferative effect on HaCaT cells. Current result shows that fermented extracted collagen are nontoxic and induce the proliferation of HaCaT cells. Current study is supported by various studies that revealed the medical application of fish extracted collagen as underline.


2021 ◽  
Vol 52 (4) ◽  
pp. 876-884
Author(s):  
Abbas & Shakir

This study aimed to investigate the anti- oxidative  function of catfish collagen hydrolysate in beef minced meat samples through 10 days  storage at 4 o C. Collagen hydrolysate were added to minced meat sample  at two different concentrations (50 & 100 mg/100gm) . The experiment consist from control sample (C without additives) , BHT sample ( B  with 200ppm  butylated hydroxytoluene ) , collagenase hydrolysate samples  C.C.H1, C.C.H2 (100&50 mg/100gm minced meat)  respectively, and collagenase-trypsin hydrolysate samples  C.H.T1 & C.H.T2 respectively (50,100mg/100gm minced meat). Peroxide values (PV), thiobarbutyric acid TBA, free fatty acid (FFA) , pH , total volatile nitrogen TVN values and total plate count assay at 0., 3, 7., 10 days  were determined  . PV of the BHT, C.C.H2 , C.H.T2, C.C.H1, C.H.T1 groups  were significantly (p<0.05) lower than control during storage period .Meanwhile C.C.H2 and  C.H.T2 groups gave the  lowest TBA values through the storage period . There were no significant difference found between the C.C.H2 , C.H.T2  groups and BHT added group in all studied factors. In conclusion, the fish collagen enzymatic hydrolysates are a promising natural antioxidant and good alternative for synthetic antioxidant.


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