scholarly journals Valorization of Cyprinus Carpio Skin for Biocompatible Collagen Hydrolysates with Potential Application in Foods, Cosmetics and Pharmaceuticals

Author(s):  
Elena Dănilă ◽  
Raluca Stan ◽  
Mădălina Albu Kaya ◽  
Georgeta Voicu ◽  
Maria Minodora Marin ◽  
...  
2021 ◽  
Author(s):  
Elena Danila ◽  
Raluca Stan ◽  
Mădălina ALBU KAYA ◽  
Georgeta VOICU ◽  
Maria Minodora MARIN ◽  
...  

Abstract Fish collagen is the safest source of collagen at present, the extraction being performed on secondary sources as skin, bones, scales or fins resulted after fish processing. The aim of the present study was to obtain biocompatible collagen hydrolysates from waste Cyprinus carpio skin, the main aquaculture species in Romania using an inexpensive and “green” neutral hydrolysis process. Neutral hydrolysis of pretreated fish skins performed for 6 hours at a temperature of 135°C and a pressure of 315 kPa produced collagen hydrolysates in 24.6-35.5% yields depending on the adopted pretreatment procedure. The extensive characterization of hydrolysate samples revealed a high purity degree (98% protein content, undetected ash content, pH value in the range 6-7), also confirmed by the absence of undesired aggregates in the characteristic fibril structure as determined by electronic microscopy. A specific collagen hydrolysate random coil structure and the absence of triple helix was determined by FTIR analysis and sustained by CD spectroscopy and X-ray diffraction. The biocompatibility assessment for the obtained fish collagen hydrolysates revealed no cytotoxic effect on Human keratinocytes, with an 80% cell viability, superior as compared to conventional bovine collagen hydrolysate.Neutral hydrolysis of waste Cyprinus carpio skin yielded collagen hydrolysates with determined characteristics and biocompatibility superior to bovine collagen, suitable for application in foods, cosmetics and pharmaceutical industry.


2009 ◽  
Vol 00 (00) ◽  
pp. 090513010017019-7
Author(s):  
Biagio Solarino ◽  
Giancarlo Di Vella ◽  
Thea Magrone ◽  
Felicita Jirillo ◽  
Angela Tafaro ◽  
...  

Planta Medica ◽  
2010 ◽  
Vol 76 (12) ◽  
Author(s):  
B Chantong ◽  
S Buranasinsup ◽  
P Toniti ◽  
P Suttiyotin ◽  
W Sirimanapong ◽  
...  

1966 ◽  
Vol 15 (01/02) ◽  
pp. 252-272
Author(s):  
K. M Moser ◽  
Mary Belle Frey

Summary1. Caseinolytic and fibrinolytic systems for assay of plasmin in fibrinolytic agents are described which are based upon the determinations of AE/min during the linear portion of the casein-plasmin and fibrin-plasmin reaction curves respectively. A " caseinolytic-rate " unit and “fibrinolytic-rate " unit of ÄE/min × 103 during the linear portion of the respective curves are proposed.2. Data are presented indicating that a reliably linear relationship exists between plasmin concentration and these caseinolytic - and fibrinolytic-rate units.3. Data comparing results obtained with the proposed assay techniques and previously-used casein and fibrinolytic techniques are presented.4. Formulae by which caseinolytic-rate and fibrinolytic-rate units can be roughly converted into Remmert-Cohen type plasmin units are offered.5. The theoretical and practical problems which have influenced development of assays for fibrinolytic components are discussed.6. The advantages of the plasmin “rate unit” techniques vis a vis existing assays are delineated.7. The potential application of the techniques to measurements other than the plasmin content of fibrinolytic agents is discussed.


2006 ◽  
Vol 19 (2) ◽  
pp. 214-226
Author(s):  
Al-Ali M. F. M ◽  
Japer A. A. and Al-Moktar M. A

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