جستجوی مقالات مرتبط با کلیدواژه "gelatin" در نشریات گروه "شیلات"

First the required amount (150 kg) of waste were collected from fish processing centers and transferred to the laboratory. In the next step, it is washed with tap water, soda solution in a ratio of 1 to 10 for 2 hours, then were removed the solution and prepared to be placed in acetic acid solution in a ratio of 1 to 10 for three hours. After washing, the residue were thoroughly washed with tap water, in a ratio of 1 to 10 combined with distilled water in a steel container and placed inside the oven at a temperature of 60 degrees celsius. After 8 hours, the container was removed and the residue separated from it using a filter and cotton. The gelatin solutions were reduced to half volume using heat and concentrated, then the concentrated solution was poured into steel trays and placed in a dryer at a temperature of 50 degrees celsius. At the end, the dried gelatin flakes were transferred to the mill and powdered. In the final stage, they were sent to the standard laboratory for analyses. The obtained results indicated that the gelatins of sturgeon skin, head of sturgeon, and head of gidder fish have a more suitable physico-chemical, sensory and standard quality than other wastes and have the ability to be produced on a larger scale.

In this study, for the first time, lanternfish gelatin (Benthosema pterotum Alcock, 1890) was extracted and the composition (moisture, ash, protein), gel strength, gelling and melting temperature of extracted gelatin was investigated and compared with those of the commercial bovine gelatin purchased from market. The two gelatin samples were also compared in terms of color properties. Moisture and ash content of lantern fish gelatin were significantly higher than commercial gelatin. The result of measurement indicates that moisture and ash content of lantern fish gel were 8.2±0.1% and 3.2±0.1%, respectively. Protein content of the bovine gelatin (91.71±0.1 %) was significantly higher than lantern fish gelatin (86.3±0.1 %) (p<0.05). The gelling temperature and gelling time of the lantern fish gelatin (135 sec±2.0, 23±0.5°C), due to its low hydroxyproline content, was significantly lower than bovine gelatin (150 Sec±1.0, 26±0.5°C) which is due to fish gelatin nature. A significant difference between the gel strength of lantern fish (45±1.00 gr) and bovine gelatin (240±1.2 gr) was observed (p<0.05) and also bovine gelatin had better quality in terms of color factors than the gelatin extracted from lantern fish. Overall, lantern fish gelatin can be used in many biotechnological industries, as an economical and halal gelatin source, instead of pig and bovine gelatin.

The aim of the present study was to extract gelatin from the skin of farmed great sturgeon at different temperatures, hydrolysis using Alcalase enzyme, and to measure molecular weight distribution of peptides, amino acid composition and antioxidant activity of hydrolysates.

After removing pigments and non‐collagenous proteins, defatting, and swelling of triple‐helix structure, gelatin was extracted at the temperatures of 50, 60, 70, and 80°C for 6h and then hydrolysed using Alcalase (E/S ratio of 1:20w/w) for 3h. Molecular weight distribution of peptides, amino acid composition and antioxidant activity of hydrolysates were determined in different models.

Degree of hydrolysis (DH) reached its maximum within the first 30min in all samples. The highest DH was in the 80°C. There were no significant differences among hydrolysates with regards to amino acid composition and peptide molecular weight distribution. Hydrolysates produced at the extraction temperature of 60°C showed that the content of small peptides (molecular weight<1kDa) and total amino acids (g/100g) were slightly higher compared to other samples. This could influence antioxidant activity. At higher extraction temperature of gelatin, the efficacy of hydrolysates in preventing the loss in total sulfhydryl groups content was decreased (p<0.05) while there was no effect on TBARS and surface hydrophobicity (p<0.05).

Extraction temperature of gelatin did not reveal a considerable effect on properties and antioxidant activities of the resulting hydrolysates and gelatin hydrolysates with antioxidant activity and rich in peptides with molecular weight less than 1kDa could be produced at 50°C.

Fish gelatin, by benefiting the lower melting point, quicker mouth melting and presenting elastic characteristics is considered as the most proper substitute for mammalians gelatin and as a Halal food item. The aim of this study was to evaluate the effects of temperature at three levels of 30, 40 and 50 ºC, enzyme at 0.055%, 0.01% and 0.1% (w/w) levels and pH at 2, 3 and 4 levels on the quality of extracted gelatin from Huso huso fish skin. Accordingly, the gel strength in form of breaking force and distance, yield and color (L*a*b*) and whiteness of resultant gelatin were determined. According to the results, the highest gelatin yields as 21.65% was related to the enzymatic assisted method at 50 ºC, 0.01% enzyme at pH=2, whereas it was obtained as 10% at the chemical extraction method. Based on the results, despite from temperature, by increasing of pH and enzyme percentage, the firmness of gelatin was increased (p<0.05). The highest firmness was recorded at 30 ºC, 0.1% enzyme at pH=4. The color data revealed that lightness (L*), redness (a*) and whiteness of enzymatic extracted gelatin powder was higher that the chemical extracted one (p<0.05). The highest lightness was observed at 40 ºC, 0.055% enzyme at pH=3. In conclusion, by application of 30 ºC and 0.1% enzyme at pH=4 the highest gelatin with the highest firmness is achievable, while using 50 ºC and 0.01% enzyme at pH=2 could results the gelatin yield.