• Title/Summary/Keyword: flounder skin gelatin

Search Result 3, Processing Time 0.021 seconds

Investigation of Pretreatment Method for Gelatin Preparation from Flounder Skin (가자미피(皮) 젤라틴 제조를 위한 전처리 방법의 검토)

  • KANG Tae-Jung;JEON You-Jin;KIM Se-Kwon;SONG Dae-Jin
    • Korean Journal of Fisheries and Aquatic Sciences
    • /
    • v.25 no.2
    • /
    • pp.93-102
    • /
    • 1992
  • In order to reduce long preparating time for alkali pretreated B-type gelatin, enzyme pretreatment was tried on flounder(Limanda aspera) skin for I-type gelatin. The optimal extraction conditions of the B-type gelatin were 9 folds of added water with material(w/w), 3 hrs of extraction time, $60^{\circ}C$ of extraction temperature and pH 5. The maximum amount of I-type gelatin was extracted at $60^{\circ}C$ for 3 hrs using water controlled to pH 6.0(material : water= 1:9, w/w). The yields of the B- and E-type gelatin were $64.2\%\;and\;59.2\%,$ respectively. The B-type was superior to the B-type in physical properties such as jelly strength, viscosity and electric conductivity. Molecular weight of B-type was so far larger than that of the E-type due to different pretreatment method. Hydrolysis ratio of the E-type was higher than that of the B-type because of its molecular weight. Results suggest that B-type product would be better than I-type as fish skin gelatin but E-type was desirable in hydrolyzate preparation.

  • PDF

A Trial for Utilizing Flounder Skin Gelatin as an Emulsifier through Enzymatic Modification (가자미피 젤라틴의 효소적 수식에 의한 유화제의 시제)

  • KIM Se-Kwon;JEON You-Jin
    • Korean Journal of Fisheries and Aquatic Sciences
    • /
    • v.24 no.5
    • /
    • pp.345-355
    • /
    • 1991
  • In order to effectively utilize the by-products of sea-food, the utilization of enzyme-modified flounder(Limanda aspera) skin gelatin as an emulsifier was investigated. In the experiment, the gelatin was extracted from the flounder skin with the heat-treatment at $60^{\circ}C$ and in pH 5.0 for 3 hrs with four volumes of distilled water and emulsifiers were enzymatically modified L-leucine alkyl esters$(L-leucine-OC_n$ : n= 2, 4, 6, 8 and 10) to the gelatin$(EMFSG-C_2,\;EMFSG-C_4,\;EMFSG-C_6,\;EMFSG-C_8,\;EMFSG-C_{10})$ for improving the functional properties such as emulsifying activity, emulsifying viscosity, whippability, electric conductivity, critical micelle concentration and interface tension, etc. Also, the functional properties of the L-leucine alkyl ester modified gelatins were compared with those of Tween-60 as reference. Molecular weights of the enzymatically modified flounder skin gelatin(EMFSG) were 20.5kDa. in $EMFSG-C_2.\;19.5 kDa.\;in\;EMFSG-C_4\;and\;16.5kDa.\;in\;EMFSG-C_6,\;EMFSG-C_8$ and $EMFSG-C_{10}$. respectively. Emulsifying activity and emulsifying viscosity in the modified gelatins were risen with increase of carbon number of the introduced L-leucine alkyl esters. Among the modified gelatins, $EMFSG-C_6$ exhibited the highest emulsifying stability and foaming stability, whereas $EMFSG-C_8$ showed the highest whippability. The electric conductivities of the all $EMFSG-C_n$ were linearly risen to critical micelle concentration(CMC) , therefore $EMFSG-C_{10}$ exhibited the lowest CMC value and interface tension, and dense particles in the microscopic observation. In conclusion, the best quality in functional properties was assured on $EMFSG-C_{10}$.

  • PDF

Proteolytic Conditions for the Hydrolysate of Flounder Skin Gelatin (효소에 의한 가자미피 젤라틴 가수분해물의 제조 조건)

  • 강태중;양현필;김세권;송대진
    • Journal of the Korean Society of Food Science and Nutrition
    • /
    • v.21 no.4
    • /
    • pp.398-406
    • /
    • 1992
  • In order to develop a new flavourant using the fish skin gelatin, the proteolytic renditions for the gelatin hydrolysate of the alkali (B-type) and Alcalase (E-type) pretreated flounder (Limanda aspera) skin gelatin were investigated, and some physical properties, molecular weight and amino acid compositions of the hydrolysates were, also, compared with each other. The proteolytic conditions of the gelatins (B-type and E-type) by trypsin were as follows : reaction temperature, 55$^{\circ}C$ : pH, 9.0 : enzyme concentration, 0.1% : re-action time, 4hrs for B-type and 1 hr for E-type. The degrees of hydrolysis of the B-type and E-type gelatin un-der the renditions stated above were 63% and 82%, respectively. The rnajor molecular weights of the hydrolysates were 15,000 dalton for B-type and 12,400 dalton for E-type. Among the amino acids in the hydrolysates, glycine, alanine, proline, hydroxyproline and serine having a sweet taste were responsible for 57% of the total amino acid. But valine, leucine, phenylalanine, tyrosine, methionine, arginine and histidine having a bitter taste were only 18%.

  • PDF