• 한국수산과학회지
• /
• 제41권6호
• /
• pp.419-426
• /
• 2008

Physicochemical characteristics of gelatin extracted from abdominal skin of yellowfin tuna (Thunnus albacares), were investigated by comparing its proximate composition, pH, amino acid composition, viscoelastic properties, gel strength and SDS-PAGE patterns, with those of bovine and porcine gelatins. The effects of gelatin concentration, maturation time, heat and freeze treatments on the gel strength of yellowfin tuna abdominal skin gelatin were studied. Amounts of $\alpha$-chains, $\beta$- and $\gamma$-components of yellowfin tuna abdominal skin gelatin were higher than those of the two mammailan gelatins. Yellowfin tuna abdominal skin gelatin had the lowest imino acids (proline and hydroxyproline) content, which was consistent with that of other fishes. However, yellowfin tuna abdominal skin gelatin was highest in glycine, alanine, and lysine. The gel strengths of all gelatins were proportional to the concentration of gelatin, but yellowfin tuna abdominal skin gelatin exhibited the greatest gel strength at each concentration. Yellowfin tuna abdominal skin gelatin required a longer maturation time than the two mammalian gelatins to form a firm gel. Higher heating temperature decreased the gel strength of yellow fin tuna abdominal skin gelatin more than in the two mammalian gelatins. Freezing decreased the gel strength of bovine gelatin only slightly, but longer freezing times resulted in greater reductions in gel strength in the yellowfin tuna abdominal skin and porcine gelatins.

• Fisheries and Aquatic Sciences
• /
• 제17권3호
• /
• pp.299-304
• /
• 2014

The objective of this study was to elucidate the physicochemical characteristics of gelatin extracted from jellyfish Rhopilema hispidum. We investigated the proximate composition, amino acids, gel strength, gelling/melting points, dynamic viscoelastic properties, and viscosity of jellyfish gelatin. Jellyfish gelatin contained 12.2% moisture, 1.5% lipid, 2.1% ash, and 84.8% protein. Glycine, hydroxyproline, proline, and alanine were the predominant amino acids. The gelatin showed a gel strength of 31.2 kPa, a gelling point of $18.0^{\circ}C$, and melting point of $22.3^{\circ}C$. The gelatin was composed of ${\alpha}_1$-chain, ${\alpha}_2$-chain, ${\beta}$-chain, and ${\gamma}$-chain. During cooling and heating process, jellyfish gelatin showed lower elastic modulus (G') and loss modulus (G") values than mammalian gelatin. Jellyfish gelatin did not show superior rheological properties to mammalian gelatin, like other fish gelatin; however, it can be used in various food and cosmetic products not requiring high gel strength.

• Asian-Australasian Journal of Animal Sciences
• /
• 제29권6호
• /
• pp.845-854
• /
• 2016

Characteristics and properties of gelatin from goat skin pretreated with NaOH solutions (0.50 and 0.75 M) for various times (1 to 4 days) were investigated. All gelatins contained ${\alpha}$-chains as the predominant component, followed by ${\beta}$-chain. Gelling and melting temperatures of those gelatins were $23.02^{\circ}C$ to $24.16^{\circ}C$ and $33.07^{\circ}C$ to $34.51^{\circ}C$, respectively. Gel strength of gelatins increased as NaOH concentration and pretreatment time increased (p<0.05). Pretreatment for a longer time yielded gelatin with a decrease in $L^*$-value but an increase in $b^*$-value. Pretreatment of goat skin using 0.75 M NaOH for 2 days rendered the highest yield (15.95%, wet weight basis) as well as high gel strength (222.42 g), which was higher than bovine gelatin (199.15 g). Gelatin obtained had the imino acid content of 226 residues/1,000 residues and the gelatin gel had a fine and ordered structure. Therefore, goat skin gelatin could be used as a potential replacer of commercial gelatin.

• 한국축산식품학회지
• /
• 제39권4호
• /
• pp.576-584
• /
• 2019

This study was performed to evaluate the physicochemical properties of myofibrillar protein (MP) gels containing pork skin gelatin at different salt concentrations. MP gels were prepared to the different salt levels (0.15, 0.30, and 0.45 M) with or without 1.0% of pork skin gelatin. Cooking yield (CY), gel strength, shear stress were measured to determine the physical properties, and SDS-polyacrylamide gel electrophoresis, scanning electron microscopy, fourier transform infrared spectroscopy, sulfhydryl group and protein surface hydrophobicity was performed to figure out the structural changes among the proteins. The addition of gelatin into MP increased CYs and shear stress. MP at 0.45 M salt level had the highest CY and shear stress, as compared to MPs at lower salt concentrations. As the salt concentration of MP gels increased, the microstructure became the compact and wet structures, and decreased the amount of ${\alpha}-helix$/unordered structures and ${\beta}-sheet$. MP with gelatin showed a decreased amount of ${\alpha}-helix$/unordered structures and ${\beta}-sheet$ compared to MP without gelatin. The addition of gelatin to MP did not affect the sulfhydryl group, but the sulfhydryl group decreased as increased salt levels. MP mixtures containing gelatin showed a higher hydrophobicity value than those without gelatin, regardless of salt concentration. Based on these results, the addition of gelatin increased viscosity of raw meat batter and CY of MP gels for the application to low salt meat products.

• 한국축산식품학회지
• /
• 제39권2호
• /
• pp.229-239
• /
• 2019

The objectives of this study were to determine the interaction between porcine myofibrillar proteins and various gelatins (bovine hide, porcine skin, fish skin, and duck skin gelatins) and their impacts on gel properties of porcine myofibrillar proteins. Porcine myofibrillar protein was isolated from pork loin muscle (M. longissimus dorsi thoracis et lumborum). Control was prepared with only myofibrillar protein (60 mg/mL), and gelatin treatments were formulated with myofibrillar protein and each gelatin (9:1) at the same protein concentration. The myofibrillar protein-gelatin mixtures were heated from $10^{\circ}C$ to $75^{\circ}C$ ($2^{\circ}C/min$). Little to no impacts of gelatin addition on pH value and color characteristics of heat-induced myofibrillar protein gels were observed (p>0.05). The addition of gelatin slightly decreased cooking yield of heat-induced myofibrillar protein gels, but the gels showed lower centrifugal weight loss compared to control (p<0.05). The addition of gelatin significantly decreased hardness, cohesiveness, gumminess, and chewiness of heat-induced myofibrillar gels. Further, sodium dodecyl poly-acrylamide gel electrophoresis (SDS-PAGE) showed no interaction between myofibrillar proteins and gelatin under non-thermal conditions. Only a slight change in the endothermic peak (probably myosin) of myofibrillar protein-gelatin mixtures was found. The results of this study show that the addition of gelatin attenuated the water-holding capacity and textural properties of heat-induced myofibrillar protein gel. Thus, it could be suggested that well-known positive impacts of gelatin on quality characteristics of processed meat products may be largely affected by the functional properties of gelatin per se, rather than its interaction with myofibrillar proteins.

• KSBB Journal
• /
• 제10권2호
• /
• pp.166-169
• /
• 1995

감 자 Rhizoctoηia stem canker 방 제 용 의 Trichoderma harzianum A Tee 52445 의 포자를 각종 천연담체에 고정화시킨 후 발아율과 강도 벚 점착성 등의 물성을 조사하였다. 천연담체 중 gelatin과 감자 전분 젤에 포자를 고정화시켰을 때 각각 2.81 % 와 2.90%의 발아율을 보였고 강도와 점착성은 감자 전분 고정화 겔보다 gelatin 고정화 겔이 우수하였 다 .. Gelatin에 몇 종의 물성 이 우수한 담체를 섞 어 서 만든 혼합담체에 포자를 고정화시 켰을 경우 물성 은 개선이 되었으냐 발아율은 오히려 낮아졌고 1% 의 corn steep liquor를 gelatin에 첨가하여 포자를 고정화시켰을 때 말아율이 약 0.6% 상승되었다.

• 폴리머
• /
• 제30권6호
• /
• pp.563-567
• /
• 2006

생체 적합성이 우수한 gelatin(GEL)과 기계적 물성이 뛰어난 poly(vinyl alcohol)(PVA)로 이루어진 블렌드막을 $3{\sim}10kV$의 고전장하에서 용액 캐스팅 법에 의해 제조하였고, 막중에 형성되는 미세한 domain 구조의 배향에 미치는 전장의 효과를 조사하였다. 5 kV이상의 높은 전장하에서 제조된 막의 경우 SEM 사진으로부터 막중의 GEL domain이 전장인가 방향으로 배향되어 있음을 관찰하였다. 이는 제막 중 상분리된 두 상의 계면장력 감소에 기인한 Maxwell의 정전 분산 효과에 의한 것으로 해석될 수 있다. 또한, 고전장 인가시 전극 판에서 발생하는 열과 GEL domain의 연신 배향 효과에 의해 PVA/GEL 블렌드막의 결정화도가 증가하는 것을 WAXD와 팽윤거동 관찰을 통해 확인 할 수 있었다.

• 한국식품과학회지
• /
• 제34권5호
• /
• pp.911-915
• /
• 2002

닭발에서 추출한 젤라틴을 이용하여 후식용 gel을 제조하기 위한 향신료 수준을 결정하기 위하여 설탕, 구연산 및 딸기향의 수준을 달리하여 gel을 제조하고 소비자기호도검사를 수행한 결과는 다음과 같다. 전체적 기호도, 단맛, 신맛, 및 향의 기호도 모두 향신료에 의한 선형효과 및 순수 2차 효과가 나타나 향신료의 일정수준까지는 모든 항목의 기호도가 증가하다가 그 이후에는 감소하는 경향을 나타내었다. 이와 같은 결과를 고려하여 후식용 젤라틴 gel 제조를 위한 최적 배합비를 설탕 19%, 구연산 0.50%, 딸기향 0.35%로 결정하였다.

• 한국식품과학회지
• /
• 제27권4호
• /
• pp.483-486
• /
• 1995

가공적성이 우수한 알코올처리 각시가자미껍질 젤라틴을 식품산업소재로 이용하기 위한 기초자료를 얻을 목적으로 젤라틴농도, pH, 정치온도 및 시간과 같은 겔화조건에 대한 알코올처리 젤라틴의 물리적 특성 및 색조의 변화를 알코올 무처리 젤라틴과 비교하여 검토하였다. 알코올처리 및 무처리 젤라틴이 모두 농도가 증가할수록 겔강도, 졸화온도 및 겔화온도 및 점도 등과 같은 물리적 특성은 증가하였다. 젤라틴 졸의 pH가 에탄올처리한 젤라틴의 경우 6.0일 때, 무처리한 젤라틴의 경우 5.0일 때 겔강도, 졸화온도 및 겔화온도가 가장 높았으나, $pH\;5.0{\sim}8.0$의 범위에서는 거의 차이가 없었고, pH 5.0 이하 및 pH 9.0 이상에서는 급격히 감소하였다. 젤라틴 졸을 겔화시키기 위하여 정치시키는 경우 온도는 낮을수록, 시간은 길수록 겔강도 및 졸화온도는 높았다. 겔화조건을 동일하게 하였을 때 에탄올처리한 젤라틴이 무처리한 젤라틴보다 물리적 특성이 우수하였다.

• 한국축산식품학회지
• /
• 제43권1호
• /
• pp.61-72
• /
• 2023

The practical use of Korean native black goat skin as a source of gelatin extraction is limited. The objective of this study was to optimize the extraction temperature and time of gelatin from Korean native black goat skin, and to compare the quality characteristics of goat skin gelatin and other commercial gelatin products. Response surface methodology was applied to optimize the extraction temperature and time of gelatin obtained from native Korean black goat skin. The effects of temperature (50℃-70℃) and time (2-4 h) on extraction yield and gel strength were investigated using a face-centered central composite design with 13 experiments. Gelatin extraction from Korean native black goat skin was prepared through the serial processes of alkali pre-treatment, bleaching, neutralization, hot-water extraction, and freeze-drying. Using the optimization plot of Minitab software, the optimized conditions for extracting temperature and time of goat skin gelatin were 59.49℃ and 3.03 h, and the optimized values of extraction yield and gel strength were 12.52% and 263.37 g, respectively. Based on a quality comparison of goat skin gelatin with commercial gelatin, the pH value of gelatin extracted from Korean native black goat skin was 5.57. The color of gelatin extracted from Korean native black goat skin was darker than that of commercial gelatin (p<0.05). Higher emulsifying properties and gel strength of goat skin gelatin were observed when compared to those of commercial gelatin (p<0.05). Therefore, the results of this study indicate that Korean native black goat skin may be a valuable source for gelatin extraction.