• Applied Biological Chemistry
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• v.39 no.5
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• pp.361-367
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• 1996

As a part of investigation for quality improvement of surimi gel from fish with a red muscle by addition of emulsion curd, we investigated the processing conditions of emulsion curd contained succinylated gelatin from conger eel skin as an emulsifier and emulsion curd-added surimi gel. Activity and stability of emulsion curd on standing at room temperature, chilled temperature and vibration were remarkably improved by the addition of 15 tunes of soybean oil and 5 times of water to succinylated gelatin from conger eel skin. The proximate composition of the emulsion curd was moisture 18%, protein 5%, lipid 76% and ash 0.5% and its appearance was white. Peroxide value and fatty acid composition of emulsion curd contained succinylated gelatin as an emulsifier were similar to these of soybean oil. By the addition of 6% of emulsion curd to mackerel surimi, gel strength, appearance and texture of the resulting surimi gel were improved, while its peroxide value and brown pigment revealed minor change. From the results of volatile basic nitrogen, viable cell counts and histamine content, the emulsion curd-added mackerel surimi gel can be safe In the sense of food sanitation.

• Journal of Pharmaceutical Investigation
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• v.37 no.2
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• pp.113-117
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• 2007

The aim of this study was to investigate the effect of different wall material on the microencapsulation efficiency of microcapsules containing fish oil. The present work reports on the microencapsulation of fish oil by spray drying using hydroxypropyl methylcellulose (HPMC) 2910, maltodextrin, gelatin, sodium caseinate as wall materials. The emulsion stability was assessed by emulsion stability index value (ESI). The microstructural properties of microcapsules was evaluated by scanning electron microscopy (SEM) and microencapsulation efficiency (ME) was assessed by soxhlet method. The highest ESI and ME were observed in the case of a 1:1 gelatin/sodium caseinate ratio and 1:1 glycerin fatty acid ester/lecithin ratio, and ME of microcapsules was increased with increasing the ESI of emulsion. Thus, the stability of emulsion was a critical factor for the encapsulation of fish oil.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.25 no.2
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• pp.93-102
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• 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.

• Food Science of Animal Resources
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• v.39 no.2
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• pp.229-239
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• 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.

• Journal of Food Hygiene and Safety
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• v.32 no.4
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• pp.254-261
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• 2017

Determining the origin of the components in commercially available gelatin, a purified protein derived mostly from pig skin and bovine tissue, is a challenge, leading to concerns on the grounds of religious beliefs and health. Therefore, regular monitoring of labeling compliance by food control authorities is also necessary. In this study, we monitored the origin of gelatin capsules from 181 commercial dietary supplements that were available for purchase on the internet, using species-specific PCR assays. Fifty five products were labeled correctly, declaring that they used bovine-, fish- and plant-derived gelatin, whereas the other 126 capsules were labeled "gelatin" without specifying the origin. Gelatin in these capsules was obtained from cattle (n = 51), pigs (n = 31), or both (n = 44). Therefore, it is important to declare all of the raw materials used to produce gelatin capsules on the labels to best protect consumers' rights, religious beliefs, and health.

• Applied Biological Chemistry
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• v.38 no.5
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• pp.393-397
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• 1995

With a view to utilizing fish skin gelatin as a clearifier or chewing gum base, yellowfin sole skin gelatin was succinylated. Up to 10% succinic anhydride to gelatin, the succinylation degree of gelatin was increased linear and above this concentration a nearly constant value was reached. The succinylated gelatin treated with 15% succinic anhydride to gelatin was examined on the reactivity properties with tannic acid in the experiment. Succinylation degree of the gelatin was about 80%. Succinylation shifted the apparent isoelectric point from pH 5.54 in untreated gelatin to pH 4.08 in succinylated gelatin. The proximate composition and amino acid composition of succinylated gelatin were similar to those of untreated gelatin. However Lysine composition for succinylated gelatin was lower than for untreated gelatin. The ratio of precipitated gelatin and tannic acid became maximum at pH 4.8 in untreated gelatin, at pH 4.0 in succinylated gelatin. Regardless of the difference between untreated and succinylated gelatins, the ratio of precipitated gelatin decreased with concentration of gelatin. The ratio of precipitated tannic acid was the highest by adding $2{\sim}4$ times in succinylated gelatin to tannic acid weight, by adding $2{\sim}3$ times in untreated gelatin. The ratios of precipitated succinylated gelatin and tannic acid were scarcely affected by the presence of sucrose, however, were affected by the presence of ethyl alcohol.

• Applied Biological Chemistry
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• v.39 no.2
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• pp.134-139
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• 1996

In order to effectively utilize marine animal skin wastes in marine processing manufacture, conger eel skin, file fish skin and arrow squid skin as raw material of edible gelatin were screened. Conger eel skin was the highest in the collagen content, followed by Ole fish skin and arrow squid skin, in the order named. In the fish skins, the soluble and insoluble collagens occupied $67.4%{\sim}72.3%\;and\;27.7{\sim}32.6%$, respectively, and in the arrow squid skin, 30.4ft and 69.6ft, respectively. No difference in the amino acid composition between soluble and insoluble collagens was detected. Collagen from the marine animal skin catched in coasted and offshore water in Korea consisted ${\alpha}$ chain and ${\beta}$ chain, and ${\alpha}$ chain were hetero type. The sum of proline and hydroxyproline contents in conger eel skin collagen was higher than that in the other skin collagens, while was lower than that pork skin collagen. Conger eel skin collagen exhibited a higher denaturation temperature in solution and a higher degree of proline hydroxylation, compared with skin collagen of the respective species. The physical properties such as gel strength, melting point and gelling point of conger eel skin gelatin were superior to those of file fish skin and arrow squid skin gelatins.

• Fisheries and Aquatic Sciences
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• v.13 no.1
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• pp.1-11
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• 2010

The study was performed to optimize the processing conditions (alkali concentration, extraction time, and temperature) for rockfish skin gelatin based on yield using response surface methodology and comparison of the physicochemical properties with those of rockfish skin gelatin pretreated and extracted under ordinary conditions (alkali treatment concentration: 1.0 M; extraction time: 2 hr; extraction temperature: $60^{\circ}C$). Predicted maximum gelatin yield of 19.1% and gelatin content of 87.8% were obtained by extraction at $106.6^{\circ}C$ for 69.0 min after pretreatment with 1.1 M calcium hydroxide. Yield of gelatin extracted under high temperature/high pressure (G-HT/HP) was 54% higher than that extracted under ordinary temperature/time (G-OT/T). However, G-HT/HP was inferior in gel strength and gelling point to (G-OT/T), but comparable in transmission. Based on the physicochemical properties, G-HT/HP was unsuitable for use in products requiring higher physical properties, but could be useful for health-functional foods.

• Journal of fish pathology
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• v.31 no.2
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• pp.87-92
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• 2018

A case of disease was occurred in tiger puffer, Takifugu rubripes, reared in circulated system (water temperature was about $20^{\circ}C$) on land in Korea. Diseased fish showed a unique external sign, the cloudy skin ulcer in various sizes. We investigated the cause of disease, and isolated one pure cultured bacterium, TP01. This had 99.7% homology with Vibrio atlanticus by sequence analysis of the 16S rRNA and rpoA genes. TP01 showed some differences with other reported V. atlanticus strains in the biochemical characteristics as like Voges-Proskauer test and gelatin hydrolysis.

• Fisheries and Aquatic Sciences
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• v.22 no.5
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• pp.10.1-10.14
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• 2019

Fish skin waste accounts for part of the solid waste generated from seafood processing. Utilization of fish skin by bioconversion into high-grade products would potentially reduce pollution and economic cost associated with treating fish processing waste. Fish skin is an abundant supply of gelatin and collagen which can be hydrolyzed to produce bioactive peptides of 2-20 amino acid sequences. Bioactivity of peptides purified from fish skin includes a range of activities such as antihypertensive, anti-oxidative, antimicrobial, neuroprotection, antihyperglycemic, and anti-aging. Fish skin acts as a physical barrier and chemical barrier through antimicrobial peptide innate immune action and other functional peptides. Small peptides have been demonstrated to possess biological activities which are based on their amino acid composition and sequence. Fish skin-derived peptides contain a high content of hydrophobic amino acids which contribute to the antioxidant and angiotensin-converting enzyme inhibitory activity. The peptide-specific composition and sequence discussed in this review can be potentially utilized in the development of pharmaceutical and nutraceutical products.