• Journal of Animal Science and Technology
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• 제62권4호
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• pp.533-542
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• 2020

The objective of this study was to observe the interactions between salt-soluble proteins extracted from beef and elephant foot yam (Amorphophallus campanulatus) flour in heat-induced gel matrix development. The effect of salt concentration; 0.5%, 1.0%, 1.5%, and 2.0% in weight/weight basis (w/w), during protein extraction on pH, salt-soluble protein concentration and myofibril fractions of beef extract was determined firstly, and no significant effect was found. The beef salt-soluble proteins extracted using salt solution at different concentrations were then added with elephant foot yam flour at 5%, 10%, and 15% w/w, gelatinized at 90℃ for 20 min, and cooled down at 4℃ for 12 h. The interactions between beef salt-soluble proteins and elephant foot yam flour resulted in an improved gel strength (p < 0.01) and the addition level of elephant foot yam flour affected the pH, instrumental color, moisture, crude protein, and ash content significantly. The addition of elephant foot yam flour also reduced the size of the pores in the gel matrix as shown by scanning electron microscope (SEM) photographs. These suggest that elephant foot yam flour well interacts with beef salt-soluble proteins to form gel matrix.

• Preventive Nutrition and Food Science
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• 제10권4호
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• pp.378-381
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• 2005

Actin and myosin solutions and fresh ground pork were irradiated with the electron beam (e-beam) at a dose of 0, 1.5, 3.0, 5.0 and 10 kGy. The changes in SDS-PAGE pattern of 2 proteins and the salt-soluble proteins extracted from ground pork after e-beam irradiation were monitored. When the myosin solution was irradiated with e-beam, myosin was degraded completely. Complete myosin degradations were observed even with the lowest dose (1.5 kGy) of e-beam treatment. Actin was degraded with the irradiation, but to a less extent than myosin was. The degradation of actin increased as the e-beam treatment increased from 1.5 to 10.0 kGy. Among the salt-soluble proteins extracted from ground pork, myosin was degraded gradually when the e-beam dose increased from 1.5 up to 10.0 kGy. Similar gradual increase in the degradation of actin also occurred with the increase of irradiation. Increases of 2 low molecular weight compounds (<29 kDa) were observed when the irradiation dose increased from 1.5 to 10.0 kGy. These 2 molecules are thought to be the breakdown products produced from the degradation of major salt-soluble proteins, myosin and actin. The salt-soluble protein content of ground pork did not change with the e-beam irradiation.

• 한국식품과학회지
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• 제23권6호
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• pp.695-701
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• 1991

0.05 M 중탄산 나트륨 및 0.04 M 인산염 완충용액 (pH 8.3)으로 처리한 노계육 가슴살 및 다리살 시료의 경우 근섬유 단백의 불안정화를 시사하는 열변성 온도의 저하가 관찰되었다. 이러한 현상을 근섬유 단백중 95 Kdalton 및 55 Kdalton protein의 추출과 관련 가능성이 있는 것으로 판단되었으며 처리 시료의 근섬유구조 변화(Z-line의 파괴)와도 관련 가능성이 있는 것으로 판단되었다.

• 한국축산식품학회지
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• 제34권4호
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• pp.464-471
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• 2014

Ground lean pork was irradiated by an electron beam or X-rays to compare the effects of two types of radiation generated by a linear accelerator on the quality of Bologna sausage as a model meat product. Raw ground lean pork was vacuum packaged at a thickness of 1.5 cm and irradiated at doses of 2, 4, 6, 8, or 10 kGy by an electron beam (2.5 MeV) or X-rays (5 MeV). Solubility of myofibrillar proteins, bacterial counts, and thiobarbituric acid reactive substance (TBARS) values were determined for raw meat samples. Bologna sausage was manufactured using the irradiated lean pork, and total bacterial counts, TBARS values, and quality properties (color differences, cooking yield, texture, and palatability) were determined. Irradiation increased the solubility of myofibrillar proteins in a dose-dependent manner (p<0.05). Bacterial contamination of the raw meat was reduced as the absorbed dose increased, and the reduction was the same for both radiation types. Differences were observed only between irradiated and non-irradiated samples (p<0.05). X-ray irradiation may serve as an alternative to gamma irradiation and electron beam irradiation.

• 한국축산식품학회지
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• 제44권3호
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• pp.551-569
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• 2024

This study was conducted to compare and analyze the changes in the biochemical characteristics and biological activity of peptide extracts derived from Chickso, Hanwoo, and Wagyu beef during digestion. The results of the in vitro digestion analysis revealed that the digestion rate, total free amino acid content, and antioxidant and antihypertensive activities of Chickso loin and shank myofibrillar proteins were significantly higher (p<0.05) than those of Hanwoo and Wagyu loin and shank myofibrillar proteins. Particularly, the peptide extracts of Chickso loin and shank had a high angiotensin-converting enzyme inhibitory activity. In mice in vivo digestion experiment, the blood serum of mice fed with Chickso loin peptide extract (<10 kDa) showed the highest antioxidant enzyme activity. Thus, Chickso peptide extracts were deemed to be similar or more bioactive than Hanwoo and Wagyu peptide extracts, and can be used as bioactive materials.

• 한국축산식품학회지
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• 제34권2호
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• pp.207-213
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• 2014

This study investigated the effects of microbial transglutaminase (MTGase) and pH-shift processing on the functional properties of porcine myofibrillar proteins (MP). The pH-shift processing was carried out by decreasing the pH of MP suspension to 3.0, followed by re-adjustment to pH 6.2. The native (CM) and pH-shifted MP (PM) was reacted with and without MTGase, and the gelling and emulsion characteristics were compared. To compare the pH-shifted MTGase-treated MP (PT), deamidation (DM) was conducted by reacting MTGase with MP at pH 3.0. Rigid thermal gel was produced by MTGase-treated native MP (CT) and PT. PM and DM showed the lowest storage modulus (G') at the end of thermal scanning. Both MTGase and pH-shifting produced harder MP gel, and the highest gel strength was obtained in PT. All treatments yielded lower than CM, and CT showed significantly higher yield than PM and DM treatments. For emulsion characteristics, pH-shifting improved the emulsifying ability of MP-stabilized emulsion, while the treatments had lower emulsion stability. PM-stabilized emulsion exhibited the lowest creaming stability among all treatments. The emulsion stability could be improved by the usage of MTGase. The results indicated that pH-shifting combined with MTGase had a potential application to modify or improve functional properties of MP in manufacturing of meat products.

• Asian-Australasian Journal of Animal Sciences
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• 제15권5호
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• pp.721-724
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• 2002

Postmortem Proteolysis of breast (BM) and leg (LM) muscles in Chiayi native chickens at $5^{\circ}C$ were compared. Myofibrils were purified from BM and LM samples that were randomly taken from carcasses after 0, 1, 3, 7 and 14 days of storage at $5^{\circ}C$. Fragmentation of myofibrils were determined, and degradation of myofibrillar proteins were analyzed by the SDS-PAGE and western blots. The results showed that myofibril fragmentation index (MFI) was significantly (p<0.05) higher in BM than in LM samples. Disappearance of titin and nebulin and appearance of the 30 kDa component were more rapidly as seen on SDS-PAGE in BM than in LM samples. Western blots labeled with a monoclonal antibody to desmin also demonstrated that desmin degraded more quickly in BM samples. Our data suggested that postmortem proteolysis occurred more rapidly in breast muscles in Chiayi native chickens.

• 한국식품영양학회지
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• 제16권3호
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• pp.209-217
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• 2003

동면어 짱뚱어에 대해 월동전ㆍ후(성숙기: 8월, 동면직전: 11월, 동면직후: 4월) 육단백질과 유리아미노산 조성 등을 각 시기별로 비교, 검토하였다. 조단백질 함량은8월 17.8%, 11월 17.5%, 4월 16.9%이었고 근원질 단백질은 육단백질 전체의 19.2～20.4%, 근원섬유 단백질은 58.8～61.3%, 세포내 잔사단백질과 기질단백질은 각각 11.2～13.2%와 7.5～8.3%를 차지하였다. 단백질 조성을 시기별로 비교한 결과 11월까지는 거의 차이가 없으나 4월은 기질단백질을 제외한 근원질과 근원섬유단백질 2종이 소량 줄었고 조성비로 근원질단백의 감소가 조금 더 큰 것으로 파악되었다. 근원질단백 구성 subunit는 총 14종이 검출되었고 구성 subunit 중 30kDa와 46kDa등의 조성이 11월보다 4월에 소폭 증가하였고 35kDa, 65kDa 등은 소폭 감소하였으나 기타 대부분은 거의 차이가 없었다. 근원섬유단백질은 총 13개의 subunit가 검출되었고 대부분의 subunit 조성이 11월까지는 거의 비슷하였으나 4월은 동면전보다 myosin heavy chain 조성이 3% 정도 늘어난 반면 actin은 3%정도 줄어들었다. 단백질 구성 아미노산 조성은 전기간에 걸쳐 일정하였고 주요 유리아미노산은 glycine과 alanine이었으며 두드러진 특징은 arginine함량이 8월보다 11월이 2배, 4월은 4배 이상 늘었고 glycine도 8월보다 4월이 2배 함량으로 모든 아미노산 중 양적 증가가 가장 현저하였다. 기타 alanine, glutamic acid, serine 및 aspartic acid와 valine 등도 동면기간 상당폭으로 증가하였고 lysine, histidine 등의 필수아미노산 함량도 유의적으로 증가하였다.

• 한국수산과학회지
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• 제19권4호
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• pp.333-338
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• 1986

우리 나라 전역에 걸쳐 널리 분포하고 있는 붕어와 가물치의 영양학적 기초자료를 제공하기 위하여 단백질, 구성아미노산 및 유리아미노산의 조성을 분석하고, 육단백질중 근형질단백질과 근원섬유단백질은 SDS-polyacrylamide gel 전기영동하여 그 구성 sub-unit를 검토하였다. 가물치는 붕어에 비하여 조단백질의 함량이 $3\%$가량 높았으며 Ex 분의 함량 또한 월등히 많았다. 육 단백질을 구성하는 단백질 조성은 붕어의 경우 근형질 단백질이 $32.6\%$, 근원섬유 단백질이 $62.0\%$, 알칼리가용성 단백질이 $4.9\%$, 기질 단백질이 $0.6\%$이었으며, 가물치는 근형질 단백질이 $30.7\%$, 근원섬유 단백질이 $64.1\%$, 알칼리가용성 단백질이 $4.7\%$, 기질 단백질이 $0.4\%$를 차지하고 있었다. 근형질 단백질과 근원섬유 단백질 분획의 일부에 대하여 구성 subunit를 분석한 결과, 붕어의 근형질단백질은 10개의 subunit로 구성되어 있었고, 가물치는 12개의 subunit로 구성되어 있었다. 한편 근원직유 단백질은 붕어가 19개의 subunit이었으며, 가물치는 18개 subunit로 이루어져 있었다. 단백질의 구성아미노산 조성은 lysine과 glutamic acid를 제외하고는 대체로 붕어와 가물치가 비슷한 편이었으며, glutamic acid, lysine, aspartic acid 및 arginine이 전체 구성아미노산의 약 $46\%$를 차지하고 있었다. 또한 유리아미노산조성에 있어서 붕어는 histidine이 전체유리아미노산의 $52.2\%$를 차지하고 있었으며, 가물치는 glutamic acid, glycine와 taurine이 전체유리아미노산의 약 $84.5\%$를 차지하였다. 그리고 총 유리아미노산의 양에 있어서 가물치는 붕어의 약 6.2배에 달하였다.

• Journal of Animal Science and Technology
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• 제58권6호
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• pp.23.1-23.17
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• 2016

Background: The functionality of myofibrillar proteins is a major factor influencing the quality attributes of muscle foods. Nonetheless, the relationships between muscle type and oxidative changes in chevon during ageing are meagrely elucidated. Postmortem changes in antioxidant status and physicochemical properties of glycolytic gluteus medius (GM) and oxidative infraspinatus (IS) muscles in goats were compared. Methods: Twenty Boer bucks (9-10 months old, body weight of $36.9{\pm}0.725kg$) were slaughtered and the carcasses were subjected to chill storage ($4{\pm}0.5^{\circ}C$). Analyses were conducted on GM and IS muscles sampled on 0, 1, 4 and 7 d postmortem. Results: Chill storage did not affect the antioxidant enzyme activities in both muscles. The IS had greater (P < 0.05) superoxide dismutase and catalase activities than GM. Carotenoid and tocopherol contents did not differ between muscles but decreased (P < 0.05) over storage. The IS had higher (P < 0.05) glycogen and ultimate pH and lower (P < 0.05) shear force and cooking loss than GM. The carbonyl content, % metmyoglobin, drip loss and TBARS increased (P <0.05) while free thiol, metmyoglobin reducing activity (MRA), shear force and myoglobin decreased (P < 0.05) over storage. Muscle type had no effect (P > 0.05) on free thiol, MRA and TBARS. The GM had lower (P < 0.05) redness on d 0 and 1 than IS while the IS had greater carbonyl, % metmyoglobin and drip loss than GM on d 7. The reflective density of slow myosin heavy chain (MHC) was higher (P < 0.05) while the density of fast MHC and actin was lower (P < 0.05) in IS than GM. Regardless of muscle type, the density of MHC decreased (P < 0.05) while that of actin was stable over storage. Nonetheless, the degradation of fast and slow MHC was greater (P < 0.05) in IS than GM. Muscle type had no effect (P > 0.05) on consumer preference for flavour, juiciness and overall acceptability. However, IS had higher (P < 0.05) tenderness score than GM on d 1 and 4 postmortem. Intramuscular fat was higher (P< 0.05) in IS compared with GM. Fatty acid composition did not differ between the muscles. However, GM had lower (P < 0.05) n-6/n-3 ratio than IS. The n-3 and n-6 PUFA declined (P < 0.05) while the SFA increased (P < 0.05) over storage. Conclusion: The changes in myofibrillar proteins and physicochemical properties of goat meat during postmortem chill storage are muscle-dependent.