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      KCI등재 SCIE SCOPUS

      The Effect of Age on the Myosin Thermal Stability and Gel Quality of Beijing Duck Breast

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      https://www.riss.kr/link?id=A106978989

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      다국어 초록 (Multilingual Abstract)

      The effect of age (22, 30, 38, and 46 days) on Beijing duck breast myosin gels was investigated. The results showed that the water holding capacity (WHC) and gel strength were markedly improved at the age of 30 days. Differential scanning calorimetry ...

      The effect of age (22, 30, 38, and 46 days) on Beijing duck breast myosin gels was investigated. The results showed that the water holding capacity (WHC) and gel strength were markedly improved at the age of 30 days. Differential scanning calorimetry suggested that the myosin thermal ability increased at the age of 30 and 38 days (p<0.05). A compact myosin gel network with thin cross-linked strands and small regular cavities formed at the age of 30 days, which was resulted from the higher content of hydrophobic interactions and disulfide bonds. Moreover, the surface hydrophobicity of myosin extracted from a 30-day-old duck breast decreased significantly under temperature higher than 80℃ (p<0.05). This study illustrated that myosin extracted from a 30-day-old duck’s breast enhanced and stabilized the WHC, thermal stability and molecular forces within the gel system. It concluded that age is an essential influencing factor on the myosin thermal stability and gel quality of Beijing duck due to the transformation of fibrils with different myosin character.

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      목차 (Table of Contents)

      • Introduction Materials and Methods Results Discussion Conclusion Conflicts of Interest Acknowledgements Author Contributions Ethics Approval References
      • Introduction Materials and Methods Results Discussion Conclusion Conflicts of Interest Acknowledgements Author Contributions Ethics Approval References
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      참고문헌 (Reference)

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      2 Liu G, "Thermal aggregation properties of whey protein glycated with various saccharides" 32 : 87-96, 2013

      3 Chan JK, "Thermal aggregation of myosin subfragments from cod and herring" 58 : 1057-1061, 1993

      4 Sharp A, "The mechanism of formation of gels from myosin molecules" 58 : 63-73, 1992

      5 Polidori P, "The effects of slaughter age on carcass and meat quality of fabrianese lambs" 155 : 12-15, 2017

      6 Pan T, "The effects of calcium chloride on the gel properties of porcine myosin–κ-carrageenan mixtures" 63 : 467-477, 2017

      7 Zhou CU, "The effect of cooking temperature on the aggregation and digestion rate of myofibrillar proteins in jinhua ham" 98 : 3563-3570, 2018

      8 Chan JK, "The dynamics of thermal denaturation of fish myosins" 25 : 117-123, 1992

      9 Han MY, "The changes and relationship of structure and functional properties of rabbit myosin during heat-induced gelation" 13 : 63-68, 2015

      10 Chelh I, "Technical note : A simplified procedure for myofibril hydrophobicity determination" 74 : 681-683, 2006

      1 Brewer MS, "Thermal gelation properties of myofibrillar protein and gelatin combinations" 16 : 126-140, 2005

      2 Liu G, "Thermal aggregation properties of whey protein glycated with various saccharides" 32 : 87-96, 2013

      3 Chan JK, "Thermal aggregation of myosin subfragments from cod and herring" 58 : 1057-1061, 1993

      4 Sharp A, "The mechanism of formation of gels from myosin molecules" 58 : 63-73, 1992

      5 Polidori P, "The effects of slaughter age on carcass and meat quality of fabrianese lambs" 155 : 12-15, 2017

      6 Pan T, "The effects of calcium chloride on the gel properties of porcine myosin–κ-carrageenan mixtures" 63 : 467-477, 2017

      7 Zhou CU, "The effect of cooking temperature on the aggregation and digestion rate of myofibrillar proteins in jinhua ham" 98 : 3563-3570, 2018

      8 Chan JK, "The dynamics of thermal denaturation of fish myosins" 25 : 117-123, 1992

      9 Han MY, "The changes and relationship of structure and functional properties of rabbit myosin during heat-induced gelation" 13 : 63-68, 2015

      10 Chelh I, "Technical note : A simplified procedure for myofibril hydrophobicity determination" 74 : 681-683, 2006

      11 Hollung K, "Systems biology : A new tool for farm animal science" 15 : 100-117, 2014

      12 Joachim G, "Study of the thermal denaturation of selected proteins of whey and egg by low resolution NMR" 38 : 501-512, 2005

      13 Liu R, "Role of secondary structures in the gelation of porcine myosin at different ph values" 80 : 632-639, 2008

      14 Li-Chan E, "Raman spectroscopic study of thermally and/or dithiothreitol induced gelation of lysozyme" 39 : 1238-1245, 1991

      15 Xu XL, "Raman spectroscopic study of heat-induced gelation of pork myofibrillar proteins and its relationship with textural characteristic" 87 : 159-164, 2011

      16 Sanchez-Gonzalez I, "Protein and water structural changes in fish surimi during gelation as revealed by isotopic H/D exchange and raman spectroscopy" 106 : 56-64, 2008

      17 Cross HR, "Palatability of individual muscles from ovine leg steaks as related to chemical and histological traits" 37 : 282-285, 1972

      18 Han MY, "Low-field NMR study of heat-induced gelation of pork myofibrillar proteins and its relationship with microstructural characteristics" 62 : 1175-1182, 2014

      19 Chantrapornchai W, "Influence of NaCl on optical properties, large-strain rheology and water holding capacity of heat-induced whey protein isolate gels" 16 : 467-476, 2002

      20 Buamard N, "Improvement of gel properties of sardine(Sardinella albella)surimi using coconut husk extracts" 51 : 146-155, 2015

      21 Tintchev F, "High hydrostatic pressure/temperature modeling of frankfurter batters" 94 : 376-387, 2013

      22 D’Alessandro AG, "Fatty acid composition and vitamin E of meat as influenced by age and season of slaughter in mediterranean light lamb" 170 : 97-101, 2019

      23 Lopez-Diaz JA, "Effects of soy glycinin addition on the conformation and gel strength of two pork myosin types" 68 : 2724-2729, 2003

      24 Ma F, "Effects of high pressure and CaCl2 on properties of salt-soluble meat protein gels containing locust bean gum" 14 : 31-37, 2012

      25 Chin KB, "Effect of soy protein substitution for sodium caseinate on the transglutaminate-induced cold and thermal gelation of myofibrillar protein" 42 : 941-948, 2009

      26 Yao J, "Effect of sodium alginate with three molecular weight forms on the water holding capacity of chicken breast myosin gel" 239 : 1134-1142, 2018

      27 Han MY, "Effect of microbial transglutaminase on NMR relaxometry and microstructure of pork myofibrillar protein gel" 228 : 665-670, 2009

      28 Foegeding EA, "Effect of heating rate on thermally formed myosin, fibrinogen and albumin gels" 51 : 104-108, 1986

      29 Jaborek JR, "Effect of energy source and level, and animal age and sex on meat characteristics of sheep" 166 : 53-60, 2018

      30 Zhou YZ, "Contribution of three ionic types of polysaccharides to the thermal gelling properties of chicken breast myosin" 62 : 2655-2662, 2014

      31 Guo MH, "Changes in the myosin secondary structure and shrimp surimi gel strength induced by dense phase carbon dioxide" 227 : 219-226, 2017

      32 Kotwaliwale N, "Changes in textural and optical properties of oyster mushroom during hot air drying" 78 : 1207-1211, 2007

      33 Promeyrat A, "Changed dynamics in myofibrillar protein aggregation as a consequence of heating time and temperature" 85 : 625-631, 2010

      34 Chen GJ, "Aroma-active compounds of Beijing roast duck" 24 : 186-191, 2009

      35 Xue SW, "Applications of high pressure to pre-rigor rabbit muscles affect the water characteristics of myosin gels" 240 : 59-66, 2018

      36 Yongsawatdigul J, "Aggregation and conformational changes of tilapia actomyosin as affected by calcium ion during setting" 21 : 359-367, 2007

      37 An YQ, "Aggregation and conformational changes of silver carp myosin as affected by ultrasound-calcium combination system" 98 : 5335-5343, 2018

      38 Liu CL, "1H NMR and multivariate data analysis of the relationship between the age and quality of duck meat" 141 : 1281-1286, 2013

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      학술지 이력
      연월일 이력구분 이력상세 등재구분
      2023 평가예정 해외DB학술지평가 신청대상 (해외등재 학술지 평가)
      2020-01-01 평가 등재학술지 유지 (해외등재 학술지 평가) KCI등재
      2019-02-28 학술지명변경 외국어명 : Korean Journal for Food Science of Animal Resources -> Food Science of Animal Resources KCI등재
      2010-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2008-09-30 학술지명변경 외국어명 : 미등록 -> Korean Journal for Food Science of Animal Resources KCI등재
      2008-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2005-01-01 평가 등재학술지 선정 (등재후보2차) KCI등재
      2004-01-01 평가 등재후보 1차 PASS (등재후보1차) KCI등재후보
      2002-01-01 평가 등재후보학술지 선정 (신규평가) KCI등재후보
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      기준연도 WOS-KCI 통합IF(2년) KCIF(2년) KCIF(3년)
      2016 0.65 0.33 0.58
      KCIF(4년) KCIF(5년) 중심성지수(3년) 즉시성지수
      0.53 0.52 0.745 0.11
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