农业工程学报
農業工程學報
농업공정학보
2014年
18期
307-316
,共10页
邓丽%李岩%董秀萍%王垚%辛丘岩%潘锦锋
鄧麗%李巖%董秀萍%王垚%辛丘巖%潘錦鋒
산려%리암%동수평%왕요%신구암%반금봉
蛋白%加工%温度%肌原纤维蛋白%胶原蛋白%疏水键%二硫键%凝胶特性
蛋白%加工%溫度%肌原纖維蛋白%膠原蛋白%疏水鍵%二硫鍵%凝膠特性
단백%가공%온도%기원섬유단백%효원단백%소수건%이류건%응효특성
proteins%processing%temperature%myofibril protein%collagen%hydrophobic bond%disulfide bond%gel stability
为探究蛋白质形成凝胶过程中其化学作用力的变化规律以及与凝胶特性之间的关系，该文以鲍鱼腹足为原料，采用溶液分级提取方法，并结合扫描电镜和红外光谱法，考察热加工中鲍鱼腹足蛋白间作用力及其质构特性的变化情况。结果表明，随着加热温度升高（60、80、100℃），扫描电镜结果显示，鲍鱼腹足中间部位与边缘和过渡部位形成孔洞较小、排列紧密的网络结构，同时红外结果表明，随温度升高，蛋白二级结构发生明显变化， N-H弯曲和C-N伸缩振动较为明显，α-螺旋变为无规则卷曲结构，肌球蛋白疏水性增加，-S-S-形成。此时，对应离子键、氢键含量均呈下降趋势，疏水键相对含量呈先上升后下降趋势，二硫键、非二硫共价键含量呈上升趋势。进一步研究表明，各化学作用力与蛋白凝胶质构特性具有高度相关性。在较低温度下（60℃）离子键、氢键和疏水键对凝胶稳定性起主要作用，此时形成的凝胶较柔软；在较高温度下（80、100℃）二硫键、非二硫共价键为维持凝胶稳定的主要作用力，此时凝胶特性较佳，富有弹性、较好的凝聚性和回复性。该研究为热加工过程中鲍鱼腹足蛋白质变化的机理提供参考依据。
為探究蛋白質形成凝膠過程中其化學作用力的變化規律以及與凝膠特性之間的關繫，該文以鮑魚腹足為原料，採用溶液分級提取方法，併結閤掃描電鏡和紅外光譜法，攷察熱加工中鮑魚腹足蛋白間作用力及其質構特性的變化情況。結果錶明，隨著加熱溫度升高（60、80、100℃），掃描電鏡結果顯示，鮑魚腹足中間部位與邊緣和過渡部位形成孔洞較小、排列緊密的網絡結構，同時紅外結果錶明，隨溫度升高，蛋白二級結構髮生明顯變化， N-H彎麯和C-N伸縮振動較為明顯，α-螺鏇變為無規則捲麯結構，肌毬蛋白疏水性增加，-S-S-形成。此時，對應離子鍵、氫鍵含量均呈下降趨勢，疏水鍵相對含量呈先上升後下降趨勢，二硫鍵、非二硫共價鍵含量呈上升趨勢。進一步研究錶明，各化學作用力與蛋白凝膠質構特性具有高度相關性。在較低溫度下（60℃）離子鍵、氫鍵和疏水鍵對凝膠穩定性起主要作用，此時形成的凝膠較柔軟；在較高溫度下（80、100℃）二硫鍵、非二硫共價鍵為維持凝膠穩定的主要作用力，此時凝膠特性較佳，富有彈性、較好的凝聚性和迴複性。該研究為熱加工過程中鮑魚腹足蛋白質變化的機理提供參攷依據。
위탐구단백질형성응효과정중기화학작용력적변화규률이급여응효특성지간적관계，해문이포어복족위원료，채용용액분급제취방법，병결합소묘전경화홍외광보법，고찰열가공중포어복족단백간작용력급기질구특성적변화정황。결과표명，수착가열온도승고（60、80、100℃），소묘전경결과현시，포어복족중간부위여변연화과도부위형성공동교소、배렬긴밀적망락결구，동시홍외결과표명，수온도승고，단백이급결구발생명현변화， N-H만곡화C-N신축진동교위명현，α-라선변위무규칙권곡결구，기구단백소수성증가，-S-S-형성。차시，대응리자건、경건함량균정하강추세，소수건상대함량정선상승후하강추세，이류건、비이류공개건함량정상승추세。진일보연구표명，각화학작용력여단백응효질구특성구유고도상관성。재교저온도하（60℃）리자건、경건화소수건대응효은정성기주요작용，차시형성적응효교유연；재교고온도하（80、100℃）이류건、비이류공개건위유지응효은정적주요작용력，차시응효특성교가，부유탄성、교호적응취성화회복성。해연구위열가공과정중포어복족단백질변화적궤리제공삼고의거。
Abalone (Haliotis discus hannai) is an important commercial seafood species. Pleopod muscle is the edible part of abalone, which is rich in protein and mainly composed of myofibril protein and collagen. The change in conformation and aggregation of protein during heating would affect the quality of the product. Chemical interactions including hydrogen bonds, disulfide bonds, non-disulfide bonds, ionic bonds, and hydrophobicity have shown great effect on textural properties of muscle protein. This study used the method of grading extraction solution, scanning electronic microscopy (SEM), and Fourier transform infrared (FTIR) to investigate the law of changes in chemical interactions and textural properties of the abalone (Haliotis discus hannai Ino) pleopod muscle protein. The results indicate that as the temperature increases (60℃, 80℃, 100℃), the changes of chemical interaction in the center and the edge or transition part of the abalone muscle protein were similar. During heating, the content of ionic and hydrogen bonds declined; the content of hydrophobic bonds first increased and then decreased whereas disulfide and non-disulfide bonds increased but the increasing amount differed due to the different composition of protein. The center part is characterized by high amounts of myofibrilllar protein while the edge or transition part contains more collagen. The textural property shows the following change during low temperature (60℃), the harness, resilience,springiness, cohesiveness, and chewiness of the abalone muscle were low. As the temperature increased, the parameters changed significantly. However, the harness and chewiness of the edge or transition part of the abalone muscle protein decreased slightly when temperature increased to 100℃.The results of SEM suggest that fresh abalone muscle exhibited a porous net structure composed of a vast amount of layers. However, as heating temperature increased (60℃, 80℃, 100℃), a porous closed-knit structure with a tiny hole was formed both in the center and the edge or transition part of the abalone muscle. FTIR analysis indicates that the secondary structure of protein changed significantly; the N-H bond bended, C-N bond stretched and vibrated,α-helix showed non-regular curved structure, hydrophobicity of myofibrillar protein increased, and disulfide bonds were formed. In addition, there were close correlations between chemical interactions and textural characteristics, which indicate that ionic, hydrogen, and hydrophobic bonds played important roles in the soft gel during the low temperature (60℃) period. However disulfide and non-disulfide bonds were the main chemical interaction for the formation and maintenance of gel with excellent harness, springiness, and cohesiveness at the high temperature period (80℃, 100℃). Our results not only expose the change of the secondary structure of the abalone muscle protein during the heating-gel forming process but also provide information on the relationship between chemical interactions and textural properties. The study provides useful information on the mechanism of protein changes in the pleopod muscle of abalone during heating and on the processing techniques of the abalone muscle.
