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題名 | 幾丁聚醣對豬肉鹽溶性蛋白質熱膠凝的影響=The Effect of Chitosan on Thermal Gelation of Porcine Salt Soluble Proteins |
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作者 | 黃建嘉; 李錦楓; | 書刊名 | 食品科學 |
卷期 | 25:2 1998.04[民87.04] |
頁次 | 頁150-162 |
分類號 | 346.217 |
關鍵詞 | 幾丁聚醣; 動態流變性; 熱膠凝; 鹽溶性蛋白質; Chitosan; Dynamic viscoelasticity; Thermal gelation; Salt soluble protein; |
語文 | 中文(Chinese) |
中文摘要 | 豬股中肌鹽溶性蛋白質(SSP)的熱膠凝過程,可以分為較低溫區(50℃以下)與較高溫區(50℃以上)二階段。由複數參數(complex modulus,G*)的變化可知,SSP在較低溫區的膠凝受到pH影響。在pH4.8~5.8中,pH愈高,離pI點愈遠,G*會愈大而範圍愈窄;且最高值會隨著pH提高而有往高溫移動的情形出現。另外,由G*對溫度微分值的變化(dG8/dT)及相角δ的變化,也可以知道pH愈遠離pI點,則變化會愈明顯,表示溫度對其膠凝的影響愈大。在較高溫區部份,發現δ角和dG*/dT都沒有明顯變化,表示此區段的膠凝受pH影響較小。將去乙醯度74%(DD74)和99%(DD99)的幾丁聚醣分別添加到SSP中,觀測對SSP的熱膠凝影響:由G*可知,添加幾丁聚醣可以降低SSP於較低溫區的膠凝,且δ角會較大,主要是因為幾丁聚醣會與SSP產生交互作用,干擾肌凝蛋白頭部的聚集,使膠凝系統有偏向黏性的情形;在較高溫區段,由G*的變化可知pH愈高,則DD99較DD74幾丁聚醣可降低SSP的膠凝作用。PH愈高,添加DD99可以增加δ角,但DD74則沒有明顯的影響。另外,由dG*/dT的變化可知,添加幾丁聚醣可以降低SSP於較高pH的變化。以掃描式電子顯微鏡觀察幾丁聚醣與SSP熱凝膠體的微細結構可知,幾丁聚醣可以和SSP形成複合膠體,其上纏繞或吸附有蛋白質顆粒的綱狀結構;pH愈高,添加DD74幾丁聚醣的膠體結構會較緊密,但是DD99幾丁聚醣則有相反的情形。 |
英文摘要 | There are two steps in the thermal gelation of salt soluble proteins (SSP) which are prepared from porcine Vastus intermedius muscle: a lower temperature section (below 50℃) and a higher temperature one (upper 50℃). Due to changes of the complex modulus (G*), the pH value affected the gelation of SSP in the lower temperature section. In the pH range of 4.8~5.8, as the pH value different from the pI of SSP increased, the G* value increased more; then, its range narrowed, and the highest value of G* changed to higher temperature range with increasing pH. By analyzing the changes of the phase angle (δ) and the differential plots of G* versus temperature (dG*/dT), it was found that if the pH was different from the pI, then the changes were greater, therefore it was concluded that the gelation was greatly affected by the temperature change. In the higher temperature section, the changes of the δ angle and dG*/dT were not significantly different, and the results showed that the gelation of this section was less affected by the pH. The influence of SSP on thermal gelation was studied by adding chitosan with a varying degree of deacetylation, 74% (DD74) and 99 (DD99), to the SSP. From the changes of G*, it was found that the gelation of the SSP in the lower temperature section decreased, and that G" also decreased, but that the δ angle increased. These results indicated there was interaction between the chitosan and SSP, and that it interfered with the aggregation of the myosin head, which caused the gelation system to have more potent viscosity. In the higher temperature section, the results showed that due to the changes of G* at higher pH, gelation decreased more with DD99 chitosan than with DD74 chitosan. The δ angle increased when DD99 chitosan was added at higher pH, but not when DD74 chitosan was added. From the changes of dG*/dT, it was found that the addition of chitosan would decrease the change of the SSP at higher pH. From observation of the microstructure of the thermal gelation in a mixed solution of chitosan and SSP, it was clear that the comlex structure was filled with SSP; thus, protein granules were absorbed, and a net structure was formed. The higher the pH, the tighter the gel structure with chitosan DD74 while the one treated with chitosan DD99 showed the reverse phenomenon. |
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