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頁籤選單縮合
題 名 | 紅麴發酵乾酪熟成期間組成及微細構造之變化=Change in Chemical Composition of Monascus--Fermented Cheese and Its Microstructure during Ripening |
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作 者 | 蘇和平; 鐘穎皓; 林慶文; | 書刊名 | 食品科學 |
卷 期 | 25:5 1998.10[民87.10] |
頁 次 | 頁610-625 |
分類號 | 473.77 |
關鍵詞 | 紅麴發酵乾酪; 化學組成; 微細構造; 熟成; Monascus-fermented cheese; Chemical composition; Microstructure; Ripening; |
語 文 | 中文(Chinese) |
中文摘要 | 本試驗乃利用經選定適用於乾酪製造之紅趜菌株Monascus purpureus CCRC 31530進行紅麴乾酪之製造,並探討熟成期間其組成之變化。 本試驗於乾酪壓型流程時接種M. purpureus CCRC 31530之冷凍乾燥紅麴米粉末3%並充分混合,使紅麴菌之蛋白?能立即充分作用,且使製品外觀呈現均勻粉紅色。結果顯示:紅麴發酵乾酪熟成期間蛋白質隨水分的減少而相對增加,可溶性氮含量亦隨熟成期的延長而逐次提高,自熟成第一週起,其可溶性氮量較對照組為多。在熟成率方面,原先以紅趜液浸置於乾酪試驗方式之製品於熟成第三週後始較對照組高,本試驗處理則自第一週起即高於對照組,在第七週時為36.39%,較一般軟質乾酪為高。乾酪熟成期間蛋白質電泳行為方面:熟成第0天,k-酪蛋白因受凝乳?水解已不復見,且因凝乳?對αs1-酪蛋白具專一性水解作用,熟成初期α-酪蛋白帶較稀,紅麴發酵乾酪及對照組對其變化不大,但對β-酪蛋白之影響差異很大,紅麴乾酪之β-酪蛋白於第二週起已受水解,對照組則在第五週後方被水解,由此可得知紅趜菌之酸性蛋白?對β-酪蛋白具水解作用。藉用掃描電子顯微鏡觀察乾酪表面之微細構造,結果發現熟成期間(0-6週)表面質地漸趨緊密,且紅麴發酵乾酪表面較對照組更為緊密,顯示紅麴乾酪蛋白質較充分被水解。本試驗之改良製造流程確可提高乾酪熟成率及充分水解蛋白質,並賦予製品美麗的外觀,可謂具有東方傳統口味之新式乾酪。 |
英文摘要 | This study produced Monascus-fermented cheese (MFC) using Monascus purpureus 31530 as starter and developed a unequal cheese with oriental flavor. A significant increase in protease was produced by Monascus purpureus after 3 weeks of ripening, which resulted from the addition of 3%lyophilized rice powder containing M. purpureus in the process of hoping. On the other hand, protease activity on cheese was enhanced and a pink surface on the cheese was formed due to release of Monascus pigment. As far as the proteolytic properties of the cheese were concerned, the total protein in all the samples increased with ripening; however, no significant difference in MFC or the control was observed. Soluble protein increased with ripening; soluble protein in MFC was greater than that in the control after one week of ripening. The ripening ratio of cheese soaked in Monascus liquid was not higher than that of the control up to 3 weeks of ripening, but that of MFC was higher than that of the control after one week of ripening, and the ripening ratio of MFC was 36.39% after 7 weeks of ripening. In SDS-PAGE, k-casein was preferentially attacked by rennin, and αs1-casein was cleaved rapidly and specifically in rennin. β-casein of MFC was hydrolyzed after 2 weeks of ripening, but β-casein in the control was degraded after 5 weeks of ripening, which suggested that β-casein could be cleaved by protease produced from M. purpureus. Scanning electron microscopy of the cheese showed that the microstructures of cheeses were packed intensively during 6 weeks of ripening, and that the microstructure of MFC was packed more tightly than that of the control, which suggested that protein in the Monascus-fermented cheese was degraded more than that in the control. In conclusion, improving the procedure of MFC may enhance ripening and protein degradation, and improve the appearance; as a result, this kind of special cheese has an oriental flavor character. |
本系統中英文摘要資訊取自各篇刊載內容。