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微生物凝乳酵素 Mucor-renin이 k-casein에 對한 作用
柳洲鉉,有馬啓 연세대학교 대학원 1976 延世論叢 Vol.13 No.2
k-casein was reacted with Mucor rennin(MR) or Calf rennin(CR). Each para-k-casein and macropeptide were separated from the hydrozed k-casein, and the casein were analyzed to elemental composition, composition of amino acids and terminal amino acids. N-terminal of para-k-casien by MR reaction was not confirmed, but Phe and Leu in C-terminal were identified on paper chromatography by examination of para-k-casein with carboxypeptidase. N-terminal of macropeptide was Met. Therefore, MR was hydrolyzed between linkage of Phe in C-terminal of para-k-casein and Met in N-terminal in macropeptide. Results of substrate specificity on k-casein with CR was corresponded to above results of MR.
유주현,전촌학조,홍윤명,유마계 한국농화학회 1969 Applied Biological Chemistry (Appl Biol Chem) Vol.12 No.1
Mucor-rennin, the crystalline milk-clotting enzyme, isolated from Mucor pusillus var. Lindt, has an acid protease activity. The optimum pH for the digestion of k-casein is 4.5, while that for hemoglobin digestion is 4.0. The skim milk solution was easily clotted acidic solution than alkalin solution, and the milk clotting activated by Ca ion. The enzyme was heat stable against heat from pH 4.0 to 6.0 but was more stable at pH 5.0. The activity of the enzyme at pH 5.0 did not decrease at 30 C for 15 days and the activity was not effected by sodium propionate and salicilic acid. Therefore, the enzyme of liguid type could store for a long time and could be transported from Erzyme production Co. to Manufacture of cheese Co. by adding the antiesptic and by adjusting pH to 5.0.