Applied Biological Chemistry

  • Volume 12
  • /
  • Pages.7-11
  • /
  • 1969
  • /
  • 2468-0834(pISSN)
  • /
  • 2468-0842(eISSN)
The Korean Society for Applied Biological Chemistry (한국응용생명화학회)
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Milk-clotting Enzyme from Microorganisms, Part 10, Studies on General Properties and storage of Mucor-rennin (Milk-clotting Enzyme) isolated from Mucor pusillus var. Lindt

미생물(微生物)이 생산(生産)하는 응유효소(凝乳酵素) (제10보(第10報)) -Mucor-pusillus의 고체배양(固體培養)으로부터 단리(單離)된 결정(結晶) 응유효소(凝乳酵素) Mucor-rennin의 일반적(一般的) 성질(性質)과 그의 저장성(貯藏性)-

  • Yu, Ju-Hyun (Department of Food Engineering, Yonsei University) ;
  • Tamura, Gakuzo (Department of Agricultural chemistry The University of Tokyo) ;
  • Hong, Yun-Myung (Department of Chemical Engineering, Yonsei University) ;
  • Arima, Kei (Department of Agricultural chemistry The University of Tokyo)
  • 유주현 (연세대학교이공대학 식품공학과) ;
  • 전촌학조 (동경대학 농예화학과 발효학교실) ;
  • 홍윤명 (연세대학교이공대학 화학공학과) ;
  • 유마계 (동경대학 농예화학과 발효학교실)
  • Published : 1969.09.15
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Abstract

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.

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