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應用
Rennin（凝乳酶），也称为 chymosin（凝乳酶），是在小牛胃中产生的乳凝酸蛋白酶。它用于奶酪制作和研究新生儿胃消化。
生化／生理作用
凝乳酶，一条 323 个氨基酸链，分泌时为无活性前体，然后通过限制性蛋白水解转化为活性酶。它能裂解 K-酪蛋白中苯丙氨酸和甲硫氨酸之间的肽键。
包裝
包装规格取决于蛋白质含量
單位定義
一个单位将在 30°C 下每分钟凝结 10 mL 牛奶。
外觀
含有氯化钠的冻干粉末
分析報告
缩二脲法测定蛋白
訊號詞
Danger
危險分類
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
標靶器官
Respiratory system
儲存類別代碼
11 - Combustible Solids
水污染物質分類（WGK）
WGK 3
其他客户在看
Kirsten Kastberg Møller et al.
Journal of agricultural and food chemistry, 60(21), 5454-5460 (2012-05-09)
Bovine chymosin constitutes a traditional ingredient for enzymatic milk coagulation in cheese making, providing a strong clotting capacity and low general proteolytic activity. Recently, these properties were surpassed by camel chymosin, but the mechanistic difference behind their action is not
Xin-ping Li et al.
Xi bao yu fen zi mian yi xue za zhi = Chinese journal of cellular and molecular immunology, 28(7), 715-717 (2012-07-10)
To optimize the prochymosin (pCHY) gene codons and express the gene in Escherichia coli (E.coli), and to prepare its antiserum and detect chymosin protein specifically. According to codon usage bias of E.coli, prochymosin gene sequence was synthesized based on the
Neil D Rawlings et al.
Nucleic acids research, 40(Database issue), D343-D350 (2011-11-17)
Peptidases, their substrates and inhibitors are of great relevance to biology, medicine and biotechnology. The MEROPS database (http://merops.sanger.ac.uk) aims to fulfil the need for an integrated source of information about these. The database has hierarchical classifications in which homologous sets
B Foltmann et al.
The Journal of biological chemistry, 254(17), 8447-8456 (1979-09-10)
The complete amino acid sequence of calf chymosin (rennin) (EC 3.4.23.4) has been determined. The sequence consists of a single peptide chain of 323 amino acid residues. The primary structure of the precursor part of calf prochymosin was published previously
Jung-Feng Hsieh et al.
Journal of agricultural and food chemistry, 60(8), 2039-2045 (2012-02-07)
Chymosin-induced coagulation of individual milk proteins during incubation at 30 °C was investigated using a proteomic approach. The addition of chymosin (0.006 units/mL) caused the milk proteins to coagulate after a 3 h incubation period. Approximately 88% of the milk
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