Abstract
Chymosin (EC 3.4.23.4) is one of the most important aspartic proteinases used as a milk-clotting enzyme in cheese production. The primary structures of two calf chymosin forms (A and B) are known.1,2 The only difference in their structures is at position 302 (preprochymosin numbering). More recently, other forms of calf chymosin were also found and sequenced.3–8 Calf chymosin has been cloned in many laboratories using different expression vector/host systems. Recombinant chymosin is comparable to the wild type enzyme in cheesemaking properties.9,10 Like traditionally ušed calf rennet, lamb rennet has also been utilized in cheese making because it has similar high milk-clotting and low proteolytic activities.11 Recently, we briefly reported on the deduced amino acid sequence of lamb preprochymosin.12
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© 1991 Plenum Press, New York
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Pungerčar, J., Štrukelj, B., Gubenšek, F., Turk, V., Kregar, I. (1991). Amino Acid Sequence of Lamb Preprochymosin and its Comparison to Other Chymosins. In: Dunn, B.M. (eds) Structure and Function of the Aspartic Proteinases. Advances in Experimental Medicine and Biology, vol 306. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-6012-4_16
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DOI: https://doi.org/10.1007/978-1-4684-6012-4_16
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