Substrate Specificity of the Milk-clotting Enzyme from Irpex lacteus on κ- and β-Casein

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概要

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• Irpex lacteus milk-clotting enzyme hydrolyzed the Phe(105)-Met(106) bond of κ-casein, causing the precipitation of para-κ-casein along with other casein fractions in the presence of calcium ions, with a mechanism similar to other milk-clotting enzymes. Furhtermore, Irpex enzyme hydrolyzed at the positions Leu(79)-Ser(80) and Tyr(30)-Val(31) of para-κ-casein. Degradation patterns of β-casein by Irpex and Mucor miehei enzymes were almost the same by polyacrylamide gel electrophoresis, but Endothia parasitica enzyme showed a different degradation pattern. Under the conditions employed, β-casein appeared to be scarcely hydrolyzed by chymosin. Comparing the specificity of Irpex enzyme on β-casein with that of chymosin, the common cleaving points were Leu(165)-Ser(166), Ala(189)-Phe(190), and Tyr(192)-Glu(193). The difference in the specificity between the enzymes was exhibited in the cleavage at the Leu(139)-Leu(140) bond by chymosin and of the Ser(142)-Trp(143) bond by Irpex enzyme. Although the cleaving points of β-casein by both enzymes resembled each other, each enzyme exhibited different degradation patterns of β-casein because of thier different order of cleavage.

• 社団法人 日本農芸化学会の論文

著者

• Murakami K

  Research And Development Department Kibun Food Chemifa Co. Ltd.

• Kusakabe Isao

  Institute of Applied Biochemistry, University of Tsukuba

• Murakami Kazuo

  Institute of Applied Biochemistry, University of Tsukuba

• KOBAYASHI Hideyuki

  Institute of Applied Biochemistry, University of Tsukuba

• YOKOYAMA Saeko

  Institute of Applied Biochemistry, The University of Tsukuba

• Kusakabe Isao

  Institute Of Applied Biochemistry University Of Tsukuba

• Murakami Kazuo

  Institute Of Applied Biochemistry University Of Tsukuba

• Kobayashi Hideyuki

  Institute Of Applied Biochemistry The University Of Tsukuba

• KUSAKABE Isao

  Institute of Applied Biochemistry, The University of Tsukuba

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