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Journal of Dairy Science Vol. 69 No. 8 2018-2026
© 1986 by American Dairy Science Association ®
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Profiles of Proteinases in Gouda-Type Cheese

Keiji Igoshi1, Shuichi Kaminogawa and Kunio Yamauchi

Department of Agricultural Chemistry, The University of Tokyo, Bunkyo-ku, Tokyo 113, Japan

ABSTRACT

The pH of buffers used for extraction of proteinases from Gouda-type cheese affected the kinds of extractable proteinases. Proteinases in the fractions extracted with pH 3.0, 4.0, and 6.0 buffers were separated by CM-Sephadex or diethylaminoethyl-cellulose. Two (F3-I and F3-II), three (F4-I, F4-II, and F4-III), and one (F6) proteinases were separated from the pH 3.0, 4.0, and 6.0 extracts. The F3-I was completely inhibited by pepstatin. The F3-I degradated {alpha}s1- and ß-casein into products with the same mobilities as {alpha}s1-casein(f24 to 199) and ß-casein(f1 to 189) peptide, respectively. The F3-II was strongly inhibited by diisopropyl-fluorophosphate and soybean trypsin inhibitor, whereas F3-II produced fragments with mobilities equal to those of {gamma}-caseins, that is, ß-casein(f29 to 209), ß-casein(f106 to 209), and ß-casein (f109 to 209). The F4-I was completely inhibited by pepstatin as well as F3-I, but changes in the polyacrylamide gel electrophoresis pattern of casein by F4-II were different from those by F3-I. Properties of F4-II and F4-III were similar to those of F3-I and F3-II; therefore, F4-II and F4-III are considered to be the same enzymes as F3-I and F3-II, respectively. The F6 was strongly inhibited by diisopropyl-fluorophosphate and ethylenediaminetetraacetic acid. In Gouda-type cheese, there are at least four proteinases, two of them being serine proteinases and the other two acid proteinases.

FOOTNOTES

1 Department of Animal Science, Kyushu Tokai University, Choyo-son, Aso-gun Kumamoto 869-14.






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Copyright © 1986 by the American Dairy Science Association ®.