Crystalline Milk-Clotting Protease from Mucor Miehei and Some of its Properties

Sternberg, M.

doi:10.3168/jds.s0022-0302(71)85805-8

Cited by 56 publications

(19 citation statements)

References 13 publications

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“…faecalis enzyme was about 34,000-36,000, which is similar to those of MCE from Irepex lacteus (34,000-36,000) (Kawai, 1971;Kobayashi et al, 1983), E. parasitica (37,500) (Hagemeyer et al, 1968), M. miehei (34,000-39,000) (Sternberg, 1971), and M. pusillus (29,000-30,600) (Arima, 1968), but different from that from B. subtilis K-26 (27,000) (Rao & Mathur, 1979). The isoelectric point of the Ec.…”

Section: Discussionsupporting

confidence: 49%

“…In addition, the pH stability of the Ec. faecalis enzyme (pH 5.5-10) was also different from those of the MCE from M. miehei (pH 4-8) (Sternberg, 1971), M. pusillus (pH 4-8) (Iwasaki et al, 1967a), I. lacteus (pH 3-6) (Kawai, 1971;Kobayashi, 1983), and B. subtilis K-26 (most stable at pH 7.5) (Rao & Mathur, 1979). As in the case of MCE from B. subtilis, the Ec.…”

Section: Discussionmentioning

confidence: 99%

“…The optimum pH for proteolysis by Ec. faecalis enzyme (pH 8.0-9.0) was higher than those of the MCE from M. miehei (Sternberg, 1971), M. pusillus (Arima et al, 1968), and I. lacteus (Kawai, 1971;Kobayashi, 1983) (4.0, 4.0, and 2.5-4.0, respectively). In addition, the pH stability of the Ec.…”

Section: Discussionmentioning

confidence: 99%

“…On the other hand, it is also well known that MCE is calf rennet used for cheese-making from the fourth stomach of the calf, as well as microbial rennet from the microorganisms Mucor pusillus (Iwasaki et al, 1967a;Iwasaki et al, 1967b;Arima et al, 1968), Mucor miehei (Sternberg, 1971), Endothia parasitica (Hagemeyer et al, 1968;Larson & Whitaker, 1970;Sardinas, 1968), and Irpex lacteus (Kawai, 1971;Kobayashi et al, 1983;Kobayashi et al, 1985a;Kobayashi et al, 1985b). These have been purified, and their enzymatic properties investigated in detail.…”

mentioning

confidence: 99%

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Purification and Characterization of an Extracellular Proteinase Having Milk-Clotting Activity from Enterococcus faecalis TUA2495L

Sato

Tokuda

Koizumi

et al. 2004

FSTR

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Lactic acid bacteria (157 stock cultures) were screened for their ability to produce extracellular proteinase with milk-clotting activity. A strain identified as Enterococcus faecalis TUA2495L showed the highest ratio of milk-clotting activity (MCA) to proteinase activity (PA). The molecular weight of the purified enzyme from the strain was estimated to be 34-36 kDa by gel filtration and by SDS-PAGE. Its isoelectric point was about 5.4, and the K m value on casein (Hammarsten) was 0.61% (w/v). The optimum temperature was 70˚C for MCA and 50˚C for PA. The MCA increased with a decrease in the pH from 7.8 to 5.8 but the PA was optimum at pH 8.0-9.0. Both MCA and PA were stable within the pH range of 5.

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Section: Discussionsupporting

confidence: 49%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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Purification and Characterization of an Extracellular Proteinase Having Milk-Clotting Activity from Enterococcus faecalis TUA2495L

Sato

Tokuda

Koizumi

et al. 2004

FSTR

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“…Chymosin 17 ) M. pusil!us 12 ) M. miehei 18 ) E. parasitica 19 striking similarities to each other. Sulfurcontaining amino acids, such as cysteine and methionine, could not be detected in each hydrolyzate, 24, 48 and 72 hr.…”

Section: [Rpes Lacteusmentioning

confidence: 92%

Purification and Characterization of Two Milk-clotting Enzymes fromIrpex lacteus

Kobayashi

Kusakabe

Murakami

1983

Agricultural and Biological Chemistry

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Purification and properties of milk‐clotting enzyme from Bacillus subtilis K‐26

Rao

Mathur

1979

Biotech & Bioengineering

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A milk-clotting enzyme from Bucillirs sirhrilis K-26 was purified by gel filtration and ion-exchange chromatography resulting in a 24-fold increase in specific activity with an 80% yield. Polyacrylamide gel electrophoresis and ultracentrifugal analysis revealed that the purified enzyme was homogeneous and had a molecular weight of 27,000 and a K , of 2.77 mgiml for K-casein. The enzyme was most stable at pH 7.5 and showed increasing clotting activity with decrease in milk pH up to 5.0. The maximum milk-clotting activity was obtained at 60°C. but the enzyme was inactivated by heating for 30 min at 60°C. The enzyme was irreversibly inhibited by EDTA and unaffected by DFP. Heavy-metal ions (Hg2+, Pb2+) inactivated the enzyme.

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Crystalline Milk-Clotting Protease from Mucor Miehei and Some of its Properties

Cited by 56 publications

References 13 publications

Purification and Characterization of an Extracellular Proteinase Having Milk-Clotting Activity from Enterococcus faecalis TUA2495L

Purification and Characterization of an Extracellular Proteinase Having Milk-Clotting Activity from Enterococcus faecalis TUA2495L

Purification and Characterization of Two Milk-clotting Enzymes fromIrpex lacteus

Purification and properties of milk‐clotting enzyme from Bacillus subtilis K‐26

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