カイコの消化液アミラーゼの精製と二・三の性質

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タイトル別名
  • Purification and some properties of amylase in the digestive juice of the silkworm larvae, <i>Bombyx mori</i>
  • カイコ ノ ショウカエキ アミラーゼ ノ セイセイ ト ニ サン ノ セイシツ

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説明

In the present study, a purification of amylase in the digestive juice of the silkworm larvae, Bomhyx mori, was carried out by the following procedures: ammonium sulfate precipitation of the digestive juice followed by amylopectin complex precipitation, Bio-gel and CM-Sephadex column chromatographies and dialysis. The amylase thus purified showed the specific activity of 1480U/mg protein nitrogen and a single and symmetrical schlieren peak on ultracentrifugation. The sedimentation coefficient (S°20, ω) of the enzyme was calculated to be 5.30S.<br>The enzyme was stable at pH 8.0-11.5 and it was most active at pH 9.2. (This value was quite similar to those of the amylase of dude state which had been reported by many authors.) The enzyme was heat stable below 55°C and calcium ion was seemed to be unnecessary for the enzyme stabilization. In the case where amylose was used as the substrate, activation energies of the enzyme were calculted to be 17.0kcal at 0-25°C and 3.8kcal at 25-40°C. The Km value was also calculated to be 2.57×10-3μmoles glucosidic bond/l at pH 9.2.<br>The molecular weight of the enzyme was assumed to be 13, 000-17, 000, by the Bio-gel column chromatography technique.

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