β-Fructofuranosidase from grape berries II. Solubilization of a bound fraction

Wilfred Niels Arnold
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引用次数: 22

Abstract

  • 1.

    1. A bound fraction of grabe β-fructofuranosidase (EC 3.2.1.26) was solubilized by treatment with 0.2 M borate buffer (pH 8.5), whereas several other aqueous salts were without effect.

  • 2.

    2. In the system described, solubilization was influenced by boric acid concentration and pH but not by presentation time. Solubilization was essentially irreversible.

  • 3.

    3. Solubilization was maximal at pH 8.5; under more alkaline conditions, enzyme inactivation occurred. The decrease in amount of bound enzyme followed an inverse trend.

  • 4.

    4. Borate solubilization gave a total yield of β-fructofuranosidase about 190% based on the starting material. This, together with the well-known interaction of borate with carbohydrates, suggested that a masking polysaccharide was operative in the starting material.

  • 5.

    5. The solubilized and soluble enzyme were partially purified and characterized. In both cases, only unsubstituted β-fructofuranosides were hydrolyzed. The Michaelis constants for sucrose were not significantly different.

  • 6.

    6. The dangers inherent in comparing the relative amounts of enzymes from different tissues were underlined by this experience.

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葡萄果实中的β-果糖呋喃苷酶结合分数的溶解
1.1. 用0.2 M硼酸缓冲液(pH 8.5)处理,可使黏结部分的β-果糖呋喃苷酶(EC 3.2.1.26)溶解,而其他几种水溶液没有效果。在所描述的体系中,硼酸浓度和pH对增溶作用有影响,但不受呈现时间的影响。溶解作用基本上是不可逆的。在pH 8.5时增溶效果最大;在碱性较强的条件下,酶发生失活。结合酶的减少呈反比趋势。硼酸盐增溶使β-果糖呋喃苷酶的总收率约为190%。这一点,再加上众所周知的硼酸盐与碳水化合物的相互作用,表明一种掩蔽多糖在起始材料中起作用。对可溶性酶和可溶性酶进行了部分纯化和表征。在这两种情况下,只有未取代的β-果呋喃苷被水解。蔗糖的米切里斯常数无显著差异。这种经验强调了比较不同组织中酶的相对量所固有的危险。
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