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Cellulase에 의한 섬유소 가수분해에 관한 연구

Studies on the Hydrolysis of the Cellulose by Cellulase

한국생화학회지 1970년 3권 1호 p.15 ~ 23
이형섭,
소속 상세정보
이형섭 (  ) - 부산대학교 의과대학 생화학교실

Abstract

Rhizopus mold cellulase의 가수분해 기구를 연구하기 위하여 appha-cellulose, CMC, CEAE cellulose, cellulose phosphate, Sigma cell, 및 CMC phosphate를 기질로 삼아 Willsta´´tter and Schudel 법으로 이들의 가수분해도를 측정하여 다음과 같은 결과를 얻었다.
1. Rhizopus mold cellulase에 의하여 상기 섬유소들은 다음 순위로 가수분해를 잘 받는다.
즉, CMC>DEAE cellulose>alpha-cellulose>Sigma cell>CMC phosphate>cellulose phosphate.
2. Aspergillus niger cellulase에 의한 가수분해 순위는 다음과 같다.
Sigma cell>CMC>DEAE cellulose>alpha-cellulose>CMC phosphate>cellulose phosphate.
3. Rhizopus mold cellulase는 pH 2.8∼6.0 범위에서 안정하며, 70˚∼90˚범위에서 내열성이 있었다.
4. Succinate 및 citrate buffer에서 Rhizopus mold cellulase의 활성도는 높고, phosphate buffer에서 낮다.
5. Bovine albumin 및 cysteine는 Rhizopus mold cellulase를 부활시키고 Na₂HPO₄는 저해하였다.
6. Ca^(++), Mg^(++)은 Rhizopus mold cellulase를 부활시키고 Cu^(++)는 이 cellulase를 저해하였다.

A prevalent explanation of the enzymic hydrolysis of cellulose involves at least two enzymes, cellulase and cellobiase. Cellulase produces and probably other oligosaccharides, whereas cellobiase hydrolyzes these products to glucose.
In an effort to characterize the enzyme concerned in the hydrolysis of cellulosc substitutes, the experiments were carried out by the following method.
Seven milliliters of citrate(pH 4.5) containing 30mg of the cellulose was incubated with 30mg of Rhizopus mold cellulase (Sigma) and 2 drops of toluene at 47˚continuing the aeration. After 24 hours the suspension was filtrated and a 1 ml aliquot of the filtrate was assyed. The activity is expressed in milligrams of reducing sugar as glucose.
In general, native cellulose exhibits a much greater resistance to enzymic hydrolysis than do regenerated cellulose, Hence, it has become customary to use treated celluloses for measurement of cellulolytic activity, since the sensitivity is thereby greately increased. Accordingly, the author used cellulose substitutes such as CMC, cellulose phosphate, DEAE cellulose and alpha-cellulose (fiber) and Sigm acell(macrocrystalline) as substrate to investigate the effects of metal ions and thiol containing compounds on Rhizopus mold cellulase. The preferability of buffer system, temperature stability, and pH stability were studied, too.
The following results were obtained; The cellulase is stable over the pH range of 2.8-6.0 and the temperature range of 70˚-90˚. The cellulase was shown to e inhibited by sodium phosphate and Cu^(2+), but not by Fe^(3+) and DETA. It was found that the addition of bovine albumin, Mg^(2+), Ca^(2+) and cystcine activated the cellulase activity.

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