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- 저자 : 맹정섭 (검색결과 2 건)
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맹정섭,남윤규,박승희,최우영 충남대학교 농업과학연구소 1995 농업과학연구 Vol.22 No.2
Two types of modified celluloses which contain trinitrophenyl groups as chromophore were synthesized from carboxymethyl cellulose Whatman CM 70 and CM 32. Diaminoethyl groups were added to the CM 70 and CM 32 to make DAE-CM celluloses and then the DAE-CM groups were substituted by 2,4,6-trinitrophenyl groups to produce TNP-celluloses. Average particle size of the TNP-cellulose from CM 32 was 44.6 ±9.6 μm in diameter and 127.9±22.5 μm in length, which was much smaller than those from CM 70, however its TNP-moiety per gram determined by using the molar extinction coefficient 1.33×10^4 of ε-TNP-lysine at 345 nm, was 0.68 millimoles, which was 5.6-fold greater than those from CM 70. The absorption spectrum of TNP-oligosaccharides which were the soluble products of TNP-celluloses by a cellulase preparation Onozuka R-10, showed a maximal peak at 344 nm. Increases in the absorbance during hydrolysis were linear with the enzyme concentration, and the differences of slope values between two types of TNP-celluloses that the more semsitive assay could be achieved by using those from CM 32 as substrate at the low range of the enzyme concentration.
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TNP-cellulose의 섬유소 분해효소 활성도 측정을 위한 기질로서의 특성
맹정섭,남윤규,최우영 충남대학교 농업과학연구소 1994 농업과학연구 Vol.21 No.2
Characteristics of TNP-cellulose which prepared from carboxymethyl cellulose powder, CM32, as substrate for cellulase activity assay were investigated. Enzymatic hydrolysis of TNP-cellulose occured on the cellulose moiety but not on amide bonds, following Michaelis-Menten kinetics. Tree cellulase preparations from Trichoderma viride, Aspergillus niger. and Cellulomonas sp. were tested for their pH and temperature dependences and compared with the method determining the increase in reducing power. The enzyme activity was found to have the same temperature range in both methods, however the pH range was broadened in the case of using TNP-cellulose as substrate. The colorimetric method for cellulase assay using TNP-cellulose as substrate was compared with the other methods: one based on determination of the increase in reducing power; and the other based on determining the decrease in viscosity of Na-CM-cellulose solution. The activities measured by the colorimetric method showed a linear correlation with the enzyme concentration of certain range in all three enzymes tested, and the activity values were proportional to those obtained from the other methods. Depending on the enzyme. however, the activity values from this method were not always in proportion to those from the viscometric method, suggesting that this method was not specific for determination of the endo-type cellulase.
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