Deactivation kinetics and the effects of additives on storage stability and structure of d-psicose 3-epimerase

被引:6
作者
Zhang, Qiao [1 ]
Jiang, Bo [2 ]
Zhang, Tao [2 ]
Duan, Zhenhua [1 ]
机构
[1] Hezhou Univ, Coll Food & Biol Engineer, Hezhou 542899, Peoples R China
[2] Jiangnan Univ, State Key Lab Food Sci & Technol, Wuxi 214122, Peoples R China
关键词
Ascorbic acid; Circular dichroism; Deactivation kinetics; Ethylene ghlycol; D-Psicose; 3-epimeras; Storage stability; Structure; D-TAGATOSE; 3-EPIMERASE; D-FRUCTOSE; ENZYME; STABILIZATION;
D O I
10.1007/s10529-017-2457-4
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
To explore deactivation kinetics and the effects of some additives on the activity and conformational changes of d-psicose 3-epimerase (DPEase) during its storage. The experimental data of DPEase inactivation during storage at 4-45 A degrees C fitted with the first-order expression model. The inactivation rate constants of DPEase stored at 4, 10, 25, 35 and 45 A degrees C were 0.0076, 0.01, 0.0223, 0.0351 and 0.0605 day, respectively. A regression formula of half-lives as storage temperatures, ln t (1/2) = 4.7396/T x 10(3) - 12.536, was obtained. MnSO4 at 0.15 g l(-1) enhanced the residual activity by 16% after 15 days and 17% after 30 days compared with control, but 2 g ascorbic acid l(-1) reduced activity by 69 and 58% at the same time. In addition, 0.15 g MnSO4 l(-1) and 20 g ethylene glycol l(-1) maintained the secondary and tertiary structure of DPEase. MnSO4 and ethylene glycol actively promoted the storage and conformational stability of DPEase. In contrast, ascorbic acid was disadvantageous.
引用
收藏
页码:173 / 179
页数:7
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