ライフサイエンスコーパス: enzyme stability

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1 ften result in a cost in the form of reduced enzyme stability.

2 ermined to gain insight into the increase in enzyme stability.

3 in A. aeolicus KDO8PS is not to increase the enzyme stability.

4 04N, that compromise active site function or enzyme stability.

5 Removal of the C(21) domain enhanced the enzyme stability.

6 without compromising catalytic activity and enzyme stability.

7 ive sites has come at a considerable cost to enzyme stability.

8 ct higher loading of viable NaR and improved enzyme stability.

9 t bound pyridine nucleotide is important for enzyme stability.

10 though cold acclimation results in increased enzyme stability.

11 h of JGW altered substrate specificities and enzyme stabilities.

12 linked directly to incremental increases in enzyme stability and activity maxima and corresponded to

13 ), which might be due to a trade-off between enzyme stability and activity with thermostable enzymes

14 ation of enzyme autodigestion, and increased enzyme stability and activity.

15 and its microenvironment in determining the enzyme stability and catalysis using human placental (PL

16 This has long been explained in terms of enzyme stability and catalytic activation energy, but re

17 discovery of a remarkably broad pH range of enzyme stability and catalytic activity led to an effici

18 n at the glycosylation site causes decreased enzyme stability and diminished catalytic activity.

19 nd mechanistically, the relationship between enzyme stability and function was investigated by substi

20 gested structural reasons for the diminished enzyme stability and hence for deficiency.

21 Poor enzyme stability and low absorption appeared to limit ly

22 f the Asn-67 site had only modest effects on enzyme stability and processing.

23 ely reduces catalytic activity but preserves enzyme stability and structure.

24 ors for whole blood analysis, to enhance the enzymes stability and to protect the transducer from bio

25 The pH dependencies of mutant enzyme stabilities are distinct from those of the wild t

26 ell-based stability assay, IDESA (intra-DHFR enzyme stability assay), where stability is coupled to c

27 The relationships between enzyme stability, catalytic activity, and flexibility fo

28 on was monitored and the assay optimized for enzyme stability, cell viability and sensitivity.

29 We propose a new strategy to improve the enzyme stability, construction and sensitivity of a mult

30 However, at pH 4.0 the enzyme stability decreased, reaching inactivation levels

31 edge, this is the first direct evidence that enzyme stability in a room temperature glass depends upo

32 and viscosity of the formulation increased, enzyme stability increased.

33 Wild-type enzyme stability is correlated with the ionization of gr

34 ions suggesting a role for these residues in enzyme stability, solubility, or catalysis.

35 lighting the limitations of high-temperature enzyme stability studies.

36 influence biotransducer performance such as enzyme stability, substrate interference, mediator selec

37 also produced a more than 6-fold increase in enzyme stability (t((1/2)) at 37 degrees C).

38 There was a significant decrease in the enzyme stability toward urea- or temperature-induced den

39 heuristic approaches that attempt to predict enzyme stability using macroscopic properties, molecular

40 Across multiple enzymes, acyl enzyme stability was assessed by mass spectrometry.

41 Enzyme stability was higher than PPO activities found in

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