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1 though cold acclimation results in increased enzyme stability.
2 ften result in a cost in the form of reduced enzyme stability.
3 ermined to gain insight into the increase in enzyme stability.
4 in A. aeolicus KDO8PS is not to increase the enzyme stability.
5 04N, that compromise active site function or enzyme stability.
6 measured the tradeoff of enzyme activity and enzyme stability.
7 Removal of the C(21) domain enhanced the enzyme stability.
8 without compromising catalytic activity and enzyme stability.
9 ive sites has come at a considerable cost to enzyme stability.
10 ct higher loading of viable NaR and improved enzyme stability.
11 t bound pyridine nucleotide is important for enzyme stability.
12 immobilization methods, which could increase enzyme stability.
13 at generates waste and poses challenges with enzyme stability.
14 h of JGW altered substrate specificities and enzyme stabilities.
17 linked directly to incremental increases in enzyme stability and activity maxima and corresponded to
18 ), which might be due to a trade-off between enzyme stability and activity with thermostable enzymes
20 and its microenvironment in determining the enzyme stability and catalysis using human placental (PL
21 This has long been explained in terms of enzyme stability and catalytic activation energy, but re
22 discovery of a remarkably broad pH range of enzyme stability and catalytic activity led to an effici
23 significant advantages, including increased enzyme stability and control, resistance to environmenta
25 solvent-exposed residue Arg371 do not impact enzyme stability and folding but could modulate direct p
26 nd mechanistically, the relationship between enzyme stability and function was investigated by substi
28 nterface important for substrate binding and enzyme stability and interactions that explain the selec
32 mation of the desired product was limited by enzyme stability and product overoxidation, with these p
35 ors for whole blood analysis, to enhance the enzymes stability and to protect the transducer from bio
38 ell-based stability assay, IDESA (intra-DHFR enzyme stability assay), where stability is coupled to c
41 We propose a new strategy to improve the enzyme stability, construction and sensitivity of a mult
43 erstanding of the impact of this approach on enzyme stability has remained elusive, which is critical
44 edge, this is the first direct evidence that enzyme stability in a room temperature glass depends upo
45 ding landscape allows for the fine-tuning of enzyme stability in a species-dependent manner while ret
51 influence biotransducer performance such as enzyme stability, substrate interference, mediator selec
54 heuristic approaches that attempt to predict enzyme stability using macroscopic properties, molecular