Table 1.

Summary of trehalose effect on several enzymes

Enzyme	M	Stabilization	Activation	>90% activity	>30% activity	Notes
MMLV RT	0.6	++	+	60/50	60/50	a
STyI	0.6	++	0	50/45	50/45
EcoRI	0.6	++	0	45/37	50/45
MluI	0.6	++	+	65/60	70/65
NcoI	0.6	++	+	60/55	>62.5/60
DNaseI	0.6	++	+	50/45	>60/55
RNaseI	0.6	+	+	50/45	>60/55
NdeI	0.6	+	+	55/nt	60/55
PvuII	0.6	+	0	45	50/45
PstI	0.6	+	0	37	45/37
DraI	0.6	0	0	50	55
HindIII	0.3	0/+	nt	65	70	b
HincII	0.6	0	nt	37	45
PNK	0.6	−	−	37	45
DNA pol (KF)	0.6	0/−	nt			b
β-Agarase	0.6	0/−	0/−	55	60	c
T3 RNA pol	0.6	−	−	37	45	d

Summary of trehalose effect on several enzymes. In the column M, the concentration of trehalose (mol/liter) is shown. In the column stabilization, ++ indicates thermostabilization (5–10°C); +, moderate stabilization (within 5°C); 0/+, possible slight stabilization; 0, no stabilization; 0/−, possible slight inhibition; and −, inhibition. In column Activation: +, activation; 0, no activation; 0/−, possible slight inhibition; −, inhibiton; and nt, not tested. In columns >90% activity and >30% activity, highest temperature tested at which enzymes still showed, respectively, activity that was difficult to distinguish from the maximal (>90%) and still partial activity (>30%). In bold are temperatures relative to enzymatic activity in the presence of trehalose, and in italics are temperatures of enzymes in the absence of trehalose. Temperatures of thermostabilization and thermoactivation are shown only if different from the control reaction. Notes: a, see further characterization; b, reaction in which the enzyme activity was too high before its inactivation thus complicating the detection of differences; c, a shift in the optimum temperature was observed, but an overall decrease in activity was caused by trehalose; and d, trehalose was inhibitory at high concentrations. Data are representative of three or more independent experiments. MMLV, Moloney murine leukemia virus; PNK, polynucleotide kinase; nt; not tested.