Table 1.

Ability of Additives to Protect LDH and Some of Their Physical Properties

Additive	g/L for 50% activity	Mole ratio for 50% activity	pI	MW (kDa)	# residues	Hphoba	Hphoba density	Charge at pH 7	Sequence charge density, pH 7	Surface hydrophobicity59
BSA	6.4	130	4.8	66	583	−279.2	−0.48	−13.9	−0.024	0.545
CAHS D	4.0	220	6.0	25.5	227	−223.5	−0.99	−3.1	−0.014	n/db
CAHS G	3.6	110	5.9	45.5	414	−341.5	−0.82	−5.1	−0.012	n/db
SH3	2.3	460	4.8	6.8	59	−85.8	−0.95	−5.6	−0.095	0.596
FlgM	1.4	180	9.1	10.6	97	−59.8	−0.62	1.9	0.020	n/db
Ubiquitinc	0.84	140	8.5	10.4	90	−85.8	−0.95	2.4	0.027	0.491
Lysozyme	n/dd	n/dd	9.0	14.3	129	−60.9	−0.47	7.9	0.061	0.471
LDH – 1e	n/af	n/af	6.0	147	1336	−186.6	−0.002	−18	−0.013	n/af
LDH – 2e	n/af	n/af	6.5	146	1334	−347.4	0.011	−9	−0.007	n/af
LPL	n/af	n/af	8.5	107	956	−499.8	−0.15	11	0.012	n/ab , f

^aHphob, Kyte, and Doolittle hydrophobicity.60

^bn/d, not determined because there is no PDB.

^cCalculations account for His tag.58, 61

^dn/d, not determined because lysozyme inactivates LDH in solution.

^eIsozymes LDH – 1 and LDH – 2 are both present in commercial LDH.

^fn/a, not applicable because these are test enzymes, not additives.