1 eference (1.2-fold) for linoleic acid at its
optimum pH.
2 e the same or at least similar values of the
optimum pH.
3 The
optimum pH 4.2-4.6 for autocatalysis was different than
4 mol P1 cross-linked min-1mg-1 enzyme, at the
optimum pH 5.5.
5 s-Kell has an acidic pH
optimum (pH 6.0 to 6.5).
6 kDa), temperature maximum (80 degrees C), pH
optimum (pH 6.3), and isoelectric point (pH 4.5) that we
7 UNANA), all neuraminidases showed similar pH
optimums (pH 6-7) that were primarily defined by changes
8 arental and chimeric BglS presented the same
optimum pH (
6.0) and temperature (50 C) for maximum acti
9 nce of the endonuclease activity of Glu-274 (
optimum pH =
6.5) is distinct from that of the wild-type
10 o related proteases, in its more alkaline pH
optimum (pH 7-8), its relative resistance to calcium che
11 ix hydrolases, the enzyme has an alkaline pH
optimum (pH 8) and requires a divalent cation for activi
12 + with double-stranded substrates, a high pH
optimum (pH 8-9) and inhibition by monovalent cations.
13 The hydrolysis reaction is pH-dependent (
optimum pH =
9.5) and is slower, by a factor of 10(-5),
14 enzyme in hydrolysis of the covalent adduct (
optimum pH =
9.5).
15 Optimum pH,
affinity to MgATP and constants for the inhi
16 The correlation between the
optimum pH and base/acid ratio is significant if only bu
17 It was demonstrated that the
optimum pH and isoelectric point could be quite differen
18 Under
optimum pH and Mg(2+) conditions this ribozyme cleaves a
19 pecificity, requirement for lipid cofactors,
optimum pH and Mg2+, and other intrinsic properties.
20 The
optimum pH and solvents for extraction by SPE and potent
21 The
optimum pH and temperature for enzyme activity were pH 1
22 The
optimum pH and temperature for the chitinolytic activity
23 The
optimum pH and temperature for the proteolytic activity
24 The
optimum pH and temperature for xylanase activity were 4.
25 The
optimum pH and temperature of fructansucrase were found
26 zymes produced were very different regarding
optimum pH and they showed stability at 50 degrees C.
27 s and disfavors the bases tends to have high
optimum pH and vice versa.
28 duced a functional enzyme that had a neutral
optimum pH and was dramatically inhibited by low concent
29 18)O isotope effects at pH 5.7 (close to the
optimum pH)
and at pH 7.7 (away from the optimum pH) are
30 tase with respect to its Mg(2+) requirement,
optimum pH,
and sensitivity to cations, amino acids, and
31 the optimum pH) and at pH 7.7 (away from the
optimum pH)
are respectively 1.016 +/- 0.003 and 1.014 +
32 Furthermore, the Q224E mutant showed an
optimum pH at 6.2, which is 1.5 pH units lower than that
33 dent of the ionic strength, and exhibited an
optimum pH between 7.0 and 7.5.
34 The
optimum pH for As sorption by BC and MgBC sorbents is in
35 The
optimum pH for both reactions was 7.0.
36 The
optimum pH for cleavage is 5.0 (half-life, approximately
37 The
optimum pH for ethanol oxidation was between 9.4 and 10.
38 tein cleavage products are determined at the
optimum pH for generating tryptic fragments, directly fr
39 Optimum pH for maximum sorption was obtained at 6.0.
40 We demonstrate that the
optimum pH for methanogenesis by this organism is lower
41 ation followed first-order kinetics, and the
optimum pH for stability was determined to be between pH
42 The
optimum pH for the activity of free a-amylase was 7, but
43 The
optimum pH for the activity of free alpha-amylase was 7,
44 The
optimum pH for the binding of melamine was found to be 4
45 nts, thus suggesting that there should be an
optimum pH for the catalytic turnover.
46 donor (citrate-phosphate as pH buffer), the
optimum pH for the function of POD-A was 4.6, and the op
47 Optimum pH for the ligation reaction of the human telome
48 The
optimum pH for the removal of Cu(2+) ions by CA-BS was a
49 The
optimum pH for this reaction is 5.0.
50 Immobilised enzyme showed a shift in the
optimum pH;
however, optimum temperature remained unaffe
51 to Ru ratios are needed (100:1) and that the
optimum pH is near 5.0.
52 The RNase H has a basic
optimum pH,
is active only in the presence of reducing a
53 enzyme could also hydrolyse lactose, with an
optimum pH of 4.0 at 40 degrees C.
54 d F(10)/gammaA5 nanocomposites showcased the
optimum pH of 5 and contact time of 45 min for all sampl
55 th potato juice and the purified PPOs had an
optimum pH of 5 and were stable over a broad pH range (6
56 M13 substrate, the helicase activity had an
optimum pH of 7 to 7.5, an optimum temperature of 45 deg
57 A Km of 45 microM and an
optimum pH of 7-8 was observed with bradykinin as the su
58 n at different pH values (5.0-9.0) showed an
optimum pH of 7.0 with a complete transformation of SMX
59 At the
optimum pH of 7.0, the oxidation of LD occurs at a poten
60 n optimum temperature of 75 degrees C and an
optimum pH of 7.5.
61 enzyme requires Mg(2+) for activity, has an
optimum pH of 7.6, and is strongly stimulated by deterge
62 0 kDa) composed of ~70 kDa monomers, with an
optimum pH of 7.8.
63 of Syrian hamster Sc237 PrP(Sc) displays an
optimum pH of approximately 7, whereas amplification of
64 The
optimum pH of both FvXTH9 and FvXTH6 was 6.5.
65 The obtained results showed that the
optimum pH of DEE was decreased by 12.3% compared to FEE
66 eins, found experimentally to have different
optimum pH of maximal stability, were studied to reveal
67 The
optimum pH of the enzyme was 2.8 and it hydrolysed o-nit
68 Optimum pH (
pH 2.0 for pepsin) digested more protein, re
69 catalytic efficiency, but showed an altered
optimum pH preference for maximum activity.
70 ACS isozymes function as dimers and have an
optimum pH,
ranging between 7.3 and 8.2.
71 It was shown that the
optimum pH results from two factors - amino acid composi
72 Each enzyme has been characterized as to pH
optimum, pH stability, isoelectrofocusing and susceptibi
73 The
optimum pH,
temperature, and molecular weight for the en
74 The immobilized acrylamidase showed
optimum pH/
temperature of 8.5/65 degrees C, improved pH/
75 The pI of the protein, and
optimum pH/
temperature of enzyme activity were 4.4, 5 an
76 re was a tendency for proteins having acidic
optimum pHs to have a base/acid ratio smaller than one a
77 .96 x 10(-9) to 7.93 x 10(-8) mol L(-1), the
optimum pH value is 6.0 and response time is less than 1
78 , it was strongly dependent upon pH, and the
optimum pH value of 5.5 probably reflected the location
79 ificity constant k(cat)/K(m)(sulfite) at the
optimum pH value of 8.25.
80 It was shown that the
optimum pH values (pH of maximal stability) of the compl
81 The
optimum pH values of quantitative biosorption for Co(2+)
82 y) of the complex tend to be the same as the
optimum pH values of the complex components.
83 The
optimum pH was 8.25 and the enzyme displayed a strong de
84 The
optimum pH was determined in the numerical calculations
85 In many cases, the
optimum pH was found at a pH corresponding to a large ne
86 es C) was not changed by immobilization, the
optimum pH was shifted from 5.0 to 5.5.
87 or the pH of maximal stability (experimental
optimum pH)
was reproducible (rmsd = 0.73).
88 e their cargo will only be released when the
optimum pH window is reached.