Contribution of Solid Food to Achieve Individual Nutritional Requirement during a Continuous 438 km Mountain Ultramarathon in Female Athlete.

Background: Races and competitions over 100 miles have recently increased. Limited information exists about the effect of multiday continuous endurance exercise on blood glucose control and appropriate intake of food and drink in a female athlete. The present study aimed to examine the variation of blood glucose control and its relationship with nutritional intake and running performance in a professional female athlete during a 155.

Application of Continuous Glucose Monitoring for Assessment of Individual Carbohydrate Requirement during Ultramarathon Race.

Background: The current study intended to evaluate the feasibility of the application of continuous glucose monitoring to guarantee optimal intake of carbohydrate to maintain blood glucose levels during a 160-km ultramarathon race.

Methods: Seven ultramarathon runners (four male and three female) took part in the study. The glucose profile was monitored continuously throughout the race, which was divided into 11 segments by timing gates.

Determination of hydrophobicity of dry-heated wheat starch granules using sucrose fatty acid esters (SFAE).

Sucrose fatty acid esters (SFAE) were adsorbed onto dry-heated (120 °C for 10, 20, 40, 60, and 120 min) wheat starch granules and extracted with ethyl ether in a Soxhlet apparatus without gelatinization of the starch granules. The amount of sucrose in the extracted SFAE was determined by the phenol sulfate method. A gradual increase of the sucrose from 159 to 712 μg, in SFAE per gram of starch, occurred with increasing dry-heating time and demonstrated the increased hydrophobicity of the starch granules.

Comparison of the wild-type alpha-amylase and its variant enzymes in Bacillus amyloliquefaciens in activity and thermal stability, and insights into engineering the thermal stability of bacillus alpha-amylase.

The starch hydrolysis activity and thermal stability of Bacillus amyloliquefaciens alpha-amylase (wild-type enzyme or WT) and its variant enzymes, designated as M77, M111, and 21B, were compared. All have an optimal pH at around 6, as well as almost the same reaction rates and Km and kcat values. The optimal temperature in the absence of Ca2+ ions is 60 degrees C for WT and M77 and 40 degrees C for M111 and 21B.

Comparison of starch hydrolysis activity and thermal stability of two Bacillus licheniformis alpha-amylases and insights into engineering alpha-amylase variants active under acidic conditions.

Bacillus licheniformis alpha-amylase (BLA) is widely used in various procedures of starch degradation in the food industry, and a BLA species with improved activity at higher temperature and under acidic conditions is desirable. Two BLA species, designated as PA and MA, have been isolated from the wild-type B. licheniformis strain and a mutant strain, respectively.

Dissociation/association properties of a dodecameric cyclomaltodextrinase. Effects of pH and salt concentration on the oligomeric state.

As an effort to elucidate the quaternary structure of cyclomaltodextrinase I-5 (CDase I-5) as a function of pH and salt concentration, the dissociation/association processes of the enzyme were investigated under various pH and salt conditions. Previous crystallographic analysis of CDase I-5 indicated that it existed exclusively as a dodecamer at pH 7.0, forming an assembly of six 3D domain-swapped dimeric subunits.

Inhibitory effects of alcohols on the activity of human matrix metalloproteinase 7 (matrilysin).

Aliphatic alcohols inhibited the activity of human matrix metalloproteinase 7 (matrilysin) competitively with K(i) of 6.1-19.4% (v/v) or 0.

Detection of antigen-antibody reaction using a fluorescent probe and its application to homogeneous competitive-type immunoassay for insulin.

The interaction of bovine insulin with anti-human insulin antibody (mAb) was examined using a fluorescent probe. The fluorescence intensity of fluoresceinthiocarbamyl (FTC)-insulin was increased by adding mAb, and the increase was saturated at 53% at a molar ratio of FTC-insulin to mAb of 2.0.

Anomalous pH-dependence of the activity of human matrilysin (matrix metalloproteinase-7) as revealed by nitration and amination of its tyrosine residues.

Matrilysin activity exhibits a broad bell-shaped pH-dependence profile, with pK(a) values of 4.0 and 9.8.

Substrate-dependent activation of thermolysin by salt.

Salt-activation of thermolysin was examined using a positively charged fluorescent substrate, (7-methoxycoumarin-4-yl)acetyl-L-Pro-L-Leu-Gly-L-Leu-[N(3)-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH(2) [MOCAc-PLGL(Dpa)AR]. Thermolysin activity increased in a biphasic exponential fashion and was 40 times higher in the presence of 4 M NaCl than in its absence. The degree of activation at X M NaCl was expressed as 4.

Inhibitory effect of 0.19 alpha-amylase inhibitor from wheat kernel on the activity of porcine pancreas alpha-amylase and its thermal stability.

The inhibitory effect of 0.19 alpha-amylase inhibitor (0.19 AI) from wheat kernel on the porcine pancreas alpha-amylase (PPA)-catalyzed hydrolysis of p-nitrophenyl-alpha-D-maltoside (pNP-G2) was examined.

Effect of nitration on the activity of bovine erythrocyte Cu,Zn-superoxide dismutase (BESOD) and a kinetic analysis of its dimerization-dissociation reaction as examined by subunit exchange between the native and nitrated BESODs.

Bovine erythrocyte Cu,Zn-superoxide dismutase (BESOD) is a dimeric enzyme composed of identical subunits associated through unusually strong non-covalent interactions. The state of the unique tyrosyl residue (Tyr 108) of BESOD was examined, and the kinetics of subunit exchange was studied using Tyr 108 as a probe. UV-absorption difference spectra demonstrate that Tyr 108 is exposed to the solvent, and that the accessibilities to ethanol, ethylene glycol, and polyethylene glycol 600 are 53.

Inhibitory effects of green tea catechins on the activity of human matrix metalloproteinase 7 (matrilysin).

Inhibitory effects of green tea catechins and their derivatives on the matrilysin-catalyzed hydrolysis of a synthetic substrate, (7-methoxycoumarin-4-yl)acetyl-L-Pro-L-Leu-Gly-L-Leu-[N(3)-(2,4-dinitrophenyl)-L-2,3-diamino-propionyl]-L-Ala-L-Arg-NH(2) [MOCAc-PLGL(Dpa)AR], were examined. The 10 catechins examined were classified into three groups according to their inhibition potency. Catechins with a galloyl group at the 3 position, including a major component of green tea catechin, (-)-epigallo-3-catechin gallate [(-)-EGCG], were the most potent inhibitors and inhibited matrilysin in a non-competitive manner with K(i) values of 0.