• Bulletin of the Korean Chemical Society
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• v.27 no.8
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• pp.1211-1218
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• 2006

The enantiomerically pure (2R,3S)- and (2R,3R)-3-amino-2-hydroxy-4-phenylbutanoic acids (AHPBA) 1 and 3 are readily obtained from D-glucono-a-lactone. Both AHPBAs are the structural key units of KMI derivatives which are the potent inhibitors of BACE 1 ($\beta$-secretase) and HIV protease. Additionally, the obtained AHPBAs 1 and 3 are converted to dipeptides of bestatin stereoisomers 2 and 4.

• Mycobiology
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• v.40 no.3
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• pp.173-180
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• 2012

A ${\beta}$-glucosidase from Penicillium italicum was purified with a specific activity of 61.8 U/mg, using a chromatography system. The native form of the enzyme was an 88.5-kDa tetramer with a molecular mass of 354 kDa. Optimum activity was observed at pH 4.5 and $60^{\circ}C$, and the half-lives were 1,737, 330, 34, and 1 hr at 50, 55, 60, and $65^{\circ}C$, respectively. Its activity was inhibited by 47% by 5 mM $Ni^{2+}$. The enzyme exhibited hydrolytic activity for p-nitrophenyl-${\beta}$-D-glucopyranoside (pNP-Glu), p-nitrophenyl-${\beta}$-D-cellobioside, p-nitrophenyl-${\beta}$-D-xyloside, and cellobiose, however, no activity was observed for p-nitrophenyl-${\beta}$-D-lactopyranoside, p-nitrophenyl-${\beta}$-D-galactopyranoside, carboxymetyl cellulose, xylan, and cellulose, indicating that the enzyme was a ${\beta}$-glucosidase. The $k_{cat}/K_m\;(s^{-1}mM^{-1})$ values for pNP-Glu and cellobiose were 15,770.4 mM and 6,361.4 mM, respectively. These values were the highest reported for ${\beta}$-glucosidases. Non-competitive inhibition of the enzyme by both glucose ($K_i=8.9mM$) and glucono-${\delta}$-lactone ($K_i=11.3mM$) was observed when pNP-Glu was used as the substrate. This is the first report of non-competitive inhibition of ${\beta}$-glucosidase by glucose and glucono-${\delta}$-lactone.

• Korean Journal of Food Science and Technology
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• v.29 no.6
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• pp.1131-1137
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• 1997

The production rates of leavening gases and textures of cookies were investigated with various chemical leavening agents(baking powders). The chemical leavening agents could be divided into three group of a fast-acting group such as potassium bicarbonate, tartaric acid, aluminium ammonium sulfate, and fumaric acid, a slow-acting group such as ammonium bicarbonate, sodium bicarbonate, $glucono-{\delta}-lactone$, and ammonium chloride. and a double-acting group such as anhydro monocalcium phosphate, disodium dihydrogenpyrophosphate, and aluminium potassium sulfate according to the different production rate of gases. The leavening rate of ammonium bicarbonate, which was the highest of all leavening agents used in this experiment, was 131.25%. But its after-taste in a cookie was not good due to the residual ammonia. $Glucono-{\delta}-lactone$ only had no after-taste. The higher leavening rate, the more peaks in texture profile graph. Ammonium bicarbonate showed the most peaks in this experiment. It was found that the number of peak had correlation with brittleness of cookies $(r^2=0.8176)$ and brittleness of cookies was different as to various chemical leavening agents.

• Journal of the Korean Society of Food Science and Nutrition
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• v.13 no.1
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• pp.9-14
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• 1984

This research aims to increase the extent of utilization of soybean curds coagulated with $Glucono-{\delta}-lactone$ (GDL) as a protein soarce by analyzing nutritive guality and preference to them. The curds were made from two kinds of soybean, domestic and imported. The results were as follows; 1. The yield of the domestic soybean curd was higher than that of the imported. 2. The total nitrogen and amino acid content of the GDL soybean curd were higher in the do- mestic while lipid and ash were higher in the imported one. 3. Rheological properties such as hardness, toughness, springiness and chewiness were higher in the domestic soybean curds than those of tile imported. 4. The 'L' values of the GDL soybean curds were higher in the domestic. However, there were no significant differences in the 'a' and 'b' values between the domestic and the imported soybeans. 5. According to the organoleptic the GDL soybean curds were not so favorable to our preferences .

• Journal of Microbiology and Biotechnology
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• v.21 no.5
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• pp.503-508
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• 2011

A ${\beta}$-glucosidase from Phoma sp. KCTC11825BP isolated from rotten mandarin peel was purified 8.5-fold with a specific activity of 84.5 U/mg protein. The purified enzyme had a molecular mass of 440 kDa with a subunit of 110 kDa. The partial amino acid sequence of the purified ${\beta}$-glucosidase evidenced high homology with the fungal ${\beta}$- glucosidases belonging to glycosyl hydrolase family 3. Its optimal activity was detected at pH 4.5 and $60^{\circ}C$, and the enzyme had a half-life of 53 h at $60^{\circ}C$. The $K_m$ values for p-nitrophenyl-${\beta}$-D-glucopyranoside and cellobiose were 0.3 mM and 3.2 mM, respectively. The enzyme was competitively inhibited by both glucose ($K_i$=1.7 mM) and glucono-${\delta}$-lactone ($K_i$=0.1 mM) when pNPG was used as the substrate. Its activity was inhibited by 41% by 10 mM $Cu^{2+}$ and stimulated by 20% by 10 mM $Mg^{2+}$.

• Korean Journal of Food Science and Technology
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• v.24 no.1
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• pp.42-48
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• 1992

The rate and extent of coagulation of milk using fast acidification with 0.1 N HCl were monitored by changes in viscosity and turbidity at various temperatures and pH. Also the gelation rate of milk using slow acidification with D-glucono-${\delta}$-lactone was measured in a small strain rheological scanner. Coagulation of milk casein occurred in a specific pH range and was accompanied by an abrupt increase in viscosity at pH 5.0. Acid coagulation rate was enhanced by increasing temperature from $20^{\circ}C{\sim}50^{\circ}C$, and the maximum rate was shown around pH 5.0. The addition of salt ($CaCl_{2}$) reduced the maximum coagulation rate at all temperature ranges and shifted the pH ranges for maximum coagulation rate and the onset pH of coagulation. The onset of gelation and the rate of network formation during slow acidification were facilitated by Cl ion, but suppressed by SCN-ion, as indicated by the rate of rigidity development. The susceptibility to syneresis was greater in the gel made at lower temperature and around pH 4.6, while preheated milk at $90^{\circ}C$ for 5 min prior to acidification showed the same syneresis profile at all heating temperatures ($60{\sim}90^{\circ}C$).