• KSBB Journal
• /
• v.26 no.4
• /
• pp.300-304
• /
• 2011

Phytases are hydrolytic enzymes that catalyze the sequential hydrolysis of phytic acid (myo-inositol-1,2,3,4,5,6-hexakisphosphate) to myo-inositols with lower numbers of phosphate groups. Two types of phytases have been identified which initiate hydrolysis of the phytic acid at either the 3- or 6- position of the inositol ring. In the present investigation, a mathematical model was proposed and computed to estimate maximum enzyme reaction rate constants which fit the experimental data obtained by other authors. Although the data points were scattered to some extent, good agreement was found between the model and the experiment data. It appears that the maximum rate constants of removal of the first, second, and third phosphate groups were not equal. Also there was neither a steady trend upward or downward in the rate constants with the stepwise hydrolysis reactions.

• The Korean Journal of Food And Nutrition
• /
• v.30 no.6
• /
• pp.1359-1363
• /
• 2017

The purpose of this study was that the optimal hydrolysis conditions of endo- and exo-type enzymes were selected to utilize organic cheese byproducts. Optimal substrate concentration and optimum enzyme ratio were measured by using 4 kinds of endo-type enzymes (alcalase, neutrase, protamex, and foodpro alkaline protease) and two exo-type enzymes (flavourzyme and prozyme 2000P) for whey protein hydrolysis were analyzed using liquid chromatography. As a result, the optimal endo-type enzyme through the first enzyme reaction was selected as alcalse, and as a result of the secondary enzyme reaction, flavourzme was selected as the Exo type enzyme. The concentration of whey protein substrate for optimal primary and secondary enzyme reactions was 10%. In addition, the optimum ratio of enzyme was 0.5% of alcalase and 0.2% of flavourzyme, which showed low molecular weight chromatography pattern compared to 2% of alcalase and 1% of flavourzyme hydrolyzate. Therefore, hydrolyzing the endo-type enzyme alcalase at a concentration of 0.5% for 10 hours and then hydrolyzing the exo-type enzyme flavouryme at a concentration of 0.2% for 4 hours was considered to be the optimum condition.

• Korean journal of food and cookery science
• /
• v.28 no.1
• /
• pp.51-55
• /
• 2012

This study was conducted to investigate the physicochemical properties of citrus peel extracts with different hot water extraction and enzymatic hydrolysis conditions. Enzymatic hydrolysis was also employed using Viscozyme L and results were compared with that of optimized hot water extract. Hot water extraction was performed under different parameters; the sample to solvent ratio(1:20, 1:15, 1:10), extraction time(2, 4 hrs), extraction temperature(85, $95^{\circ}C$) and enzymatic hydrolysis(0, 1%) and the subsequent extracts were used for determining their physicochemical properties, such as total yield, total phenolics, total flavonoids, and electron donating ability (EDA). With the increase in the sample to solvent ratio and extraction time, total yield, total phenolics, total flavonoids and EDA increased. But extraction temperature did not significantly affect the hot water extract. As hot water extract was hydrolyzed by the enzyme, total yield and active ingredients increased rapidly. In the result of total yield, total phenolics, total flavonoids and EDA, the activity of enzyme-treated extract was higher than those of enzyme-untreated extract. Based upon the overall hot water extraction efficiency, it was found that 20 times volume or 120 min at a time at $95^{\circ}C$ after enzyme treatment was optimal.

• Food Science of Animal Resources
• /
• v.27 no.3
• /
• pp.329-336
• /
• 2007

This study was designed to find the optimum conditions for converting isoflavone glycoside to aglycone by ${\beta}-galactosidase$. Three different forms of the enzyme were tested and the optimum enzyme concentration, incubation temperature, pH, and incubation time were determined. Before treatment with enzyme, isoflavone contained 89.4% glycoside including daidzin, glycitin and genistin, and only 10.6% aglycone including daidzein, glycitein and genistein. Among the enzymes tested, the highest rate of isoflavone hydrolysis to aglycone, 35%, was observed when 3 unit/g Fungal Lactase (Amano Enzyme) was used. Higher incubation temperatures resulted in a higher rate of hydrolysis along with a greater loss of isoflavone mass. Therefore, body temperature $(37^{\circ}C)$ may be adequate for isoflavone conversion, with 44.9% hydrolysis and less than 10% loss of mass. As expected, a higher amount of aglycone was produced at pH 7 compared with other pH values. During 5hr of incubation, the conversion of glycoside to aglycone increased dramatically from 0 to 1hr, and plateaued thereafter. In addition, commercial soy-based milk was hydrolyzed more effectively with ${\beta}-galactosidase$ when incubated for 5hr. Based on the above results, the optimum conditions for isoflavone hydrolysis by ${\beta}-galactosidase$ were for 3 hr at $37^{\circ}C$, pH 7 with 3 unit/g Fungal Lactase (Amano Lactase), yielding an average total amount of aglycone ranging from 40 to 47%.

• Natural Product Sciences
• /
• v.16 no.1
• /
• pp.1-5
• /
• 2010

$\beta$-Glucuronidases (E.C. 3.2.1.31) from Escherichia coli, Helix pomatia, and bovine liver activity have been investigated on 7-O-glucuronides (baicalin, wogonoside, and luteolin-7-O-glucuronide) and 3-O-glucuronides (quercetin-3-O-glucuronide and kaempferol-3-O-glucuronide). Bovine liver enzyme was not active on any of these substrates. E. coli and H. pomatia enzymes were active on 7-O-glucuronides, however, 3-O-glucuronides were resistant to $\beta$-glucuronidase hydrolysis. These results suggest that glucuronic acid at 7-position is more susceptible to E. coli and H. pomatia $\beta$-glucuronidases than that at 3-position. In addition, the subtle difference of aglycone structure on 7-O-glucuronides affected the preference of enzyme. E. coli enzyme was favorable for the hydrolysis of baicalin, however, H. pomatia enzyme was found to be efficient for the hydrolysis of wogonoside. Both enzymes showed the similar hydrolytic activity towards luteolin-7-O-glucuronide. When the Scutellaria baicalensis crude extract was subjected to enzymatic hydrolysis, baicalin and wogonoside were successfully converted to their aglycone counterparts with H. pomatia at 50 mM sodium bicarbonate buffer pH 4.0. Accordingly, the enzymatic transformation of glycosides may be quite useful in preparing aglycones under mild conditions.

• Journal of Microbiology and Biotechnology
• /
• v.31 no.6
• /
• pp.823-832
• /
• 2021

Mushroom cultivation along with the palm oil industry in Malaysia have contributed to large volumes of accumulated lignocellulosic residues that cause serious environmental pollution when these agroresidues are burned. In this study, we illustrated the utilization of lignocellulolytic enzymes from the spent mushroom substrate of Pleurotus pulmonarius for the hydrolysis of palm oil mill effluent (POME). The hydrolysate was used for the production of biohydrogen gas and enzyme assays were carried out to determine the productivities/activities of lignin peroxidase, laccase, xylanase, endoglucanase and β-glucosidase in spent mushroom substrate. Further, the enzyme cocktails were concentrated for the hydrolysis of POME. Central composite design of response surface methodology was performed to examine the effects of enzyme loading, incubation time and pH on the reducing sugar yield. Productivities of the enzymes for xylanase, laccase, endoglucanase, lignin peroxidase and β-glucosidase were 2.3, 4.1, 14.6, 214.1, and 915.4 U g^-1, respectively. A maximum of 3.75 g/lof reducing sugar was obtained under optimized conditions of 15 h incubation time with 10% enzyme loading (v/v) at a pH of 4.8, which was consistent with the predicted reducing sugar concentration (3.76 g/l). The biohydrogen cumulative volume (302.78 ml H₂.L^-1 POME) and 83.52% biohydrogen gas were recorded using batch fermentation which indicated that the enzymes of spent mushroom substrate can be utilized for hydrolysis of POME.

• Journal of Microbiology and Biotechnology
• /
• v.11 no.3
• /
• pp.362-368
• /
• 2001

The effects of water soluble materials in paper mill sludge on cellulase and $\beta$-glucosidase activities were studied while the optimization of enzyme system for hydrolysis of the paper mill sludge for production of glucose was made. Water soluble materials in the paper mill sludge showed stimulatory effect on carboxymethyl cellulose (CMC) activity, inhibitory effect on filter paper (FP) activity, and no effect on avicelase and $\beta$-glucosidase activities. CMC and ${\beta}$-glucosidase activities at 5 and 10, 5 or 10 and 10, and 10 and 10 U/ml were optimal for hydrolysis of 5, 10, and 20% of the paper mill sludge, respectively.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.24 no.3
• /
• pp.427-433
• /
• 1995

The optimal condition for hydrolysis of oyster was evaluated with proteases using response surface methodology(RSM). Among 11 commerical proteases, APLTM 440 was selected as the suitable protease for producing oyster hydrolysate on the basis of cost per unit enzyme activity. The effect of autolysis on degree of hydrolysis in oyster was negligible comparing to that of APL 440 protease treatment. From RSM and ridge analysis, the conditions favoring the highest degree of hydrolysis were pH 9.95, 61.1$^{\circ}C$, 2.64 hr reaction time, 49.2% substrate, and 0.35% enzyme/substrate ratio. Oyster hydrolysate prepared under optimal conditions shwoed virtually 51.98% of hydrolysis.

• KSBB Journal
• /
• v.26 no.4
• /
• pp.347-351
• /
• 2011

In this study, we investigated the effect of reaction factors on enzymatic hydrolysis of Hizikia fusiforme, which is brown algae in marine biomass resource, using commercial enzymes. The composition of H. fusiforme is 38.9% of reducing sugar, 4.8% of moisture, 17.8% of ash, and 38.5% of others. In the condition of 1-5% substrate, the increase of substrate concentration enhanced the increase of reducing sugar formation; however, the hydrolysis yield did not increase after 24 h. After reaction of 75 h, conversion yield of reducing sugar were obtained to 16.45%, 17.99%, and 14.55% at 1, 2.5, and 5% substrate, respectively. As a result of effect of enzyme amount, the formation of reducing sugar did not show considerable change at 1% substrate. However, in the condition of 2.5% substrate, the great change of reducing sugar formation was observed by the increase of enzyme amount. The conversion yields of reducing sugar were obtained to 18.77% and 22.83% at 1% and 2.5% substrate with 30% enzyme, respectively. As a result of heat treatment of biomass, the high yield was obtained in 2.5% substrate and the yields were increased to 0.06-7.2% by the heat treatment. This result will provide the basic information for production process of biofuels and chemicals from marine biomass H. fusiforme.

• Microbiology and Biotechnology Letters
• /
• v.20 no.1
• /
• pp.46-52
• /
• 1992

The optimum condition for the developement of a whey beverage from the concentrated whey was studied. Reverse osmosis system was used to obtain concentrated lactose from cheese whey. The hydrolysis degree of lactose by $\beta$-D-galactosidase was determined using HPLC (high performance liquid chromatography). The order of hydrolysis degree was 1:1, 2:l and 3:l concentrated lactose. It resulted from the concentrated salt which slightly inhibited $\beta$-D-galactosidase with constant enzyme dosage. The optimum condition for enzyme dosage was 2% in non-concentrated lactose, 3% in 2:l and 3% in 3:l concentrated lactose after 4 hours of reaction. When the 3:l concentrated lactose was used, more than 70% was hydrolyzed by 3% enzyme dosage. Furthermore the change of fermented whey by lactic acid bacteria was investigated. Based on the result of sensory test, the most favorable response was obtained at pH 4.2 and titratable acidity of 0.7% about 6 hours of fermentation at $37^{\circ}C$ with 2%: thermophilic starter.