• Journal of the Korean Society of Food Science and Nutrition
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• v.22 no.6
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• pp.811-814
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• 1993

Properties of a protease purified from Sarcodon asparatus(Berk.) S. Ito have been investigated. The enzyme displays as a glycosylated serine protease. The sequence for the 21 amino acids of the N-terminal side in the enzyme was determined by automated sequence analysis. The sequence was V-T-T-K-Q-T-N-A-P-W-G-L-G-N-I-S-T-T-N-K-L-.

• Korean Journal of Food Science and Technology
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• v.30 no.6
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• pp.1333-1338
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• 1998

Several enzymes of kimchi ingredients were assayed to improve the product quality using these quality related enzyme information. Among various hydrolases, amylase and protease were selected with respect to lactic acid fermentation. Peroxidase and ascorbic acid oxidase were studied for off flavor production and ascorbic acid destruction. The amount of protein in kimchi ingredients, specific and total enzyme activity of sample were compared. Regarding total enzyme activity of sample, ${\alpha}-amylase$ activity of salted and fermented anchovy, dried red pepper and salted and fermented shrimp were higher than other ingredients. Activity of salted and fermented anchovy was 2,790.0 units/g sample. Salted and fermented anchovy, oyster and Chinese radish showed the highest ${\beta}-amylase$ activity (4.4, 2.1, 1.0 units/g sample, respectively). Salted and fermented anchovy showed the highest protease activity of 13.4 PU/g sample, followed by salted and fermented shrimp and dried red pepper. For peroxidase, Chinese radish, cucumber, green onion showed the highest activity of 7.2, 6.8 and 5.6 units/g sample, respectively. In case of ascorbic acid oxidase, salted and fermented anchovy showed the strongest enzyme activity (331.4 units/g sample), followed by dried red pepper and salted and fermented shrimp.

• Food Science and Preservation
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• v.14 no.6
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• pp.617-623
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• 2007

To utilize the non-heat treated alcoholic by-products of brown rice(Goami) as food sources, the quality characteristics change according to the treatment conditions of ${\alpha}-amylase$ were evaluated. It resulted that the increase of hydrolysis temperature correspondingly increased the soluble solids, total dietary fiber and total sugar in the by-products of Goami, and the highest reducing sugar content was observed at $80^{\circ}C$. The free amino acids contents were tended to slowly decrease by the hydrolysis temperature more than $70^{\circ}C$, and the highest content of oligosaccharides were detected at the hydrolysis temperature of $80^{\circ}C$. The soluble solid according to the ${\alpha}-amylase$ concentration resulted to increase with the increase of the enzyme concentration and the total dietary fiber revealed similarly showing approximately 0.65%. The high content of reducing sugars was observed at the enzyme concentration around 0.08%(v/w). Total sugars and oligosaccharides contents tend to increase as the concentration of enzyme increased, and the content of oligosaccharides acquired at the enzyme concentration more than 0.10%(v/w) maintained to show rather similar contents. The soluble solids and total dietary fiber by hydrolysis time were found to show 6.66% and 0.65%, respectively at more than 60 min of hydrolysis, and the reducing sugars and total sugars were found to be 3,600 and 4,800 mg% in all treatment groups showing no significant difference. The content of oligosaccharides was increased with the increase of hydrolysis time, and the content was similar at more than 90 min of hydrolysis by ranging around 2,100 mg%. Based upon these results, the by-products of Goami are expected to be used as various food sources showing the highest dietary fiber and oligosaccharides contents by the hydrolysis at $80^{\circ}C$ for 90 min with the addition of 0.10%(v/w) of ${\alpha}-amylase$.

• Korean Journal of Agricultural Science
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• v.21 no.2
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• pp.142-147
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• 1994

Characteristics of TNP-cellulose which prepared from carboxymethyl cellulose powder, CM32, as substrate for cellulase activity assay were investigated. Enzymatic hydrolysis of TNP-cellulose occured on the cellulose moiety but not on amide bonds, following Michaelis-Menten kinetics. Three cellulase preparations from Trichoderma viride, Aspergillus niger, and Cellulomonas sp. were tested for their pH and temperature dependences and compared with the method determining the increase in reducing power. The enzyme activity was found to have the same temperature range in both methods, however the pH range was broadened in the case of using TNP-cellulose as substrate. The colorimetric method for cellulase assay using TNP-cellulose as substrate was compared with the other methods: one based on determination of the increase in reducing power; and the other based on determining the decrease in viscosity of Na-CM-cellulose solution. The activities measured by the colorimetric method showed a linear correlation with the enzyme concentration of certain range in all three enzymes tested, and the activity values were proportional to those obtained from the other methods. Depending on the enzyme, however, the activity values from this method were not always in proportion to those from the viscometric method. suggesting that this method was not specific for determination of the endo-type cellulase.

• Proceedings of the Korean Society of Food and Cookery Science Conference
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• 1997.11a
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• pp.519-529
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• 1997

젓갈류는 우리 고유의 수산발효식품으로서 아미노산이나 무기물 성분이 풍부하고 소화흡수도 양호하여 영양적으로 우수한 식품이다. 그러나 식염농도가 지나치게 높을 뿐만 아니라, 제품의 풍미는 서구식 식생활에 익숙해진 미래세대로부터는 외면 당하고 있어서 사실상 대량소비가 불가능하다. 이러한 문제를 해결하기 위하여 젓갈로부터 분리한 단백분해활성이 강한 효소를 생산하는 미생물을 고정화시켜, 다단계 가수분해법으로 가수분해액을 얻고 여기에 천연의 첨가물과 gum류를 첨가함으로써 새로운 풍미의 액젓류와 페이스트형 젓갈을 생산하는 방법을 제시하였다. 그리고 제품의 저장안전성을 위하여 액젓의 경우에는 전기저항가열법으로, 그리고 페이스트형 젓갈은 고압 증기가열법으로 살균하여야 함을 확인하였다. 그러나 보다 다양한 풍미의 제품의 다품종 소량생산을 위하여서는 앞으로 적절한 풍미의 발현을 위한 조리과학적 연구가 수행되어야 할 것으로 믿어진다.

• Microbiology and Biotechnology Letters
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• v.16 no.6
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• pp.484-488
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• 1988

Two forms of extracellular endo-inulinase, designated as PIand P II were resolved from a species of Pseudomonas isolated from soil. Both enzymes were glycoproteins with their carbohydrate content of 15% for PIand 2.4% for P II inulinase. Tryptophan residue was proved to be an essential amino acid for their catalytic activity. The molecular weights of PIand P II were estimated to be 210, 000 and 170, 000, respectively. The activity of the two enzymes was strongly inhibited by p-chloromercuribenzoate but the inhibition was nearly completely offset by the addition of the reducing agents such as cysteine or dithiothreitol. On the other hand, the two enzymes were activated about 50-60% of their activities by the presence of Co$^{+2}$ ion, and quite stable at pH values ranging from pH 4.0 to 1.5. They also appeared to be relatively thermostable, and no appreciable inactivation was observed after incubation at 55$^{\circ}C$ for 2 hours. About 70 % hydrolysis rate with PIand 56 % with P II were achieved when inulin was hydrolyzed at 5$0^{\circ}C$ for 12 hours with 60 units of the enzymes in 2 % inulin solution.

• Korean Journal of Food Science and Technology
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• v.39 no.3
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• pp.276-282
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• 2007

In this study, attempts were made to develop a garlic juice extraction method that would result in minimum changes in quality. Protopectinase and a mutienzyme containing cellulase, pectinesterase, ${\beta}-glucanase$, etc. were applied to garlic residue after first extraction, and the yields of garlic juice and the flavor component changes of the juices were investigated. Enzyme concentrations of 0.04, 0.08, and 0.12% which were based on pulp weight before extraction were added and allowed to hydrolyze for 30, 60, 90 and 120 min,. respectively. Increase in the garlic juice yield was observed according to the amount of enzyme added and the reaction time until reaching a maximum point. When 0.12% protopectinase was applied to the garlic residue for 90 min, the yield increased by 13.8%. Under the same conditions, when multienzyme was applied to the garlic residue, the yield increased by 14.5%, which was considered the maximum. The flavor compounds decreased when compared with the total GC peak area of garlic juice prepared without enzymes(control). The volatile flavor compounds in garlic juice prepared with 0.12% protopectinase for 60 min decreased by 6%. The free sugars profile of the garlic juice prepared with 0.12% protopectinase for 60 min was similar to that of the control. The type of enzyme used did not affect the free amino acid profile of the garlic juice. These results indicate that the optimum conditions for extraction of garlic juice are hydrolyzing the residue with 0.12% protopectinase for 60 min, extracting garlic juice from the hydrolyzed reside, and then combining the extracted juice with the first extraction.

• KSBB Journal
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• v.15 no.4
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• pp.352-358
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• 2000

Preparation for the simplified separation of chitosandoligosaccharides from enzymatic hydrolysate was investigated. Two different types of chitosan beads as substrate were prepared as organic-based bead by W/O emulsion method and water-based bead by alkaline treatement. The average size of organic-based bead was $200{\mu}m$, and that of water based beads were $4000{\mu}m$, $100{\mu}m$, $30{\mu}m$, in diameter respectively. Enzyme stability was maintained over 80% at PH 6 after 24 hours. The optimal condition for the production of chitosanoligosaccharides was at pH 6.0, $50^{\circ}C$ and 40U (200U/g-chitosan) According to final oligosaccharide concentration water-based bed showed the similar result with that of organic-based bead even through it had smaller surface area attacked by chitosanse than that of organic-based bead. It is probable that the structure of water-based chitosan bead was looser than that of organic-based bead so enzyme penetrated easily into the bead structure. For the oligosaccharide production versus surface area the different size of water-based beads was investigated, Maxiaml production yield was observed in the $30{\mu}m$ beads. Consequently the water-based chitosan bead was better than the organic-based bead in this reaction system.

• Korean Journal of Microbiology
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• v.52 no.4
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• pp.463-470
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• 2016

The enzymatic degradation of xylans is the most versatile way to obtain the high value-added functional compounds or the fermentable sugars for renewable energy. The endo-${\beta}$-xylanases are the major enzymes which hydrolyze the internal ${\beta}$-1,4-linkages of xylan backbones to produce the mixtures of xylooligosaccharides including xylobiose and xylotriose. Among them, glucuronoxylanase GH30 can exclusively hydrolyze the internal ${\beta}$-1,4-linkages of xylans decorated with methylglucuronic acid branches. In the present study, two xylanolytic enzyme (PaXN_10 and PaGuXN_30) genes were cloned from Paenibacillus amylolyticus KCTC 3005, and expressed in Escherichia coli, respectively. PaXN_10 (38.7 kDa) belongs to the endo-${\beta}$-xylanases GH10 family, while PaGuXN_30 (58.5 kDa) is a member of glucuronoxylanase GH30. They share the same optimal reaction conditions at $50^{\circ}C$ and pH 7.0. Enzymatic characterization proposed that P. amylolyticus can utilize the hardwood glucuronoarabinoxylans via the cooperative actions of xylanases GH10 and GH30. The extracellular PaGuXN_30 is secreted into the medium and hydrolyzes glucuronoarabinoxylans to release a series of aldouronic acid mixtures with a methylglucuronic acid branch. The resultant products being transported into the microbial cell are successively degraded into the smaller xylooligosaccharides by the intracellular PaXN_10, which will be utilized for the cellular metabolism.

• Korean Journal of Food Science and Technology
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• v.38 no.6
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• pp.793-798
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• 2006

We investigated the effects on the cytotoxicity against several cancer cells of the hydrolysis and molecular weight fractionation of crude laminaran from E. bicyclis, a brown seaweed collected from Uleung island in Korea, was extracted with boiling water and then crude laminaran was prepared by ethanol precipitation of extract obtained after elimination of calcium alginate by calcium chloride. Crude laminaran was hydrolyzed by enzyme (Econase CE), acid (0.1 N HCl) and autoclaving ($121^{\circ}C$, 180 min), and the molecular weight fractions by ultrafiltration to generate molecular weight fractions. Total sugar and sulfate contents of hydrolyzed laminaran were 72.3 and 3.5% (enzyme hydrolysate), 68.5 and 3.0% (acid hydrolysate), 70.2 and 3.2% (autoclaved), and monosaccharides of which consisted of glucose (74.7-78.5%), mannose (9.9-11.5%), galactose (8.5-9.6%) and fucose (3.1-4.5%), respectively. When the cytotoxicity of hydrolyzed laminaran on SNU-1, HeLa and SW cells was evaluated by MTT assay, growth-inhibitory activity of the enzyme hydrolysate against cancer cells was higher than that of acid hydrolysate or autoclaved laminaran. Furthermore, the fraction at a molecular weight range of 10 to 50 kDa revealed higher anti-proliferative activities. The $IC_{50}$ values of 10-50 kDa fraction at a molecular weight range of 10 to 50 kDa revealed higher anti-proliferative activities. The $IC_{50}$ values of 10-50 kDa fractions on SNU-1, HeLa and SW cells were 60.4, 58.6 and 53.9 ${\mu}g/mL$ for enzymatic hydrolysate, 75.6, 73.5 and 77.4 ${\mu}g/mL$ for acid hydrolysate, and 61.7, 68.2 and 60.8 ${\mu}g/mL$ for autoclaved, respectively.