• Food Science and Biotechnology
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• v.14 no.6
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• pp.860-865
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• 2005

A gene for a putative glucoamylase, stg, of a hyperthermophilic archae on Sulfolobus tokodaii was cloned and expressed in Escherichia coli. The recombinant glucoamylase (STGA) had an optimal temperature of $80^{\circ}C$ and was extremely thermostable with a D-value of 17 hr. The pH optimum of the enzyme was 4.5. Being different from fungal glucoamylases, STGA hydrolyzed maltotriose (G3) most efficiently. Gel permeation chromatography and sedimentation equilibrium analytical ultracentrifugation analysis showed that the enzyme existed as a dimer. STGA was stable enough to hydrolyze liquefied com starch to glucose in 4 hr at $90^{\circ}C$ with a yield of95%. Comparison of the $k_{cat}$ values for the hydrolysis and the reverse reaction at $75^{\circ}C$ and $90^{\circ}C$ indicated that glucose production by STGA was more efficient at $90^{\circ}C$ than $75^{\circ}C$. Therefore, STGA showed great potential for application to the industrial glucose production process due to its high thermostability.

• Korean Journal of Food Science and Technology
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• v.31 no.3
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• pp.651-657
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• 1999

These experiments focused on processing low sugar fig jam having marketability by selected substitute for extracted and purified pectinesterase (PE), colorant for colour improvement, food additive to make texture better, and stabilizer for stable storage. Cherry tomato pulp as PE substitute to hydrolyze pectin substance in fig pulp into low-methoxyl pectin was most effective among used vegetables and fruits pulp. Carmacid-R among natural colorants for imprving colour, addition of 20% starch syrup as sugar substitute for texture and addition of $MULTIPHOSE^{TM}$ for red colour change control at cold storage were effective. The low sugar fig jam processed by using the above selected materials showed higher score than others (typical jam and orange PE low sugar fig jam) for colour in sensory evaluation and did no significant difference in taste, odor, texture and overall acceptability.

• Applied Biological Chemistry
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• v.40 no.3
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• pp.220-224
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• 1997

As corn starches with different amylose content were heated at different temperature $(100^{\circ}C,\;121^{\circ}C)$ with starch / water ratio (1:3.5, 1:9) and heating-cooling treatment was repeated up to 4 times, the yield of RS(resistant starch) from heated corn starches was investigated by the enzymatic-gravimetric method and the ${\alpha}-amylase$ treatment. Compared to ${\alpha}-amylase$ method, enzymatic-gravimetric method was more effective to hydrolyze the amorphous region of heated corn starch. With increasing the amylose content and the number of heating-cooling treatment, the yield of RS increased, regardless of isolation method. Heated corn starches formed at $121^{\circ}C$ provided higher yield of RS than those formed at $100^{\circ}C$. Higher RS yield was also observed in the case of starch/water ratio (1:3.5) compared to the case of ratio (1:9).

• Korean Journal of Microbiology
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• v.43 no.3
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• pp.222-226
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• 2007

Proteases are degradative enzymes which hydrolyze a peptide bond between amino acids and they are abundantly applied to commercial field. In order to screen new source of pretense, bacteria secreting extracellular pretense were isolated by enrichment culture from deep sea water samples of East Sea, Korea. A bacterium, named as HJ19, showed the best growth and the largest clear zone in plates supplemented skim milk at $30^{\circ}C$. The partial DNA sequence analysis of the 16S rRNA gene, phenotypic tests and morphology identified that this strain was In genus Micrococcus. The strain HJ19 could not grow at $10^{\circ}C$ but it started growth and showed pretense activity at $20^{\circ}C$. The optimal growth was at $37^{\circ}C$ and the maximal protease activity at $30^{\circ}C$ was about 480unit/ml.

• Korean Journal of Microbiology
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• v.45 no.3
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• pp.257-262
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• 2009

Carboxymethyl celluase (cellulase) was purified from cell-free extract of the recombinant Escherichia coli carrying a Bacillus licheniformis WL-12 cellulase gene by DEAE-Sepharose and phenyl-Sepharose column chromatography with specific activity of 163 U/mg protein. The molecular mass of the purified enzyme was estimated to be approximately 49.5 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme had a pH optimum at 5.5 and a temperature optimum at $55^{\circ}C$. The activity of the enzyme was completely inhibited by SDS (5 mM), and slightly enhanced by $Cu^{2+}$ (5 mM). The cellulase was active on CMC, konjac, barely glucan and lichenan, while it did not exhibit activity towards xylan, locust bean gum, and p-nitrophenyl-$\beta$-glucopyranoside. The predominant products resulting from the cellulase hydrolysis were cellobiose and cellotriose for cellooligosaccharides including cellotriose, cellotetraose and cellopentaose. The enzyme could hydrolyze cellooligosaccharides larger than cellobiose.

• Journal of Applied Biological Chemistry
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• v.50 no.3
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• pp.109-114
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• 2007

Sar1p is a ras-related GTP-binding protein that functions in intracellular protein transport between the endoplasmic reticulum (ER) and the Golgi complex. The effector domain of Ras family proteins is highly conserved and this domain is functionally interchangeable in plant, yeast and mammalian Sar1. Using a recombinant Brassica sar1 protein (Bsar1p) harboring point mutations in its effector domain, we here investigated the ability of Sar1p to bind and hydrolyze GTP and to interact with the two sar1-specific regulators, GTPase activating protein (GAP) and guanine exchange factor (GEF). The T51A and T55A mutations impaired Bsar1p intrinsic GTP-binding and GDP-dissociation activity. In contrast, mutations in the switch domain of Bsar1 did not affect its intrinsic GTPase activity. Moreover, the P50A, P54A, and S56A mutations affected the interaction between Bsar1p and GAP. P54A mutant protein did not interact with two regulating proteins, GEF and GAP, even though the mutation didn't affect the intrinsic GTP-binding, nucleotide exchange or GTPase activity of Bsar1p.

• Applied Biological Chemistry
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• v.41 no.2
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• pp.119-124
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• 1998

In this study, the bacteria which could hydrolyze the fibrin produced through the blood coagulation mechanism in the human body, were isolated from Chungkookjang. The KCK-7 strain was selected among the isolated bacteria as the best strain for fibrinolytic activity. It was spore forming and Gram positive. $C_{150}$ anteiso fatty acid and $C_{150}$ iso fatty acid were 40.85% and 19.47%, respectively as major component among its cellular fatty acid composition. It showed the similarity of 63.6%, compared with standard strain. It was thus identified to be Bacillus subtilis according to Bergey's manual of systematic bacteriology and its fatty acid profiles af Gas chromatography. The optimum culture temperature and pH were $37^{\circ}C$ and 8 for the production of fibrinolytic enzyme by Bacillus subtilis KCK-7.

• Korean Journal of Food Science and Technology
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• v.15 no.4
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• pp.326-332
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• 1983

Acorn wine was manufactured experimentally with koji inoculated the strain producing acorn tannin hydrolyzing enzyme in order to apply fungal tannase to food processing. Starch value of several Korean acorns was found to be 72.84 and the acorns were worthy of use as a carbohydrate food. Mixed koji was prepared by combination of rice and acorn powder at a ratio of 50to 50 and inoculation of Aspergillus oryzae producing amylase and Aspergillus sp. AN-11 producing tannase into the mixture in order to hydrolyze efficiently acorn tannin inhibiting alcohol fermentation in the medium, and then the mixed koji was used as a suitable koji to manufacture acorn wine. Acorn wine brewed with medium of the acorn powder treated with water and cooked and the mixed koji prepared was superior about two times to that brewed with medium of untreated acorn powder and general koji with respect to the rate of alcohol production and sugar fermentation during the 1st and 2nd brewing.

• Journal of Life Science
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• v.8 no.2
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• pp.181-188
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• 1998

Two distinct ADP-ribosyltransferases, termed Yac-1 and Yac-2 from mouse lymphoma cells were recently cloned and characterized. Yac-1 enzyme possesses ADP-ribosyltransferases activity. In contrast, Yac-2 has significant NAD glycohydrolase activity and may preferentially hydrolyze NAD. Yac-2 possesses a glutamate at position 219 adjacent to the two consdrved glutamic acid residues. To study the effect of Glu-219 on enzyme activities, Glu-219 was mutagenized to Glutamine (E219Q) or alanine (E219A) using a two-step recombinant polymerase chain reaction procedure. Replacing Glu at position 219 with Gln or Ala resulted in 56 (E219Q) or 66% (E219A) reduction in ADP-ribosyltranferase activity. The NAD glycohydrolase activity of Yac-2 protein were not altered by the mutations. These results indicate that Glu-219 in Yac-2 enzyme plays an important role in ADP-ribosyltransferase, but not NAD glycohydrolase activity.

• Food Science of Animal Resources
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• v.37 no.1
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• pp.62-70
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• 2017

The aim of this study was identifying a suitable food grade enzymes to hydrolyze whey protein concentrates (WPCs), to give the highest bioactivity. WPCs from ultrafiltration retentate were adjusted to 35% protein (WPC-35) and hydrolyzed by enzymes, alcalase, ${\alpha}-chymotrypsin$, pepsin, protease M, protease S, and trypsin at different hydrolysis times (0, 0.5, 1, 2, 3, 4, and 5 h). These 36 types of hydrolysates were analyzed for their prominent peptides ${\beta}-lactoglobulin$ (${\beta}-Lg$) and ${\alpha}-lactalbumin$ (${\alpha}-La$), to identify the proteolytic activity of each enzyme. Protease S showed the highest proteolytic activity and angiotensin converting enzyme inhibitory activity of IC50, 0.099 mg/mL (91.55%) while trypsin showed the weakest effect. Antihypertensive and antioxidative peptides associated with ${\beta}-Lg$ hydrolysates were identified in WPC-35 hydrolysates (WPH-35) that hydrolyzed by the enzymes, trypsin and protease S. WPH-35 treated with protease S in 0.5 h, responded positively to usage as a bioactive component in different applications of pharmaceutical or related industries.