• Journal of the Korean Society of Food Science and Nutrition
• /
• v.43 no.4
• /
• pp.530-536
• /
• 2014

In this study, we investigated the quality and antioxidant activity of wet noodles fortified by adding brown rice and sorghum powders. Wet noodles were divided into four groups: WN-p (wheat flour 100%, purified salt 2%), WBN-b (wheat flour 80%, brown rice powder 20%, bamboo salt (${\times}1$) 2%), WBSN-b (wheat flour 80%, brown rice powder 10%, sorghum powder 10%, bamboo salt (${\times}1$) 2%), and WSN-b (wheat flour 80%, sorghum powder 20%, bamboo salt (${\times}1$) 2%). The wet noodles were evaluated for their quality characteristics and capacities to scavenge free radicals. The weight, volume, capacity to absorb water, and turbidity of cooked WBSN-b were close to those of cooked WN-p. Springiness, cohesiveness, and chewiness of cooked WBSN-b were the highest among all cooked noodles added with brown rice or sorghum powders and textural properties of cooked WBSN-b were not significantly different from WN-P. In the sensory evaluation, the overall acceptance of WBSN-b received the highest score of 6.4 points, which was higher than the score for WN-p. DPPH and hydroxyl radical scavenging activities increased significantly with addition of brown rice and sorghum powder, and radical scavenging activities of WBSN-b and WSN-b were the highest. In conclusion, wet noodles added with 10% brown rice powder, 10% sorghum powder, and 2% bamboo salt (${\times}1$) exhibited the same quality properties of WN-p. Addition of 10% brown rice powder, 10% sorghum powder, and 2% bamboo salt (${\times}1$) increased the sensory and antioxidant activities of wheat flour noodles.

• Korean journal of food and cookery science
• /
• v.26 no.1
• /
• pp.104-109
• /
• 2010

Korean Chinese cabbage (Brassica campestris L. ssp. pekinensis) is one of the major cruciferous vegetables. Cruciferous vegetables contain a series of relatively unique secondary metabolites of amino acids called glucosinolates. Although glucosinolates do not appear to be bioactive, they are hydrolyzed by plant myrosinase when the cells in plants are damaged, and release biologically active compounds such as isothiocyanates, nitriles, and thiocyanates. The objective of this study was to determine the myrosinase activity and total glucosinolate levels of Korean Chinese cabbages by different salting times (0, 12, 18, and 24 h) and salt concentrations (6, 10, 14%). The total water content, salt content, and pH of brined cabbages decreased with increasing salting time. The myrosinase activity as determined by a glucose kit, decreased with increasing salting time and salt content. The total glucosinolates were purified using an anion exchange column and measured by UV-visible spectrophotometer. The fresh Korean Chinese cabbages contained $25.38{\pm}1.45\;{\mu}mol/g$ dry weight of glucosinolates. However, the total glucosinolates of brined cabbages decreased with increasing salting time and salt concentration. After 24 h of salting time, the total glucosinolates of brined cabbages rapidly decreased by $16.12{\pm}11.09$, $11.25{\pm}10.91$, $9.29{\pm}10.73\;{\mu}mol/g$ in 6%, 10%, and 14% salt solution, respectively. Overall, the total glucosinolate levels of Korean Chinese cabbages were found to vary inversely with salting time and salt concentration.

• Food Science and Preservation
• /
• v.18 no.2
• /
• pp.256-265
• /
• 2011

To investigate the effect of a solar salt on Kimchi fermentation, Chinese cabbages were brined with four-years aged solar salt (FS), one-year aged solar salt (OS), and purified salt (PS). The Kimchi was fermented at $7^{\circ}C$ for 33 days. The changes in pH and acidity of the Kimch brined with PS was slower than those of Kimchis brined with FS and OS. In the Kimchis with FS and OS, lactic acid bacteria (LAB) counts increased from 7.10~7.22 log CFU/mL at 0 day to 9.26~9.42 log CFU/mL at 12 days, after which counts slightly decreased to 8.04~8.75 log CFU/mL by 33 days of fermentation. The LAB counts of the kimchi with PS slowly increased from 7.24 log CFU/mL at 0 day to 8.99 log CFU/mL at 27 days, after then which counts sharply decreased to 7.92 log CFU/mL by 33 days of fermentation. Yellowness (b) color values of the kimchi with PS (59.10) was higher than the Kimchi with FS (53.68) and the Kimchi with OS (53.77). Hardness of the Kimchi with FS was more firm than the other Kimchis after 33 days storage. Sensory evaluation of the Kimchi with FS showed higher score than that of the other Kimchis.

• BMB Reports
• /
• v.36 no.4
• /
• pp.390-398
• /
• 2003

The CDP/Cux transcription factor was previously shown to be proteolytically processed at the G1/S transition. In view of characterizing and eventually identifying the protease responsible for CDP/Cux processing, we have established an in vitro proteolytic processing assay. CDP/Cux recombinant proteins expressed in mammalian or bacterial cells were efficiently processed in vitro using as a source of protease either whole cell extracts, the nuclear or the cytoplasmic fraction. Processing was found to take place optimally at a lower pH, to be insensitive to variations in salt concentration, and to be inhibited by the protease inhibitors MG132 and E64D. Interestingly, the bacterially-produced substrate was more efficiently processed than the substrate purified from mammalian cells. Moreover, processing in vitro was more efficient when CDP/Cux substrates were purified from populations of cells enriched in the S phase than in the G1 phase of the cell cycle. Altogether, these results suggest that post-translational modifications of CDP/Cux in mammalian cells inhibits processing and contributes to the cell cycle-dependent regulation of processing. The in vitro processing assay described in this study will provide a useful tool for the purification and identification of the protease responsible for the processing of CDP/Cux.

• BMB Reports
• /
• v.29 no.5
• /
• pp.436-441
• /
• 1996

The palmitoyl acyl carrier protein (ACP) specific thioesterase (EC 3.1.2.14) from Iris pseudoacorus was purified and characterized. The thioesterase which was very unstable in relatively high salt concentrations was eluted using a co-gradient of Triton X-100 and low concentration of KCl or Na-phosphate from Q-Sepharose, DEAE-Sepharose, and hydroxyapatite chromatography. SDS-PAGE analysis showed a single band with a molecular weight of 35,000. The native molecular weight of approximately 37,000 was estimated by Sephacryl S-200 chromatography, indicating that the enzyme is a monomer. The thioesterase activity was inhibited about 75% and 50% by N-ethylmaleimide (2 mM) and phenylmethylsulfonyl fluoride (2 mM). respectively. The N-ethylmaleimide-inactivation was protected by sodium palmitate but the inactivation with phenylmethylsulfonyl fluoride was not protected. Oxidation of thiols by 2 mM 5.5'-dithio-bis-(2-nitrobenzoic acid) resulted in 65% inactivation of the enzyme. These results suggest that a cysteinyl residue is essential to the catalytic reaction of the enzyme. The enzyme activity was increased by sodium citrate and also by $Cu^{2+}$

• Biotechnology and Bioprocess Engineering:BBE
• /
• v.11 no.1
• /
• pp.32-37
• /
• 2006

In this study, we have purified and characterized the membrane bound nitrate reductase obtained from the denitrifying bacteria, Ochrobactrum anthropi SY509, which was isolated from soil samples. O. anthropi SY509 can grow in minimal medium using nitrate as a nitrogen source. We achieved an overall purification rate of 15-fold from the protein extracted from the membrane fraction, with a recovery of approximately 12% of activity. The enzyme exhibited its highest level of activity at pH 5.5, and the activity was increased up to $70^{\circ}C$. Periplasmic and cytochromic proteins, including nitrite and nitrous oxide reductase, were excluded during centrifugation and were verified using enzyme essay. Reduced methyl viologen was determined to be the most efficient electron donor among a variety of anionic and cationic dyestuffs, which could be also used as an electron donor with dimethyl dithionite. The effects of purification and storage conditions on the stability of enzyme were also investigated. The activity of the membranebound nitrate reductase was stably maintained for over 2 weeks in solution. To maintain the stability of enzyme, the cell was disrupted using sonication at low temperatures, and enzyme was extracted by hot water without any surfactant. The purified enzyme was stored in solution with no salt to prevent any significant losses in activity levels.

• KSBB Journal
• /
• v.5 no.2
• /
• pp.183-189
• /
• 1990

An efficient method has been developed for the purification of urokinase from 1, 000 liter batches of human urine. The procedure involved precipitation of urokinase with 2mM zinc chloride, resuspension of the precipitate with 0.1M EDTA/0.5M Glycine solution, and CM-Toyopearl and benzamidine-Sepharose column chromatography. The purified urokinase was fully active and possessed a specific activity of 1.07$\times$105IU/mg. The recoveries ranged from 42 to 65% in several preparations(mean value was 51%). And the urokinase purified by this process consisted of about 13% of single chain urokinase (pro-urokinase) as evaluated by SDS-polyacrylamide gel electrophoresis in reducing condition and by S-2444 amldolytic activity under plasmin treatment.

• Microbiology and Biotechnology Letters
• /
• v.22 no.5
• /
• pp.485-490
• /
• 1994

A restriction endonuclease, PsyI, has been isolated from Pseudomonas syringae pv. pha- seolicola, and its catalytic properties have been studied. This enzyme was purified through strepto- mycin sulfate and ammonium sulfate fractionation, phosphocellulose Pll, DEAE-cellulose, hydroxy- apatite and Sephadex G-100 column chromatography. It's molecular weight was about 50,000 dalton as determined by 7.5% polyacrylamide gel electrophoresis containing 0.1% SDS. In catalytic proper- ties, PsyI shows stable at wide ranges of pH between 7.0 and 10.0, of temperature between 30$\circ$C and 37$\circ$C, and its thermal stability is between 25$\circ$C, and 45$\circ$C, at the presence Of 10 mM MgCl$_{2}$-PsyI essentially require Na salt for enzyme reaction, is rather inhibited in the high Na salt concent- ration. The presence of 2-mercaptoethanol is absolutely required for the enzyme activity. This endonuclease, PsyI was determined to be an isoschizomer of SalI from the results of the restriction mapping and DNA sequencing.

• Korean Journal of Food Science and Technology
• /
• v.18 no.6
• /
• pp.485-491
• /
• 1986

Gulbi were made by salting fresh Yellow corvenia (Pseudosciaena manchurica) in three ways; the dry salting method with bay-salt, the dry salting method with purified salt or the abdominal brine injection method with purified salt. Half of the sample was dried by controlling temperature and relative humidity and the other part was dried under the natural condition. The moisture content of the samples were decreased more rapidly by the controlled system than by the natural condition. The lipid content and the iodine values of the muscle and skin of the Gulbi were decreased slowly with laps of drying period. The peroxide values of the sample were increased to its peak after 10 days of drying, and were decreased rapidly thereafter. Both acid values and the thiobarbituric acid values were increased. The deterioration of lipids during Gulbi processing was not notable depending on the salting method, but the natural drying condition affected more severely in their deterioration.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.15 no.3
• /
• pp.263-275
• /
• 1986

Gulbi were processed by salting Yellow corvenia (Pseudosciaena manchurica) with in three ways: the dry salting method with bar salt, the dry salting method with purified salt or with the abdominal brine injection method with purified salt. The half of the sample was dried by the control system of temperature and humidity; the other part was dried by the natural condition. The moisture content of fresh Yellow corvenia muscle and eggs were 76.8%, and 68.2% while those of dried samples decreased to 57.7% and 45.3%, respectively. The total nitrogen content of fresh muscle and eggs were 11.0g% and 7.6g%, respectively (dry weight basis), which decreased slightly during salting and showed no significant changes during drying prosess. The protein nitrogen content of fresh muscle and eggs were 10.2g% and 7.5g%, which decreased during Gulbi processing. On the other hand, the nonprotein nitrogen content of both muscle and eggs increased. The content of free amino acids of fresh muscle and eggs were 508.8mg/100g and 1,110.6mg/100g, which increased to between 5.3 and 2.7 times, respectively after 25 days of drying. The composition patterns of free amino acids in muscle and eggs were similar to each other. The four amino acids - Ala, Glu, Lys and Leu - were most abundant in both fresh and dried samples. These amino acids are known as taste and flavour constituents.