• Journal of Animal Science and Technology
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• v.44 no.6
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• pp.727-738
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• 2002

This study was conducted to investigate the effect of essential amino acid(EAA) deficient diets on short-term feeding response and the Fos expression in brain area when methionine deficiency diet fed, and thereby to know the mechanism of feed intake regulation. In all trials, experimental diets were formulated with pure amino acid mixture to level of 15% nitrogen. Rats were adapted to a 6-hr single-meal feeding per day(17:00${\sim}$21:00). Feed intake and body weight were monitored every hour after 7-day of feeding of individual EAA deficient diets in Exp. Ⅰ. In Exp. Ⅱ, Fos immuno- histochemistry was determined in various regions of brain to identify the regions that is related to suppressed feed intake following feeding methionine-deficient diet. Fos expression was examined to know the initial sensitive region in the brains of rats at 3h after feeding of the control and methionine deficient diet(-Met). Initial response to EAA deficiency diets was severely depressed in methionine deficiency diet, but the depression was low in threonine deficiency diet. However, the feed intake at 3rd day in rats was depressed in the order of His(71%), Leu(68%), Ile(66%), Thr(63%), Trp(61%), Val(55%), Phe(52%), Met(51%), Lys(44%) and Arg(24%). Fos immunoreaction in neural regions(PPC, amygdala and EPC) of pyrifrom cortex was increased in the -Met group more than in the control diet group, but those in LH, VMH and PVM were similar. Thus, based on these data, the PPC was identified as the initial response area in the -EAA diet.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.35 no.5
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• pp.424-439
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• 1990

The protein content of seed meal were examined to evaluate genotypes of higher protein content from 164 peanut germplasms. The variations in amino acids content were investigated from nine Korean leading varieties grown at five locations. Amino acids contents of protein fractions were also ana lysed in the present study, too. The results of the study were summarized as fallows. The seed protein of 164 peanut varieties averaged 24.5% ranging from 19.5% to 28.7%, showed 9.2% varietal variation in proteins. Differences were not observed in protein content between plant types, however, protein contents were higher in small-seeded than large seeded varieties. The differences were more greater particulaly in Spanish type varieties. The varieties introduced from Taiwan and Philippine showed higher protein contents, and the cultivars or lines bred in Korea and introduced from Japan were lower in protein contents. protein contents showed non-significantly negative correlations with 100-kernel weight and pod weight per plant, but positive correlations were observed between oil and protein content in all types of peanuts. Significant differences among the varieties and locations were observed for total, essential and non-essential amino acids contents, and aspartic acid. Locational differences for arginine, lysine, methionine, threonine, glutamic acid, glycine and tyrosine, and varietal difference for phenylalanene were revealed as significant. The limiting amino acids from the leading varieties were isoleucine, methionine, threonine, alanine and tyrosine, comparing with FAO recommanding levels of amino acids. Among the protein fractions prolamins was the highest in total amino acids, but essential amino acids was the highest in globulins

• Korean Journal of Food Science and Technology
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• v.28 no.6
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• pp.1164-1170
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• 1996

Studies were carried out to investigate the changes of constituent components in chestnuts (Castanea crenata Sieb. et Zucc) during storage at $20^{\circ}C$ for 9 weeks and $1^{\circ}C$ for 15 weeks. Ascorbic acid content of chestnut was 4.08 mg% in oxidized form and 17.7 mg% in reduced form which was 81.3% of total ascorbic acid. The reduced form gradually decreased during storage, while the oxidized forms increased during 5 weeks at $20^{\circ}C$ and 7 weeks at $1^{\circ}C$. The major organic acids in chestnut were malic acid, citric acid and quinic acid. Citric acid significantly decreased during storage, while malic acid increased during storage at $20^{\circ}C$ and decreased at $1^{\circ}C$. Free sugars in chestnuts were identified as glucose, fructose, sucrose and maltose. Glucose and fructose decreased after 5 weeks storage at $20^{\circ}C$ followed by an increase thereafter. Sucrose and maltose also increased. The major free amino acids in the chestnut were glutamic acid, aspartic acid, arginine, alanine, proline and serine. Glutamic acid, arginine, alanine, threonine, phenylalanine, valine and lysine increased during storage at $20^{\circ}C$, while proline, serine, isoleucine. leucine and ${\gamma}-aminobutyric$ acid decreased.

• Food Science and Preservation
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• v.9 no.4
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• pp.375-379
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• 2002

This study has been carried out to investigate the food chemical composition in dried powder of main and lateral root of Acorus calamus L. Content of crude protein and crude fat in dried powder of main and lateral root were 12.76% and 9.84%, 7.43% and 3.42%, respectively. Total and reducing sugar of main and lateral root were 21.99％ and 7.67%, 24.12% and 0.65%. Major free sugars of root were sucrose, stachyose, raffinose, glucose and fructose. Sucrose of main and latent not were found to be the most predominant free sugars, contained 10.85 ％ and 1257%. Content of total amino acid were 427 mg% of main mot and 470 mg% of lateral root. Major total amino acids of root were arginine, glutamic acid, major free amino acids of main and lateral root were detected asparagine, arginine, glutamic acid and phenylalanine, respectively. Among the essential amino acids, the content of threonine was the highest (15.62 mg%) in main root and phenylalanine was the highest (12.67 mg%) in lateral root.

• Journal of Microbiology and Biotechnology
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• v.17 no.5
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• pp.721-727
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• 2007

Stability-enhanced mutants, H44, 11-94, 5A2-84, and F8, of L-threonine aldolase(L-TA) from Streptomyces coelicolor A3(2)(SCO1085) were isolated by an error-prone PCR followed by a high-throughput screening. Each of these mutant, had a single amino acid substitution: H177Y in the H44 mutant, A169T in the 11-94 mutant, D104N in the 5A2-84 mutant and F18I in the F8 mutant. The residual L-TA activity of the wild-type L-TA after a heat treatment for 20 min at $60^{\circ}C$ was only 10.6%. However, those in the stability-enhanced mutants were 85.7% for the H44 mutant, 58.6% for the F8 mutant, 62.1% for the 5A2-84 mutant, and 67.6% for the 11-94 mutant. Although the half-life of the wild-type L-TA at $63^{\circ}C$ was 1.3 min, those of the mutant L-TAs were longer: 14.6 min for the H44 mutant, 3.7 min for the 11-94 mutant, 5.8 min for the 5A2-84 mutant, and 5.0 min for the F8 mutant. The specific activity did not change in most of the mutants, but it was decreased by 45% in the case of mutant F8. When the aldol condensation of glycine and 3,4-dihydroxybenzaldehyde was studied by using whole cells of Escherichia coli containing the wild-type L-TA gene, L-threo-3,4-dihydroxyphenylserine(L-threo-DOPS) was successfully synthesized with a yield of 2.0 mg/ml after 20 repeated batch reactions for 100 h. However, the L-threo-DOPS synthesizing activity of the enzyme decreased with increased cycles of the batch reactions. Compared with the wild-type L-TA, H44 L-TA kept its L-threo-DOPS synthesizing activity almost constant during the 20 repeated batch reactions for 100 h, yielding 4.0 mg/ml of L-threo-DOPS. This result showed that H44 L-TA is more effective than the wild-type L-TA for the mass production of L-threo-DOPS.

• Animal Bioscience
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• v.37 no.6
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• pp.1053-1064
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• 2024

Objective: This study aims to investigate the interactive effect of a glycine equivalent (Gly_equi) and standardized ileal digestible threonine (SID Thr) levels in low crude protein diets on performance, blood biochemistry, pectoral muscular creatine content and oxidative stability of meat in broiler chickens from 21 to 42 days. Methods: A total of 1,500, twenty-one-day-old Cobb-Vantress male broiler chickens were distributed in a completely randomized 5×3 factorial arrangement of Gly_equi×SID Thr with five replicates of 20 birds each. Fifteen dietary treatments of 16.5% CP were formulated to contain five levels of total Gly_equi (1.16%, 1.26%, 1.36%, 1.46%, and 1.56%) and three levels of SID Thr (0.58%; 0.68% and 0.78%). Results: Interaction effects (p<0.05) of Gly_equi and SID Thr levels were observed for weight gain, carcass yield, pectoral muscular creatine content and serum uric acid. Higher levels of Gly_equi increased (p = 0.040) weight gain in 0.58% and 0.68% SID Thr diets compare to the 0.78% SID Thr diet. The SID Thr level at 0.68% improved (p = 0.040) feed conversion compared to other SID Thr diets. Levels of Gly_equi equal to or above 1.26% in diets with 0.78% SID Thr resulted in birds with higher (p = 0.033) pectoral muscular creatine content. The breast meat yield observed in the 0.68% SID Thr diet was higher (p = 0.05) compared to the 0.58% SID Thr diet. There was a quadratic effect of Gly_equi levels for pectoral pectoral muscular creatine content (p = 0.008), breast meat yield (p = 0.030), and serum total protein concentrations (p = 0.040), and the optimal levels were estimated to be 1.47%, 1.35%, and 1.40% Gly_equi, respectively. The lowest (p = 0.050) concentration of malondialdehyde in the breast meat was found in 0.68% SID Thr diets at 1.36% Gly_equi. Conclusion: The minimum dietary level of Gly_equi needed to improve performance in low crude protein diets is 1.26% with adequate SID Thr levels for broiler chickens.

• Korean Journal of Pharmacognosy
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• v.2 no.4
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• pp.173-175
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• 1971

By means of the two-dimensional thin-layer chromatography, free amino acid components of the leaves of $Perilla\;frutescens\;B_{RITTON}$ have been examined and twelve spots have been detected by the coloration with ninbydrin reagent. These were found to be aspartic acid, asparagine, alanine, phenylalanine, tryptophan, leucine, glutamic acid, proline, threonine, histidine, cystine, and glycine, tentatively.

• The Korean Journal of Zoology
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• v.7 no.1
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• pp.19-22
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• 1964

The free amino acid content of Indian meal moth (Plodia interpunctella HUBNER) was analysed at various developmental stages by means of paper chromatography. 1) The free amino acids : present are alanine , arginine, aspartic acid, glutamic acid, glycine, histidine, leucine, methionine, proline, serine, threonine, tyrosine and valine. 2) Proline was detectable only in the acid-hydrolyzed Indian meal moth. 3) Arginine was clearly detected only in the larva stage. 4) Tyrosine methionine and valine were increased in the pupa stage. 5) Serine, glycine and tyrosine were present in high concentration in all stages.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 2003.06a
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• pp.103-104
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• 2003

• 한국생물공학회:학술대회논문집
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• 2005.10a
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• pp.1007-1007
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• 2005