• Journal of Sericultural and Entomological Science
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• v.43 no.2
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• pp.67-76
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• 2001

The "crescent-egg" a new spontaneous mutant was detected in a white egg strain k37. Studies were carried out the linkage analysis, to investigate phenotypic characteristics and biochemical analysis of haemolymph and ovarian protein. The mutant, ore was independent from 20 linkage groups P(2), Ze(3),L(4), oc(5), sn8), Ia(9), w-1(10), K(11), ch(13), U(14), bl(15), cts(16), bts(17), mln(18), nb(19), oh(20),Lan(21), or(22), tub(23) and Xan(27). The fertilization, hatchability and larval growth were not different from the those of normal eggs. The content and composition of yolk protein were similared to normal eggs. Scanning electron microscopy revealed the areal specific structure in dorsal region of egg-shell of cre mutant. Analysis of chorion protein by isoelectrofocusing(IEF), was resolved no difference in the composite of the chorion protein. We conclude that the egg mutant ere is expressed only in the egg-shape formation and region specific determination.

• Journal of Sericultural and Entomological Science
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• v.42 no.2
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• pp.86-92
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• 2000

Studies were carried out to investigate the phenotypic characteristics of the non-molting mutant (nm-f) which was mapped on the 2nd linkage group. The results obtained were as follows : The nm-f mutant was distinguishable in the 3rd day of hatching. About 80 percentage of the non-molting mutant larvae died at the first instar within 10 days of hatching. The remaining larvae survived to the 2nd ad the 3rd instar but did not live to the final instar. There was no difference in non-molting nutant manifestation between hibernating and artificial hatching eggs. As a result of hemolymph protein analysis, the protein content on nm-f mutant was less than the normal larvae's. Therefore, we conclude that the characterization of nm-f is similar to the already known strains of non-molting mutant and the shortage of hemolymph protein is closely related to the non-molting characteristic in nm-f.

• Journal of Life Science
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• v.11 no.1
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• pp.43-47
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• 2001

A mutant tryptophan synthase $\alpha$-subunit, where Pro28 was replaced with Leu, tends to be expressed in recombinant E. coli. CD and fluorescence spectra of this protein indicate some changes in secondary and tertiary structure. Wild type protein was more or less affected by {TEX}$Ca^{2+}${/TEX} ion in regards of the fluorescent properties of its native, unfolded and intermediate forms, but the mutant protein was not at all. The dramatic structural changes may be related to the aggregation of this mutant protein.

• Journal of Microbiology and Biotechnology
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• v.4 no.4
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• pp.250-255
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• 1994

Wild-type and four mutant R100 merR genes were cloned and the proteins overproduced under tac promoter control of pKK223-3. His118Ala, Cys117Ser, Cys126Ser, and wild-type MerR were successfully overproduced although amino-terminal 14 amino acids deletion mutant MerR was not successful. The amount of overproduced wild-type MerR protein as well as other mutant MerR was between 15%-20% of the total protein. The protein was able to be purified up to 95% homogeneity. Specific DNA-protein blotting experiments showed that the 95 bp operator containing DNA fragment could bind to Cys126Ser, His118Ala, and wild- type MerR, but not to Cys117Ser. These results were consistent with the previously reported complementation experiment results that His118Ala, Cys126Ser, and wild-type MerR could repress the mer operon but Cys117Ser could not.

• Journal of Microbiology and Biotechnology
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• v.34 no.9
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• pp.1912-1918
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• 2024

Single-cell protein (SCP) derived from microorganisms is widely recognized as a viable alternative protein source for the future. Nevertheless, the commercialization of yeast-based SCP is hampered by its relatively low protein content. Therefore, this study aimed to enhance the protein content of Saccharomyces cerevisiae via random mutagenesis. To achieve this, S. cerevisiae KCCM 51811, which exhibited the highest protein concentration among 20 edible S. cerevisiae strains, was selected as a chassis strain. Subsequently, a KCCM 51811 mutant library was constructed (through UV irradiation) and screened to isolate mutants exhibiting high protein content and/or concentration. Among the 174 mutant strains studied, the #126 mutant exhibited a remarkable 43% and 36% higher protein content and concentration, respectively, compared to the parental strain. Finally, the #126 mutant was cultured in a fed-batch system using molasses and corn-steep liquor, resulting in a protein concentration of 21.6 g/l in 100 h, which was 18% higher than that produced by the parental strain. These findings underscore the potential of our approach for the cost-effective production of food-grade SCP.

• 한국생물공학회:학술대회논문집
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• 2002.04a
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• pp.528-530
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• 2002

We have previously reported recombinant deletion mutant was constructed from cycloinulo-oligosaccharide fructanotransferase(CFTase) gene of Xanthmonas oryzae MGL21. Purification of the mutant protein from E. coli and reation condition for the production of inulo-oligosaccharide(ISO) were studied. The molecular mass of the CFTase deletion mutant protein was estimated to be 90kDa by SDS- Polyacrylamide gel electrophoresis. Optimum reaction pH and temperature were pH6.5 and $40^{\circ}C$, respectively. Under optimal reaction conditions, endo-inulinase activating enzyme was rapidly produced ISO from inulin. Components were DP(degree of polymerization) 3and 4 with trace amount of smaller oligosaccharides.

• Bulletin of the Korean Chemical Society
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• v.32 no.5
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• pp.1640-1644
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• 2011

Water-soluble mutant of intrinsically insoluble protein, crambin, was produced by mutagenesis based on the sequence analysis with homologous proteins. Thr1, Phe13, and Lys33 of crambin were substituted for Lys, Tyr, and Lys, respectively. The resultant mutant was soluble in aqueous buffer as well as in dodecylphosphocholine (DPC) micelle solution. The $^1H-^{15}N$ spectrum of the mutant crambin showed spectral similarity to that of the wild-type protein except for local regions proximal to the sites of mutation. Solution structure of water-soluble mutant crambin was determined in aqueous buffer by NMR spectroscopy. The structure was almost identical to the wild-type structure determined in non-aqueous solvent. Subtle difference in structure was very local and related to the change of the intra- and inter-protein hydrophobic interaction of crambin. The structural details for the enhanced solubility of crambin in aqueous solvent by the mutation were provided and discussed.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 2000.04a
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• pp.78-89
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• 2000

Protein secretion in filamentous fungi has been shown to be restricted to actively growing hyphal tips. To determine whether an increase in the amount of growing surface area of a fungus can lead to an increase in the amount of protein secretion, we examined secretion in a temperature-sensitive Neurospora crassa mcb mutant that shows a loss of growth polarity when incubated at restrictive-temperature. Incubation of the mcb mutant at restrictive-temperature results in a three- to five-fold increase in the level of extracellular protein and a 20- fold increase in carboxymethyl cellulase activity relative to a wild-type strain. A mutation in the cr-l gene has been shown previously to suppress the apolar growth phenotype of the mcb mutant, and we find that the level of extracellular protein produced by a mcb; cr-l double mutant was reduced to that of the wild-type control. Immunolocalization of a secreted endoglucanase revealed that proteins are secreted mainly at hyphal tips in hyphae exhibiting polar growth and over the entire surface area of bulbous regions of hyphae that are produced following a shift of the mcb mutant to restrictive-temperature. These results support the hypothesis that secretion of extracellular protein by a filamentous fungus can be significantly increased by mutations that alter growth polarity.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.39 no.3
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• pp.278-284
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• 1994

The sulfur amino acid composition in soybean (Glycine max L.) seeds may be an essential characteristic of new cultivars for some animal diets. Variation in seed storage protein among genotypes might make it possible to improve the quality of seed protein by genetically altering seed storage protein composition through plant breeding. This study was carried out to determine if mutant strains have potential for improving seed protein quality in soybean. Ten mutant strains had a distinct characteristic of seed storage protein subunits. Among the mutant strains, the sulfur amino acid compositions(methionine plus cystein) of Keburi(P.I.417016), Keburi(P.I.506817), and P.I.54608-1 were relatively higher than those of the others and were 1.9, 2.1, and 1.8%, repectively, which might be due to low levels of ${\alpha}$, ${\alpha}$', and ${\beta}$ subunits of 7S protein. Therefore, it is concluded that the mutant strains, Keburi(P.I.417016), Keburi(P.I.506817), and P.I.54608-1 appear to be potential materials for a breeding program for improving sulfur amino acid composition, and the others also seem to be possible breeding materials for other uses.

• Biotechnology and Bioprocess Engineering:BBE
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• v.3 no.2
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• pp.67-70
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• 1998

In order to understand the influence of ferroxidase center on the protein assembly and solubility of tadpole ferrin, three mutant plasmids, pTH58K, pTH61G, and pTHKG were constructed with the aid of site-directed mutagenesis and mutant proteins were produced in Eshcerichia coli. Mutant ferritin H-subunits produced by the cells carrying plasmids pTH58K and pTHKG were active soluble proteins, whereas the mutant obtained from the plasmid pTH61G was soluble only under osmotic stress in the presence obtained from the plasmid pTH61G was soluble only under osmotic stress in the presence of sorbitol and betaine. Especially, the cells carrying pTH61G together with the plasmid pGroESL harboring the molecular chaperone genes produced soluble ferritin. The mutant ferritin H-subunits were all assembled into ferritin-like holoproteins. These mutant ferritns were capable of forming stable iron cores, which means the mutants are able to accumulate iron with such modified ferroxidase sites. Further functional analysis was also made on the individual amino acid residues of ferroxidase center.