• Journal of Pharmaceutical Investigation
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• v.20 no.4
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• pp.209-215
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• 1990

The activities of s-amylase, ${\alpha}-amylase$ and protease of three combination products containing digestive enzymes, antacids and herbal drugs on the Korean market were estimated. The effects of antacids and herbal drugs on the activities of digestive enzymes were investigated. Starch-saccarifying activity of s-amylase, starch-dextrinizing activity of ${\alpha}-amylase$ and protein-peptic activity of protease were estimated by Somogy, Mc'Credy, and Casein-Folin method, respectivley. The optimal pH of s-amylase, ${\alpha}-amylase$ and protease were pH 5.0, 4.8 and 7.0, rcspectively. The digestive activities at optimal pH continued about eight hours. The digestive activities of individual enzymes were reduced to 40-90% by antacids and were affected somewhat positively or negatively by herbal drugs. Enzyme activities of the combination products were also affected by pH and reaction time.

• Journal of Life Science
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• v.10 no.3
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• pp.279-285
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• 2000

CRP (cyclic AMP receptor protein) regulate transcription of catabolite-sensitive genes in Escherichia coli. Wild-type and mutant CRP (S83G and S128A) proteins were used to measure the thermal stability and the temperature-dependent structural change by proteolytic digestion, UV spectrophotometer and CD spectrapolarimeter. The result indicated that wild-type CRP was more thermally stable than the mutant CRPs in the presence of cAMP. At a low temperature, wild-type CRP with cAMP was more sensitive to subtilisin than the mutant CRPs. At a high temperature, there was no difference of sensitivity to subtilisin among wild-type, S83G and S128A CRPs. CD spectra suggested that the secondary structure of CRP was destroyed partially at a high temperature.

• Microbiology and Biotechnology Letters
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• v.26 no.5
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• pp.450-455
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• 1998

Aspergillus oryzae M-2-3 strain (argB$\^$-/) was transformed with pTAalp plasmid which was constructed for expression of the alkaline pretense gene, alpA, and 16 transformants were selected on arginine minus medium. When these transformants were tested for productivity of alkaline proteases using agar plate containing skim milk, the halo was observed around each colony of transformants, but not observed around the host strain in this condition. Southern analysis showed that the pTAalp plasmid having alpA gene was integrated into the chromosome of the host strain. The highest level of alkaline protease production was obtained in the culture filtrate of the transformant No. 14, which was estimated to 80-90% of total secreted proteins, and the enzyme activity was 64-450 times higher than those of host strain and industrial strain. Total nitrogen content and the digestion rate in soybean Koji extracts were also increased to 1.5 times in Aspergillus oryzae transformant No. 14.

• Journal of Life Science
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• v.14 no.2
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• pp.309-314
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• 2004

Cyclic AMP receptor protein (CRP) is involved in the transcriptional regulation of more than 100 genes in E. coli. CRP dimer is converted into active form via the sequential conformation change of cAMP binding pocket, hinge region and HTH DNA binding motif by binding of cAMP. The temperature gradient gel electrophoresis (TGGE) was applied to CRP protein to know whether it was an efficient technique to study the conformational transitions and the thermal stability. TGGE showed the unfolding process of wild-type and S83G CRP proteins with the temperature gradient set from 29 to 71$^{\circ}C$ on nondenaturing polyacrylamide gel. Melting temperature (Tm) was 57$\pm$1 and 55$\pm$1$^{\circ}C$ for wild-type and S83G CRP, respectively in acidic buffer[89.8 mM Glycine and 24 mM Boric acid (pH 5.8)].

• Korean Journal of Microbiology
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• v.30 no.2
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• pp.71-77
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• 1992

A 50 KD metalloprotease of Serratia marcesrens ATCC 21074 was purified by ammoniumsulfate precipitation. DEAE-cellulose ion exchange chromatography, and sephadex ti-100gel filtration. Optimal pH and temperature of enzyme were pH 8.0 and 37"C, respectively.This enzyme was stable in the ranges of 10-37$^{\circ}$C and pH 5.0--11.0. Thermal denaturationwas investigated by differential scanning calorimetry. Onset temperature of denaturationand endothermic peak temperature were 376$^{\circ}$C and 43.2"C. re:,pectively. The denaturationenthalpy was -8.4mJimg. The purified metalloprotease was ri.sistant to autodigestion for24 hr at 30$^{\circ}$C. Metalloprotease in culture supernatant was also resistant to autodigestionin this conditions. Heat-denatured enzyme. however. was rapidly digested by the nativeenzyme. The metalloprotease was stable to proteolytic digestion by mammalian proteasessuch as trypsin. a-chymotrypsin, and elastase. But the enzyme was easily digested bybacterial protease. thermolysin.bacterial protease. thermolysin.

• Korean Journal of Food Science and Technology
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• v.18 no.3
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• pp.197-203
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• 1986

An enzymatic flour milling process for barley into three major fractions (barley flour, bran-crease-germ and water solubles) was studied. Carbohydrate and protein of barley endosperm could be efficiently solubilized by the digestion process of partially pearled barley with enzymes. Bran, crease and germ were removed from hydrolyzate by filtering through 30-40mesh sieves. And then filtered product was separated into fractions by sedimentation or centrifugation. The most effective digestion of the barley was obtained by the enzyme with higher activities of glucanase and protease under such conditions as barley-water ratio, 1:1.5(W/V) and temperature at $45^{\circ}C$. Total flour yield recovered was approximately 73-76% of the barley, and the portions recovered as bran-crease-germ and water solubles were about 3.6 and 15.8%, respectively.

• Asian-Australasian Journal of Animal Sciences
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• v.29 no.7
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• pp.998-1003
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• 2016

Although exogenous protease enzymes have been used in poultry diets quite extensively, this has not been the case for pig diets. In general, due to their better gut fermentative capacity and longer transit time, pigs have greater capacity to digest dietary proteins than poultry. However, in early-weaned piglets, the stress brought about by weaning adversely affects the digestion of dietary proteins. Therefore, a study was conducted to determine the effects of a commercial protease enzyme in weanling pigs. Indices of growth, nutrient digestibility, blood profiles, fecal microflora, fecal gas emission and fecal scores were measured during the study. A total of 50 weanling pigs ($6.42{\pm}0.12kg$) at 28 d of age were randomly assigned to receive 1 of 2 dietary treatments: i) control diet (corn-soy based) with no supplemental protease (CON), and ii) control diet+200 g/ton protease (PROT) for 42 d. A completely randomized design consisting of 2 treatments, 5 replicates, and 5 pigs in each replicate was used. Growth performance in terms of body weight ($27.04{\pm}0.38kg$ vs $25.75{\pm}0.39kg$; p<0.05) and average daily gain ($491{\pm}7.40g$ vs $460{\pm}7.46g$; p<0.05) in PROT fed pigs were increased significantly, but gain per feed ($0.700{\pm}0.01$ vs $0.678{\pm}0.01$; p>0.05) was similar between treatments at d 42. Relative to CON pigs, PROT fed pigs had increased (p<0.05) apparent total tract digestibility ($84.66%{\pm}0.65%$ vs $81.21%{\pm}1.13%$ dry matter and $84.02%{\pm}0.52%$ vs $80.47%{\pm}1.22%$ nitrogen) and decreased (p<0.05) $NH_3$ emission ($2.0{\pm}0.16ppm$ vs $1.2{\pm}0.12ppm$) in the feces at d 42. Except for a decreased (p<0.05) in blood creatinine level, no differences were observed in red blood cell, white blood cell, lymphocyte, urea nitrogen, and IgG concentrations between treatments. Fecal score and fecal microflora (Lactobacillus and E. coli) were also similar between CON and PROT groups. Overall, the supplementation of protease enzyme in weanling pigs resulted in improved growth rate and nutrient digestibility. Exogenous protease enzyme reduced fecal $NH_3$ emission, thus, potentially serving as a tool in lowering noxious gas contribution of livestock production in the environment.

• Bulletin of the Korean Chemical Society
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• v.33 no.9
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• pp.2883-2889
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• 2012

LL-37 is the only antimicrobial peptide (AMP) of the human cathelicidin family. In addition to potent antimicrobial activity, LL-37 is known to have the potential to inhibit lipolysaccharide (LPS)-induced endotoxic effects. To provide the stability to proteolytic digestion and increase prokaryotic selectivity and/or anti-endotoxic activity of two Lys/Trp-substituted 19-meric antimicrobial peptides (a4-W1 and a4-W2) designed from IG-19 (residues 13-31 of LL-37), we synthesized the diastereomeric peptides (a4-W1-D and a4-W2-D) with D-amino acid substitution at positions 3, 7, 10, 13 and 17 of a4-W1 and a4-W2, respectively and the enantiomeric peptides (a4-W1-E and a4-W2-E) composed D-amino acids. The diastereomeric peptides exhibited the best prokaryotic selectivity and effective protease stability, but no or less anti-endotoxic activity. In contrast, the enantiomeric peptides had not only prokaryotic selectivity and anti-endotoxic activity but also protease stability. Our results suggest that the hydrophobicity and ${\alpha}$-helicity of the peptide is important for anti-endotoxic activity. In particular, the enantiomeric peptides showed potent anti-endotoxic and LPS-neutralizing activities comparable to that of LL-37. Taken together, both a4-W1-E and a4-W2-E holds promise as a template for the development of peptide antibiotics for the treatment of endotoxic shock and sepsis.

• Food Science and Preservation
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• v.23 no.3
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• pp.355-360
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• 2016

In this study, the quality characteristics of spray dried powders from unripe fig extract were investigated. The protease activities of unripe fig and peeled unripe fig extract were 0.11 unit/mL and 0.28 unit/mL, respectively. The spray dried powder of unripe fig extracts was analzed using different maltodextrin ratios (F-MD 5, 5% maltodextrin; F-MD 10, 10% maltodextrin; and F-MD 20, 20% maltodextrin). The spray-dried powder showed the highest protease activity with F-MD 10 (0.84 unit/g). The moisture content and L value of the spray-dried powder were higher than those of the freeze-dried powder. The particle diameter of the freeze-dried powder ($209.67{\mu}m$) was higher than that of the spray-dried powders ($22.18{\sim}37.33{\mu}m$). The water absorption index ranged from 0.18 to 0.40, while the water solubility index ranged from 94.40% to 98.80%. In the in vitro digestion study, spray-dried powders of the unripe fig showed a protease survival range of 16.47%~24.80%. In conclusion, it is considered appropriate to use the spray-dried powder (F-MD 10) of unripe fig as a meat tenderizer for processing food.

• Journal of Microbiology and Biotechnology
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• v.2 no.1
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• pp.14-20
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• 1992

Some microorganisms isolated from soil, including some bacteria and fungi, were found to secrete an extracellular soymilk-clotting enzyme. Among them, an isolated fungus showed the highest soymilk-clotting activity and the strain was assigned to genus Penicillium based on its cultural and morphological characteristics, and designated as Penicillium sp. L-151K. Soymilk-clotting enzymes A and B produced by Penicillium sp. L-151K were purified by ammonium sulfate precipitation and chromatographies on Sephadex G-25, CM-Sephadex, Sephadex G-100 and phenyl-Toyopearl gel. The two purified enzymes A and B were found to be homogeneous by polyacrylamide gel electrophoresis at pH 9.5. The molecular weights of enzyme A and B were 24, 000 and 40, 000, respectively, by gel filtration on Sephadex G-100. Enzymes A and B coagulated soymilk optimally at $60^\circ{C}$ and were stable up to $50^\circ{C}$. Both enzymes were most active at pH 5.8 for soymilk coagulation, and were stable with approximately 80% of original activity from pH 3.0 to 5.0. Each enzyme was an acidic protease with an optimum pH of 3.0 for casein digestion. The soymilk-clotting efficiency of these enzymes was improved with $CaCl_2\;or\;MgCl_2$ when making soymilk-curd.