• Proceedings of the Korean Society of Near Infrared Spectroscopy Conference
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• 2001.06a
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• pp.1286-1286
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• 2001

Despite extensive theoretical and experimental studies the structure of the protein-solvent interface is subject of many controversy. Understanding the processes that occur in aqueous solution requires understanding of the solvent influence on the structure of protein. The aim of this study is to investigate the applicability of NIR methods in the study of hydration phenomena in protein solutions. Temperature-induced changes in NIR spectra of -lactoglobulin (BLG) in aqueous solutions have been investigated by means of two-dimensional correlation spectroscopy (2DCOS) and principal component analysis (PCA). With the temperature increase the balance of forces between the BLG's interaction with itself and the BLGs interaction with its environment is disrupted leading to BLG unfolding. Significant differences of 2D signals and distinct discrepancies of loading on PC1 and PC2 were observed as a result of temperature increase. In the native folded conformation of BLC, most of the nonpolar amino acids are hidden in the centre of the structure, out of contact with water molecules, while charged groups are outside, in the contact with water. The polar groups promote low density Ih-type structure in the water outside this first hydration shell. When BLG unfolds it assumes a more extended configuration on which the previously buried nonpolar groups are exposed to water and promote the higher density II-type structure outside its first shell. Detailed assignments of bands attributed to the bulk water, different states of the hydrated water and the changed conformation of BLG are proposed.

• Journal of Pharmaceutical Investigation
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• v.32 no.3
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• pp.199-207
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• 2002

In order to develop a sustained release formulation of bovine somatotropin (BST), which has been used to increase the body weight of oxen or the milk production of dairy cows, poly(D,L-lactide-co-glyceride)(PLGA) microspheres were made by W/O/W multiple emulsification method and solvent extraction method. Physical properties including particle size, drug entrapment, drug release, protein denaturation, and in vivo body weight increase in rats were characterized. The size of the microspheres was increased as the molecular weight of PLGA increased. When Span 65 and stearic acid during preparation were added, the size was decreased but the amount of surface protein was increased, resulting in a high loading efficiency, with fast release of BST from the microspheres. Aggregation or fragmentation of BST by SDS-PAGE during microsphere preparation and drug release study was not observed. Body weight of Sprague-Dawley's male rats was significantly increased after subcutaneous administrations of BST-loaded PLGA microspheres. There was a good correlation between in vivo weight gain and in vitro release rate of microspheres. PLGA microspheres with a high surface protein ratio could be a good candidate for the sustained delivery of BST.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.26 no.1
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• pp.21-25
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• 1993

In order to obtain the fundamental factors influencing on gelation of Alaska pollack meat paste during processing, thermograms of protein using differential scanning calorimetry (DSC) were investigated. The thermal transition temperatures of Alaska pollack meat paste due to protein denaturation were $38^{\circ}C,\;49^{\circ}C,\;55^{\circ}C\;and\;77^{\circ}C$, but those temperatures were changed to $35^{\circ}C,\;45^{\circ}C,\;50^{\circ}C\;and\;73^{\circ}C$ after adding salt($3\%$ NaCl). The starch did not affect the thermal transition of fish protein and its thermal properties were changed independently in starch-meat paste mixture system.

• Asian-Australasian Journal of Animal Sciences
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• v.19 no.6
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• pp.898-904
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• 2006

Effects of sodium bicarbonate (SBC) injection on meat quality and functionality of porcine M. longissimus lumborum were investigated. Fifteen pigs ($100{\pm}5kg$) were randomly selected at a commercial slaughter plant. After slaughtering the loins were dissected from the carcass before chilling at approximately 30 minutes post mortem. The loins were divided into four cuts for sample treatment, and SBC of 0.25 M, 0.40 M and 0.75 M was injected (2% w/w) using a syringe. As SBC injection level was increased, muscle pH increased significantly (p<0.05). SBC injection decreased lightness ($L^*$) values on the surface of muscle. Moreover, with injection of SBC, drip loss %, cooking loss % and shear force were significantly (p<0.05) decreased, whereas WHC and $Na^+$ content were significantly (p<0.05) increased. From panel testing of uncooked pork loin, no significant differences (p>0.05) were found in aroma, off-flavor and drip between injection of SBC at different levels and the control, although color and acceptability were significantly lower (p<0.05) in control pork loin compare with injection of SBC at 0.75 M. In cooked pork loin from the panel test, aroma, flavour, off-flavour and juiciness were found to be similar (p>0.05) on all treatments, but tenderness and acceptability were significantly higher (p<0.05) with injection of SBC at 0.75 M than for control loin. Myofibrillar protein solubility of muscles treated with SBC was significantly (p<0.05) higher than that of the control, although no significant differences (p>0.05) were found in sarcoplasmic protein solubility between the treatments. These results indicated that SBC injection into pre-rigor porcine M. longissimus lumborum could improve ultimate pork quality characteristics such as meat color, water-holding capacity, and could inhibit muscle protein denaturation due to an increase in muscle pH.

• Korean Journal of Food Science and Technology
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• v.20 no.3
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• pp.447-452
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• 1988

In order to study effect of freezing rates on the quality changes such as pH, TBA value, free fatty acids and protein extractability, cylindrical chopped beef logs with 10cm of diameter and 10cm of height were frozen at three freezing rates(0.97cm/hr, 2.05cm/hr, 3.71cm/hr)using air blast freezer. Physicochemical changes of frozen meat were investigated during forzen storage at $-20^{\circ}C$ for 16weeks. Results on pH change showed $0.1{\sim}0.2unit$ increase at the 16th week of the frozen storage and the change was smaller with the increasing freezing rates. Free fatty acids content and TBA value also were increased during forzen storage, but they were minimal at 3.71cm/hr freezing rate. Correlation coefficient between TBA value and free fatty acids content were highly significant(r=0.804). After 16weeks of storage, extractibilities of salt soluble protein were decreased by 17.7%, 6.1% and 1.6% at freezing rates of 0.97, 2.05 and 3.71cm/hr, respectively. On the other hand, extractabilities of water soluble protein were decreased by 26.0%, 21.2% and 18.5%, respectively. The effect of freezing rates on the protein extractability appeared to be greater in salt soluble protein than in water soluble protein, but freezing denaturation was more rapid in water soluble protein.

• Journal of the Korean Chemical Society
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• v.55 no.5
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• pp.746-750
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• 2011

Fluorescence correlation spectroscopy (FCS) is an emerging fluorescence technique used to study the dynamics of proteins on a millisecond to microsecond time scale at the single-molecule level. Solution pH-modulated protein conformational changes can be manifested by binding rate, fluorescence lifetime, and binding specificity of a probe molecule. The fluorescence lifetime of Nile red (NR) bound to apomyoglobin (apoMb) was measured to be $6{\pm}0.3$ ns, much longer than that in water solution ($2.9{\pm}0.2$ ns). As the unfolding population of apoMb increased by lowering pH of solution, the fraction for the longer lifetime of NR decreased with an increasing fraction for the shorter lifetime of NR in water. Unlike 1-anilino-8-naphthalene sulfonic acid, which has many lifetimes due to nonspecific binding to the unfolded apoMb, NR bound to apoMb possesses only a single lifetime. These results suggest that NR binds specifically to native apoMb and thus can be utilized to probe the folding/unfolding dynamics of apoMb using FCS.

• Journal of the Korean Society of Food Science and Nutrition
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• v.23 no.6
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• pp.1027-1031
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• 1994

A method for the process of making fig conserves to prevent the denaturation of ficin (EC3.422.3) that is a proteolytic enzyme in fig (Fixus carica L. ) has been developed. The suutable composition ratio of materials such as, fig, sugar, citric acid and potassium sorbate, to make fig conserves was 1,000, 600 , 1.0 and 0.67g , respectively. to maintain the ficin activity, it was necessary that these materials were heated on 55$^{\circ}C$ and concentrated in the reduced pressure. At a result of sensory evaluation , meat treated with fig was the softest among samples. Then the treated beef with 55$^{\circ}C$ converse, 7$0^{\circ}C$ conserves, sugar and control have been shown the decreased rate respectively. There was significantly different in the effect of tenderness between each group(0.1%) . The nitrogen content of connective tissue was relatively low in the groups of the treated beef with fig and 55$^{\circ}C$ converses, 7$0^{\circ}C$ converses sugar and control , which was similar to the order of the ficin activity. This research revealed that the constituent protein of meat muscle was decomposed by ficin and its solubility was relatively higher than before.

• BMB Reports
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• v.42 no.12
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• pp.812-816
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• 2009

To screen chaperone proteins from Schizosaccharomyce pombe (S. pombe), we prepared recombinant citrate synthase of the fission yeast as a substrate of anti-aggregation assay. Purified recombinant citrate synthase showed citrate synthase activity and was suitable for the substrate of chaperone assay. Several heat stable proteins including aspartyl aminopeptidase (AAP) for candidates of chaperone were screened from the supernatant fraction of heat-treated crude extract of S. pombe. The purified AAP migrated as a single band of 47 kDa on SDS-polyacrylamide gel electrophoresis. The native size of AAP was estimated as 200 kDa by a HPLC gel permeation chromatography. This enzyme can remove the aspartyl residue at N-terminus of angiotensin I. In addition, AAP showed the heat stability and protected the aggregation of citrate synthase caused by thermal denaturation. This study showed that S. pombe AAP is a moonlight protein that has aspartyl aminopeptidase and chaperone activities.

• Journal of Microbiology and Biotechnology
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• v.30 no.7
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• pp.1082-1091
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• 2020

Microbial transglutaminases (MTGs) are widely used in the food industry. In this study, the MTG gene of Streptomyces sp. TYQ1024 was cloned and expressed in a food-grade bacterial strain, Bacillus subtilis SCK6. Extracellular activity of the MTG after codon and signal peptide (SP Ync M) optimization was 20 times that of the pre-optimized enzyme. After purification, the molecular weight of the MTG was 38 kDa and the specific activity was 63.75 U/mg. The optimal temperature and pH for the recombinant MTG activity were 50℃ and 8.0, respectively. MTG activity increased 1.42-fold in the presence of β-ME and 1.6-fold in the presence of DTT. Moreover, 18% sodium chloride still resulted in 83% enzyme activity, which showed good salt tolerance. Cross-linking gelatin with the MTG increased the strength of gelatin 1.67 times and increased the thermal denaturation temperature from 61.8 to 75.8℃. The MTG also significantly increased the strength and thermal stability of gelatin. These characteristics demonstrated the huge commercial potential of MTG, such as for applications in salted protein foods.

• 한국생물공학회:학술대회논문집
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• 2000.11a
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• pp.721-724
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• 2000

The possibility of the enzymatic in vitro glycosylation using peptide-N-glycosidase F was examined. Oligosaccharide chains in the glycoproteins are important for the biological activity, solubility, immunogenecity, recognition, and prevention of degradation. After 4 h incubation of deglycosylated glycoprotein with excess glucose oligomer and ammonia in acetone at $50^{\circ}C$, upper shift of protein band was observed on SDS-PAGE. And the different deglycosylation characteristics of glucose oxidase and fetuin were investigated.