• The Microorganisms and Industry
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• v.12 no.1
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• pp.9-14
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• 1986

We have adopted a genetic approach to identifying those residues and local sequences in a polypeptide chain which play an important role on the folding pathway. Our approach has been to isolate and characterize mutants which specifically alter the folding and subunit association pathway of a polypeptide chain, without altering the native protein. Such mutants distinguish residues involved in the kinetic control of conformation from residues involved in the stability and activity of the native protein. This approach is complementary to the efforts to characterize mutations which alter the stability of the mature protein(6,7,8). It is likely that many residues will have roles in both aspects of the functioning of the polypeptide chain. We thought it likely, however, that at least with large proteins, these aspects might be segregated in different local sequences.

• Korean journal of food and cookery science
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• v.9 no.1
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• pp.43-51
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• 1993

Buckwheat protein isolate was tested for the effects of pH, addition of sodium chloride and heat treatment on solubility, emulsion capacities, emulsion stability, surface hydrophobicity, foam capacities and foam stability. The solubility of buckwheat protein isolate was affected by pH and showed the lowest value at pH 4.5, the isoelectric point of buckwheat protein isolate. The solubility significantly as the pH value reached closer to either ends of the pH, i.e., pH 1.0 and 11.0. The effects of NaCl concentration on solubility were as follows; at pH 2.0, the solubility significantly decreased when NaCl was added; at pH 4.5, it increased above 0.6 M; at pH 7.0 it increased; and at pH 9.0 it decreased. The solubility increased above $80^{\circ}C$, at all pH ranges. The emulsion capacity was the lowest at pH 4.5. It significantly increased as the pH approached higher acidic or alkalic regions. At pH 2.0, when NaCl was added, the emulsion capacity decreased, but it increased at pH 4.5 and showed the maximum value at pH 7.0 and 9.0 with 0.6 M and 0.8 M NaCl concentrations. Upon heating, the emulsion capacity decreased at acidic pH's but was maximised at pH 7.0 and 9.0 on $60^{\circ}C$ heat treatment. The emulsion stability was the lowest at pH 4.5 but increased with heat treatment. At acidic pH, the emulsion stability increased with the increase in NaCl concentration but decreased at pH 7.0 and 9.0. Generally, at other pH ranges, the emulsion stability was decreased with increased heating temperature. The surface hydrophobicity showed the highest value at pH 2.0 and the lowest value at pH 11.0. As NaCl concentrationed, the surface hydrophobicity decreased at acidic pH. The NaCl concentration had no significant effects on surface hydrophobicity at pH 7.0, 9.0 except for the highest value observed at 0.8 M and 0.4 M. At all pH ranges, the surface hydrophobicity was increased, when the temperature increased. The foam capacity decreased, with increased in pH value. At acidic pH, the foam capacity was decreased with the increased in NaCl concentration. The highest value was observed upon adding 0.2 M or 0.4 M NaCl at pH 7.0 and 9.0. Heat treatments of $60^{\circ}C$ and $40^{\circ}C$ showed the highest foam capacity values at pH 2.0 and 4.5, respectively. At pH 7.0 and 9.0, the foam capacity decreased with the increased in temperature. The foam stability was not significantly related to different pH values. The addition of 0.4 M NaCl at pH 2.0, 7.0 and 9.0 showed the highest stability and the addition of 1.0 M at pH 4.5 showed the lowest. The higher the heating temperature, the lower the foam stability at pH 2.0 and 9.0. However, the foam stability increased at pH 4.5 and 7.0 before reaching $80^{\circ}C$.

• Applied Biological Chemistry
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• v.36 no.3
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• pp.172-177
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• 1993

To extract insoluble proteins from sesame meal residue by microorganism, the sesame meal residue was treated with crude enzyme solution of Bacillus sp. CW-1121. The foaming capacity of salt soluble protein was quite lower than that of water soluble protein and the foaming stability of salt soluble protein decreased abruptly in 10 min., while it sustained for 30 min in case of water soluble protein. Emulsion capacities of all the protein fractions showed minimum value near isoelectric point of protein and salt soluble protein had lower emulsion capacities than that of water soluble protein. The emulsion stability of the protein was relatively stable for 30 min at $80^{\circ}C$. Oil and water absorption capacities of salt soluble protein were higher than those of water soluble protein.

• Food Science of Animal Resources
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• v.23 no.1
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• pp.63-69
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• 2003

This experiment was carried out to study changes in solubility and emulsifying properties of whey protein. Whey protein hydrolysates were obtained from tryptic hydrolysis of whey protein concentrate at pH 8.0 and 37$^{\circ}C$ for 6 hours. Emulsifying activity of whey protein hydrolysate was highest at 4 hours of hydroysis and at 5.50% of DH. During hydrolysis of whey protein concentrate with trypsin, ${\alpha}$-lactalbumin was not easily broken down. But ${\beta}$-lactoglobulin was hydrolysed rapidly from the early stage of hydrolysis, producing several low molecular weight peptides, which have to participate in increasing emusifying activity. The solulbility of hydyolysates tended to increase depending on hydrolysis time; however, there was a gradual decrease after 5 hours. The hydrolysate had a minimum solubility near the isoelectric point range (pH 4∼5). The more hydrolysed the whey protein concentrates, the more soluble they are near the pl. They aye also more soluble above pH 6. Emulsifying activity of hydrolysates showed similar results to solubility. Creaming stability gradually increased when hydrolysis increased, increasing rapidly above pH 8 after 4 hours of hydrolysis.

• Journal of the Korean Society of Food Science and Nutrition
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• v.12 no.3
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• pp.251-258
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• 1983

This experiment was carried out to investigate the capability of production of artificial milk for leaf protein concentrate (LPC). Chloroplastic protein and cytoplasmic protein were extracted from leaves of Dystaenia takeshimana Nakai and LPC was extracted from leaves of Italian ryegrass to increase the functional properties of LPC as a level of milk casein. One gram of chloroplastic protein and cytoplasmic protein and 1g of LPC were succinylated by addition of succinic anhydride 0.1, 0.25, and 1g respectively. Their functional properties were investigated in this experiment. The results obtained were summarized as follows: 1. The non-succinylated LPC showed a higher value in bulk density than the chloroplastic protein, the cytoplasmic protein and LPC succinylated by addition of succinic anhydride 0.1, 0.25, and 1g respectively. Nevertheless, succinylation had an enhancing effect as indicated by the rises as the degrees of succinylation was increased. 2. Although solubility of non-succinylated LPC was lower than that of milk casein, succinylation caused an effective increase in the solubility of the protein and LPC. 3. Water absorption and fat absorption of succinylated LPC were twice to eight times higher than those of milk casein. Fat absorption was not influenced to the extent by succinylation as the water absorption. Excessive succinylation resulted in the decrease of both water absorption and fat absorption. 4. Emulsifying activity and emulsion stability were increased in proportion to the succinylated degree of LPC. More than 10% increase in the amount of succinic anhydride resulted in an apparent increase in emulsifying activity and emulsion stability. Besides, the succinylated LPC showed more excellent functional properties in emulsifying activity and emulsion stability than milk.

• Korean Journal of Food Science and Technology
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• v.37 no.3
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• pp.345-351
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• 2005

Physicochemical properties and functionalities of sodium caseinate, whey protein, skim milk, and whole milk with or without transglutaminase (TGase, 200 : 1) at $38^{\circ}C$ were determined. After crosslinking by TGase, whey protein was effective in improving heat stability compared to native protein at over $70^{\circ}C$. Whole milk was stable with lower turbidity compared to native solution. Whey protein showed low hydrolysis degree, fewer than sodium caseinate, during early activation time and increased slightly thereafter Emulsifying activities of sodium caseinate at pH 2 and 8, and whey protein at pH 7 and 8 improved. Emulsion stability of sodium caseinate improved at entire pH range studied. Foam expansion and foam stability of samples improved with TGase-treatment. Viscosities of TGase-treated samples were higher than those of untreated ones.

• Journal of the Korean Magnetic Resonance Society
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• v.26 no.4
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• pp.66-70
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• 2022

Protein structure determination using NMR spectroscopy requires a suite of heteronuclear 3-D NMR experiments that can take a couple of weeks for completion. During the experiments, protein samples may suffer from slow degradation due to co-purifying proteases, which complicates and slows down the assignment procedure. Here we describe a practical protocol to avoid unwanted proteolysis during the experiment.

• Asian-Australasian Journal of Animal Sciences
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• v.33 no.4
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• pp.556-567
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• 2020

Objective: To improve the utility of native grass resources as feed in China, we investigated the dynamics of protein and carbohydrate fractions among Inner Mongolian native grasses, during ensiling and the aerobic stage, using the Cornell Net Carbohydrate and Protein System. Methods: Silages were prepared without or with lactic acid bacteria (LAB) inoculant. We analyzed the protein and carbohydrate fractions and fermentation quality of silages at 0, 5, 15, 20, 30, and 60 d of ensiling, and the stability at 0.5, 2, 5, and 10 d during the aerobic stage. Results: Inner Mongolian native grass contained 10.8% crude protein (CP) and 3.6% water-soluble carbohydrates (WSC) on a dry matter basis. During ensiling, pH and CP and WSC content decreased (p<0.05), whereas lactic acid and ammonia nitrogen (N) content increased (p<0.05). Non-protein N (PA) content increased significantly, whereas rapidly degraded true protein (PB₁), intermediately degraded true protein (PB₂), total carbohydrate (CHO), sugars (CA), starch (CB₁), and degradable cell wall carbohydrate (CB₂) content decreased during ensiling (p<0.05). At 30 d of ensiling, control and LAB-treated silages were well preserved and had lower pH (<4.2) and ammonia-N content (<0.4 g/kg of fresh matter [FM]) and higher lactic acid content (>1.0% of FM). During the aerobic stage, CP, extract ether, WSC, lactic acid, acetic acid, PB₁, PB₂, true protein degraded slowly (PB₃), CHO, CA, CB₁, and CB₂ content decreased significantly in all silages, whereas pH, ammonia-N, PA, and bound true protein (PC) content increased significantly. Conclusion: Control and LAB-treated silages produced similar results in terms of fermentation quality, aerobic stability, and protein and carbohydrate fractions. Inner Mongolian native grass produced good silage, nutrients were preserved during ensiling and protein and carbohydrate losses largely occurred during the aerobic stage.

• Journal of the Korean Society of Food Science and Nutrition
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• v.18 no.4
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• pp.410-422
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• 1989

Soybean protein isolates were acylated with succinic anhydride and partially hydrolyzed with trypsin. Chemical modification decreased protein contents of samples and, in amino acid composition, tyrosine was increased comparatively. And lysine was increased remarkably by partial proteolysis. Succinylation and trypsin treatment increased the aqueous solubility and shifted the isoelectric potint that showed high pH-dependence of protein solubility. Protein solubility was influenced by salt concentration such as $NaCl,\;CaCl_2,\;NaNO_3$ and $NaH_2PO_4$. Chemical modification increased the absorption of oil and water, emulsification properties and foam capacity, but decreased foam stability, ultraviolet absorbance and bulk density. Protein-protein Interaction between soybean protein isolates and beef protein increased the emulsifying activity, emulsifying activity index and foaming properties, but it didn't have any influence on emulsion stability.

• Korean journal of food and cookery science
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• v.9 no.4
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• pp.308-311
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• 1993

This study was carried out in order to study the effect of mungbean protein on quality characteristics of angel parfait. The foaming properties of mungbean protein was tested and angel parfait was made with mungbean protein. The results were as follows: 1. Foam expansion values of mungbean protein were generally dependent on protein concentration to 3かio protein suspension. From 1％ to 3％ suspen-sion, foam expansion values increased. However, over 3％ suspension, the values decreased. 2. The foaming stability appeared the greatest value as protein concentration increased. But it was not signifi-cantly different over than 5% concentration. 3. The overrun of angel parfait made with munbean protein was significantly higher than that of made with soybean protein and sensory evaluation data presented that angel parfait made with mungbean protein was significantly higher than that of soybean protein.