• Journal of Korean Society on Water Environment
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• v.35 no.4
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• pp.299-307
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• 2019

The purpose of this study was to investigate the effect of low temperature thermal pre-treatment on biodegradation of waste activated sludge for anaerobic digestion as a countermeasure for increasing sludge generation. The experimental condition was accomplished in 2 %, 4 %, and 6 % TS concentration, and $70^{\circ}C$, $80^{\circ}C$, $90^{\circ}C$ of temperature for a maximum of 120 minutes retention time. Then, it was followed by analysis of physical/chemical properties, BMP test and composition of biogas. The biogas characteristic was evaluated by applying the modified Gomperz model. As a result, solubility of dissolved substrate, such as $SCOD_{Cr}$, soluble carbohydrate, and soluble protein, and biogas production increased as temperature increased. Solubilization efficiency at $90^{\circ}C$ was 18.4 %, 17.03 % and 16.88% in 2 %, 4 %, and 6 % TS concentration respectively. Also, solubilization rates of carbohydrate and protein similarly increased. BMP test results also showed that methane production in excess sludge increased to 0.194, 0.187 and $0.182m^3/kg$ VS. respectively, and lag phase decreased to 0.145, 0.220, 0.351 day due to acceleration of the hydrolysis step. Consequently, low-temperature thermal pre-treatment could increase biodegradability of sludge, positively affecting biogas production and sludge reduction.

• Food Science of Animal Resources
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• v.41 no.4
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• pp.687-700
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• 2021

This study performed to evaluate the applicability of functional dairy food materials by comparing the calcium solubilization ability and anti-inflammatory effects of hydrolyzed casein protein. Commercial enzyme (Alcalase^®; Neutrase^®; Protamex^®; Flavourzyme^®) was added to the 10% casein solution to prepare the casein hydrolysates. Samples obtained every hour [1:200 (w/v)]. According to results of measuring the degree of hydrolysis (DH), all of four enzymatic hydrolysates increased rapidly from 30 to 40 min, and after 150 min, there were no change. Protamex^® and Neutrase^® had the highest DH compared to others enzymatic hydrolysates. After that, peptides obtained throughout a preparative liquid chromatography system. In the calcium solubility experiments, neutrase fraction (NF) 4 and NF7 showed similar activities with casein phosphopeptide (CPP). In vitro cell experiments showed that no cytotoxicity except for NF6. Also, the production of nitric oxide (NO) inhibited as the concentration of fraction samples increased. The cytokine (IL-1α, IL-6, and TNF-α) production was lower than lipopolysaccharide (+) group significantly. Therefore, the possibility of anti-inflammatory activity found in the hydrolyzed samples. According to the above experiments, NF3 and Protamex Fraction (PF) 3 selected. Amino acids selected throughout an AccQ-Tag system. As a result, 17 species of amino acids and several species of unknown amino acids identified. Both fractions had the highest content of phenylalanine. This study identified the potential of biologically active and functional peptides derived from casein that affect the food and dairy industry.

• The Korean Journal of Food And Nutrition
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• v.2 no.2
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• pp.21-26
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• 1989

The morphological changes of fresh beef treated with ficin(0.1% : 2 hrs, 6 hrs)were examined with transmission electron microscope(TEM), the results obtained were as follows ; Connective tissue protein in fresh beef treated with ficin became gradually fragmentation and was occurred solubilization with time The length of sarcomere in myofibrillar protein was elongated, M-line became dim, and the 1-band of Z-line was broken and beck me fragmentation with time.

• The Korean Journal of Food And Nutrition
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• v.1 no.2
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• pp.1-8
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• 1988

The morphological changes of fresh beef treated with ficin(0.1% : 35$^{\circ}C$ 2hrs, 6hr,) were examined with scanning electron microscope(SEM), the results obtained were as follows ; Connective tissue protein in fresh beef treated with ficin was occurred solubilization with time and gradually trasformed from a definite form into amorphous form, followed by showing an opening-up phenomenon again and subdivision. Myofibrillar protein was cracked and breaked slightly, followed subdivision with time.

• The Korean Journal of Food And Nutrition
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• v.1 no.2
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• pp.9-17
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• 1988

The morphological changes of fresh beef treated with ficin(0.1% : 2hrs, 6hrs) were examined with optical microscope (OM, LM), the results obtained were as follows : Connective tissue protein in fresh beef treated with ficin was occurred swelling and separation of endomysial reticulum with time, followed showing granulation and solubilization slightly. Myofibrillar protein was loosed wavy contractile muscle fiber, and showed erosin, cracks and breaks in fibers with time.

• Biomedical Science Letters
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• v.18 no.2
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• pp.96-103
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• 2012

Kv 4.2 ion channel protein has an ability to open at subthreshold membrane potentials and to recover quickly from inactivation. That is very important for neuronal signal transmission in vertebrate brain. In order to purify Kv 4.2 protein, the novel purification methods were experimented. The purification procedure utilized chromatography on DE-52 ion exchange column and affinity chromatography on a WGA-Sepharose 4B, and Kv 4.2 affinity column chromatography. It was found that 0.5% (wt./vol.) Triton X-100 detergent in lysis buffer worked well for Kv 4.2 protein solubilization from rat brain membrane. Protein quantitative determination was conducted by BCA method at 562 nm for each purification step to avoid determination interference of protein at 280 nm by detergent. The confirmation of Kv 4.2 existence and amount is performed using by SDS-PAGE/immunoblotting or 96-well dot blotting. The Kv 4.2 without interacting protein that contains carbohydrate, was purified from novel biochemical 3-steps purification method for further research.

• Korean Journal of Food Science and Technology
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• v.21 no.4
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• pp.542-548
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• 1989

For the selective separation of proteins, the solubilization and desolubilization of proteins in sodium-di-2-ethylhexyl sulfosuccinate (AOT)-isooctane reverse micellar system were investigated. Protein solubilization increased with increasing the concentration of AOT to 200 mM and then decreased above that concentration. Protein was solubilized into reverse micelles in the pH range below the isoelectric Point of each protein, pH 4-10 for lysozyme and pH 5-6 for trypsin and ${\alpha}-chymotrypsin$, Lysozyme, trypsin and ${\alpha}-chymotrypsin$ were efficiently extracted in the precence of KCl and NaCl while larger molecular weight proteins such as pepsin and BSA had high solubilization with $CaCl_2$. At higher ionic strength all proteins exhibited murk less tendency to solubilize and the increase of ionic strength resulted in the decrease of micelle size. Lysozyme was successfully back transfered at pH 12.2 and 1.0M KCl; trypsin at pH 12.6 and 0.5M KCl; and ${\alpha}-chymotrypsin$ at pH 6.7 and 0.5M KCl. In a test group separation experiments, complete separation of lysozyme from BSA could be obtained.

• Korean Journal of Food Science and Technology
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• v.26 no.5
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• pp.484-489
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• 1994

Solubilization of plant ceil wall(tofu-residue) using enzyme complex obtained by Aspergillus niger CF-34 was attempted. The hydrolysis reaction was done at pH 4.0, $50^{\circ}C$, which were optimum pH and temperature of the enzyme, respectively. At the enzyme dosage of 2.5% (in terms of solid content of tofu-residue) and reaction time of 3 hr, the solubilizing percent of protein and carbohydrate were 62% and 50% respectively. Homogenization prior to enzyme reaction did not have much effect on tofu-residue solubilization. To improve solubility of tofu-residue, additional treatment such as alkali with 0.1% NaOH solution was found to be useful. The results showed that tofu-residue, which mainly consists of cell wall component of cellulose and hemicellulose, was not accessible to enzyme reaction and some prior treatment is required to enhance enzyme hydrolysis.

• 한국생물공학회:학술대회논문집
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• 2000.04a
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• pp.157-160
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• 2000

Solubilization of bovine serum albumin(BSA) is performed using a reverse micellar system consisting of sodium bis(2-ethylhexyl) sulfosuccinate(AOT). Of particular, effects of pH, salt concentration and its type on the solubilization are investigated by means of the phase-transfer method. One of significant findings in our study is that the protein is to a large extent aggregated in the interface between organic and aqueous phases at lower pH and small salt concentration. In this presentation, the optimal extraction process conditions for BSA, which is bulky, are proposed.

• Archives of Pharmacal Research
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• v.14 no.3
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• pp.231-236
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• 1991

The high affinity binding sites for angiotensin II were solubilized from rat liver membranes by treatment with CHAPS. The binding protein was also partially purified by angiotensin III inhibitor-coupled Affi-gel affinity chromatography. Binding to the intact membrances as well as to the solubilized preparation was specific and saturable. According to the Scatchard plot, the membrane preparations exhibited a single class of high affinity binding sites with a Kd OF 0.71 nM. The solubilized preparation also showed the presence of a single class of bindings sites with less affinity (Kd of 14 nM). Meanwhile the competition studies using angiotensin II analogues represented two separate binding sites for angiotensin II and single binding site for antagonist. These latter findings were correlated to the results provided by Garrison's research group. More works are needed to clarify this discrepancy.