• Microbiology and Biotechnology Letters
• /
• v.18 no.5
• /
• pp.517-524
• /
• 1990

The solubilization and desolubilization of proteins in CTAB/hexanol/isooctane reverse micellar system were investigated for the selective separation of proteins. Several proteins were used, including bovine serum albumin (BSA), pepsin, trysin and ribonuclease-a. Most proteins could be solubilized into reverse micelles in the pH range above the isoelectric point of each protein, where the net charge of protein was opposite to that of surfactant. However BSA was solubilized above pH 10, which is serveral pH units above the pI 4.9. The kinds of anions in aqueous phase influenced on protein solubilization while no significant trend was observed with different cations, Protein solubilization decreased with increase of the ion size in the order of F -, C1-, Br- and I -. The size of CTAB micelles did not change significantly with increasing ionic strength, but the solubilization decreased. Protein desolubilization showedropposite behaviors to the solubilization. Several model mixtures such as pepsin/ trypsin, pepsin/ribonuclease-a and BSAlribonucleaee-a were successfully separated from each other without changing enzymatic activities.

• 한국생물공학회:학술대회논문집
• /
• 2005.04a
• /
• pp.129-130
• /
• 2005

• Journal of the Korea Organic Resources Recycling Association
• /
• v.29 no.3
• /
• pp.35-40
• /
• 2021

In order to investigate the degree of solubilization of sewage sludge using sono-activated persulfate(UV/PP), VSS reduction rate, solubilization rate and extracellular polymeric substances were measured. Ultrasonic(US) and alkali·ultrasonic method using sodium hydroxide(US/SH) were compared. Under the persulfate·ultrasonic conditions, the VSS reduction rate and the solubilization rate increased to 27.6% and 58.9%, respectively. TB-EPS as Carbohydrate and Protein were extracted by 770 mg/L and 2,162 mg/L. Compared to the other methods, US and US/SH, the VSS reduction rate and solubilization rate were higher. And also, according to the TB-EPS values, cell wall destruction was more efficient.

• Journal of the Korea Organic Resources Recycling Association
• /
• v.27 no.4
• /
• pp.43-49
• /
• 2019

In order to investigate the relation between sewage sludge solubilization and extracellular polymeric substances(EPS) during alkaline-ultrasonic pretreatment, SCOD/TCOD ratio, solubilization rate, VSS/TS ratio, VSS reduction rate, LB-EPS(Loosely-Bound EPS) and TB-EPS(Tightly-Bound EPS) were measured. At the condition of TS 1.0% and pH 12, solubilization rate increased by 27.7%, LB-EPS as Carbohydrate and Protein increased by 14.6 and 13.3 mg/L/g TS, respectively. Withal, VSS decreased by 26.7% and TB-EPS as Carbohydrate and Protein were extracted by 15.7 and 21.9 mg/L/g TS, respectively. Consequently, the concentrations of organic matter and LB-EPS increased and the trends appeared similarly. In addition, the concentrations trend of decreasing solid matter and extracted TB-EPS also appeared similarly.

• Fisheries and Aquatic Sciences
• /
• v.19 no.3
• /
• pp.14.1-14.10
• /
• 2016

Isoelectric solubilization/precipitation (ISP) processing allows selective, pH-induced water solubility of proteins with concurrent separation of lipids and removal of materials not intended for human consumption such as bone, scales, skin, etc. Recovered proteins retain functional properties and nutritional value. Four roe protein isolates (RPIs) from yellowfin tuna roe were prepared under different solubilization and precipitation condition (pH 11/4.5, pH 11/5.5, pH 12/4.5 and pH 12/5.5). RPIs contained 2.3-5.0 % moisture, 79.1-87.8 % protein, 5.6-7. 4 % lipid and 3.0-3.8 % ash. Protein content of RPI-1 and RPI-2 precipitated at pH 4.5 and 5.5 after alkaline solubilization at pH 11, was higher than those of RPI-3 and RPI-4 after alkaline solubilization at pH 12 (P < 0.05). Lipid content (5.6-7.4 %) of RPIs was lower than that of freeze-dried concentrate (10.6 %). And leucine and lysine of RPIs were the most abundant amino acids (8.8-9.4 and 8.5-8.9 g/100 g protein, respectively). S, Na, P, K as minerals were the major elements in RPIs. SDS-PAGE of RPIs showed bands at 100, 45, 25 and 15 K. Moisture and protein contents of process water as a 2'nd byproduct were 98.9-99.0 and 1.3-1.8 %, respectively. Therefore, yellowfin tuna roe isolate could be a promising source of valuable nutrients for human food and animal feeds.

• Environmental Engineering Research
• /
• v.20 no.2
• /
• pp.163-169
• /
• 2015

In this study, we attempted to solubilize protein in slaughter blood (SB) using ultrasonic technology. The application of ultrasonic technology can make enzymatic degradation of SB more effective, which has no comparable alternative for treatment. The SB was homogenized by grinding it for 10 minutes at 10,000 rpm as a pretreatment for preventing its clotting, and then ultrasonic treatment was attempted to solubilize protein in SB. To maximize the efficiency of ultrasonic treatment for SB, the optimum condition of ultrasonic frequency (UF) was determined to be 20 kHz. To optimize the operation conditions of ultrasonification with 20 kHz of frequency, we used response surface methodology (RSM) based on ultrasonic density (UD) and ultrasonification time (UT). The solubilization rate (SR) of protein (%) was calculated to be $101.304-19.4205X_1+0.0398X_2+7.9411X_1{^2}+0.0001X_2{^2}+0.0455X_1X_2$. From the results of the RSM study, the optimum conditions of UD and UT were determined at 0.5 W/mL and 22 minutes, respectively, and SB treated under these conditions was estimated to have a 95% SR. Also, experimentally, a 95.53% SR was observed under same conditions, accurately reflecting the theoretical prediction of 95%.

• BMB Reports
• /
• v.28 no.2
• /
• pp.129-137
• /
• 1995

The ryanodine-receptor $Ca^{2+}$ release channel protein in the sarcoplasmic reticulum membrane of rabbit skeletal muscle plays an important role in muscle exitation-contraction (E-C) coupling. Various types of detergents were tested, including Chaps, cholate, octylglucoside, Zwittergents, Mega-9, Lubrol PX, and Triton X-100 for solubilization of this protein. Among these, Chaps and Triton X-100 were found to optionally solubilize the channel complex. Optimum conditions for this solubilization were pH 7.4 with a salt concentration of 1 M. The addition of phospholipid in the solubilization step helped in stabilizing the protein. The purification of the receptor was performed using sucrose density gradient centrifugation. Various methods [dilution, freeze-thaw, adsorption (Biobeads), and dialysis] were investigated to incorporate the Chaps-solubilized and purified $Ca^{2+}$ release channel protein into liposomes made from different types of phospholipids. Of these, a combined method consisting of a dialysis, freeze-thaw and sonication steps yielded the best results. Reconstituted vesicles produced by this method with 95% phosphatidylcholine (from soybean extract) had good function.

• KSBB Journal
• /
• v.5 no.3
• /
• pp.215-221
• /
• 1990

The solubilization of BSA, pepsin, trypsin and ribonuclease-a in cationic reverse micellar solutions has been investigated. For complete solubilization into reverse micellar solutions, pH values of several pH units above the isoelectric point of each protein were required. Solubilization was observed to decrease with increasing ionic strength of KCI. The size of empty micelles showed no significant change with increasing ionic strength. Trioctylmethyl ammonium chloride (TOMAC) in cyolohexane showed the lowest solubilization for the proteins. The system didodecyl dimethyl ammonium bromide (DDAB)-tetrachloroethylene was capable of solubilizing larger amounts of proteins than the system DDAB-benzene. Cetyl trimethyl ammonium bromide(CTAB)-hexanol-isooctane system showed lower solubilization than DDAB-tetrachloroethylene system, while it had higher Wo value.

• Korean Journal of Fisheries and Aquatic Sciences
• /
• v.51 no.4
• /
• pp.351-361
• /
• 2018

This study investigated the potential of collagenous protein fractions (CPFs) as functional foods. The specific CPFs studied were recovered from the roe of bastard halibut (BH), Paralichthys olivaceus; skipjack tuna (ST), Katsuwonus pelamis; and yellowfin tuna (YT), Thunnus albacares through the alkaline solubilization process at pH 11 and 12. The buffer capacity, water-holding capacity and solubility of CPFs with pH-shift treatment were significantly better at alkaline pH (10-12) than at acidic pH (2.0). At pH-shift treatment (pH 2 and 12), the foaming capacities of CPFs from ST and YT were improved compared to those of controls, but they were unstable compared to BH CPFs. The emulsifying activity index (EAI, $m^2/g$ protein) of CPFs (controls) was 16.0-21.1 for BH, 20.1-23.9 for ST and 9.3-13.7 for YT (P<0.05). CPFs adjusted to pH 12 showed improved EAI and YT CPFs showed significantly greater emulsifying ability than those from BH and ST. CPFs recovered from fish roe are not only protein sources but also have a wide range of food functionalities, confirming the high availability of fish sausage and surimi-based products as protein or reinforcing materials for functional foods and alternative raw materials.

• KSBB Journal
• /
• v.13 no.1
• /
• pp.114-118
• /
• 1998

The effects of fibron solubilization conditions on molecular weight distribution of enzymatically-hydrolyzed silk peptides were investigated. The weight-averaged molecular weights of silk proteins prepared by solubilization with calcium chloride, ethylenediamine and sulfuric acid were 41600, 3308, and 1268 dalton, respectively. Silk peptides in the average molecular weight range of 600-1200 dalton were obtained by protease treatment from solubilized silk fibroin. After the acid hydrolysis of silk protein using hydrochloric acid for 24 hr, silk protein was hydrolyzed to peptides whose average molecular weight and free amino acid content were 145 dalton and 80%, respectively. It was possible to control molecular weight distribution of silk peptides by the combination of solubilization and hydrolysis methods. Among the various treatment methods, acid solubilization followed by protease treatment had an advantage of molecular weight control for the peptide production.