Earticle

Protein conjugation of curdlan belonging to $\beta$-1, 3-glucan was carried out to improve it surface functionalities. The glucan was mixed with phosvitin, {TEX}$$\alpha$_{s}${/TEX}-casein, lysozyme or ovalbumin, respectively. The mixture was freeze-dried, and he resulting powder was incubated at 6$0^{\circ}C$ and 79% relative humidity for 12 days in order to generate a controlled Maillard reaction between curdlan and proteins. conjugation with unfolding proteins, i.e., phosvitin and {TEX}$$\alpha$_{s}${/TEX}-casein, drastically increased the solubility of the glucan, whereas lysozyme and ovalbmin did not. The solubility in water of curdlan was 3.44% for the phosvitin conjugate and 1.09% for the {TEX}$$\alpha$_{s}${/TEX}-casein conjugate. SDS-slab polyacrylamide gel electrophoresis showed that curdlan was solubilized due to covalent binding with phosvitin. Emulsifying properties of curdlan were substantially improved by the conjugation with phosvitin and {TEX}$$\alpha$_{s}${/TEX}-casein. Emulsion stability of the curdlan-phosvitin conjugate was about 2.9 times greater than that of the curdlan-phosvitin mixture.

The dynamic evolution process has resulted in the myriad shapes, functions, and systems evident in every living organism. For centuries, people have been harnessing the power of evolution to produce new varieties of plants and animals, such as producing tomatoes from berries and Chihuahuas from wolves. Now scientists are using it to produce better molecules, ranging from drugs to industrial chemicals, and doing it in days or weeks rather than eons. The ingenious process, which creates genetic diversity and selects those with desired features in the laboratory, is called directed evolution or test tube evolution. In this paper, concepts of directed molecular evolution and some examples will be discussed.

Three kinds of roe protein concentrates (RPCs: boil-dried concentrate, BDC; steam-dried concentrate, SDC; freeze-dried concentrate, FDC) were prepared from yellowfin tuna to produce value added products for food applications. The buffer capacities of the RPCs were higher under alkaline than under acidic conditions. The water holding capacities of the RPCs were in range 4.5-4.7 g/g protein at pH 6.0. The protein solubility of the FDC (14.2%) was higher than those of the BDC (5.4%) and SDC (5.5%) at pH 6.0. The foaming capacity of the FDC (156.8%) was higher than those of the BDC (109.7%) and SDC (109.4%); the FDC foam was stable for 60 min. The oil-in-water emulsifying activity index of the FDC ($12.2m^2/g$ protein) exceeded those of the BDC and SDC ($2.2m^2/g$ protein). Protein concentrates from yellowfin tuna roe may be useful as a potential protein source and as a high-value food ingredient.

This study was investigated to determine the effect of microbial transglutaminase (MTG) with or without red bean protein isolate (RBPI) on the porcine myofibrillar protein (MP) gel functionality at different pH values (pH 5.75-6.5). Cooking yield (CY, %), gel strength (GS, gf), differential scanning calorimetry (DSC), and scanning electron microscopy (SEM) were determined to measure gel characteristics. Since no differences were observed the interaction between 1% RBPI and pH, data were pooled. CY increased with the addition of 1% RBPI, while it was not affected by pH values. GS increased with increased pH and increased when 1% RBPI was added, regardless of pH. There were distinctive endothermic protein peaks, at 56.55 and 75.02℃ at pH 5.75, and 56.47 and 72.43℃ at pH 6.5 in DSC results, which revealed decreased temperature of the first peak with the addition of 1% RBPI and increased pH. In SEM, a more compact structure with fewer voids was shown with the addition of 1% RBPI and increased pH from 5.75 to 6.5. In addition, the three-dimensional structure was highly dense and hard at pH 6.5 when RBPI was added. These results indicated that the addition of 1% RBPI at pH 6.5 in MTG-mediated MP represent the optimum condition to attain maximum gel-formation and protein gel functionality.

Collagen type III, a member of the fibrillar collagen group, is a major component of the extracellular matrix in various internal organs, the vascular systems, and skin. It is essential to maintain the structural integrity and functionality of these tissues, and plays a significant role in wound healing, often found alongside collagen type I. Despite being the second most abundant collagen in human tissues after type I, its biological functions on various skin properties have not been thoroughly studied. In this study, we have isolated and developed an effective recombinant protein derived from human collagen type III alpha 1 chain (hCOL3A1). Our findings demonstrate that the recombinant proteins hCOL3A1-THR-M1 and M4 stimulate cell proliferation and collagen biosynthesis in human dermal fibroblasts (HDFs), and enhance wound healing. Notably, hCOL3A1-THR-M1 (referred to as HUCOLLATIN3) specifically penetrates both the epidermal and dermal layers in a full-thickness skin model. These results collectively indicate that hCOL3A1-THR-M1 holds promise as a potential biomaterial to prevent skin aging.

We investigated the functional properties and in vitro bioactivity of protein isolates (RPIs) recovered from olive flounder Paralichthys olivaceus roes by isoelectric solubilization/precipitation process, according to pH-shift treatments. The buffer capacity of RPIs was shown to be stronger in alkaline pH than in acidic pH. Water holding capacity of RPIs was in range of 4.5-5.2 g/g protein with no significant differences (P>0.05). The foaming capacity and emulsifying activity index of RPIs did not show any significant differences between RPI-1 (pH 11/4.5) and 3 (pH 12/4.5), however they were superior to RPI-2 (pH 11/5.5) and 4 (pH 12/5.5). The 2,2'-azino-bis-3-ethylbenzo-thiazoline-6-sulfonic acid radical scavenging activity of RPI-3 (2.5 mg protein/mL) was 102.4 ㎍/mL, and the angiotensin I converting enzyme inhibitory activity was 30.8%. Among the RPIs, RPI-3 was relatively superior in protein functional properties such as buffer capacity, foaming capacity, emulsification, and anti-oxidative activity. Therefore, we suggest that RPI prepared from olive flounder roes could serve as a potential food resource.

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.

Roe protein hydrolyzates were prepared from protein isolate of olive flounder Paralichthys olivaceus roe using various proteases, and their bioactivity and functional properties were investigated. Pantidase NP-2 (PN, 14.2%) showed the highest degree of hydrolysis, followed by flourzyme (FL, 6.7%) and aroase AP-10 (AA, 6.5%). Free and released amino acid contents were significantly higher in PN (2,931.2 mg/100 g) and FL (2,725.6 mg/100 g) than in the other hydrolyzates (437.3-812.8 mg/100 g). The foaming activities (%) of papain (PA), trypsin (TR), and bromelain (BR) hydrolyzates were 193.4%, 176.7%, and 144.2%, respectively. The emulsifying activity indices of PA, BR, chymotrypsin, and TR (9.5-30.9 m²/g-protein) were superior to those of other the hydrolyzates (2.0-8.0 m²/g-protein, (P<0.05). The 2,2'-azino-bis-3-ethylbenzo- thiazoline-6-sulfonic acid (ABTS⁺) radical scavenging activities of protamex (PR, 108 ㎍/mL) and AA (115.5 ㎍/mL) were more potent (P<0.05). Angiotensin I converting enzyme inhibitory activities of all enzyme hydrolyzates (52.0-83.3%) were more robust compared with that of control. Among the enzyme hydrolyzates, AA, FL, and PR showed relatively good tyrosinase inhibitory activities compared to that of the control (29.3%). Bioactivity and food functional properties showed that TR, BR, AA, and FL were superior.

This study evaluated the protein recovery, functional properties and biological activity of isolate processed water (IPW) generated in the preparation of protein isolates from fish roes (BH, bastard halibut Paralichthys olivaceus; ST, skipjack tuna Katsuwonus pelamis; YT, yellowfin tuna Thunnus albacares) by an isoelectric solubilization and precipitation process. The IPWs contained 2.7-5.4 mg/mL of protein, and the protein losses were 8-21% (P<0.05). The form capacity of IPW-3 for BH and ST, and IPW-4 for YT was 155, 194, and 164%, respectively. The emulsifying activity index ($27-43m^2/g$) of the YT-IPWs was the strongest, followed by ST ($7-29m^2/g$) and BH ($10-19m^2/g$). The 2,2-diphenyl-1-picrylhydrazyl scavenging activities of IPW-1 and -3 were higher than those of IPW-2 and -4. The 2,2'-azino-bis-3-ethylbenzothiazoline-6-sulfonic acid scavenging activity ($IC_{50}$, mg/mL) of IPW-2 and -4 was 0.03 mg/mL for BH, 0.04-0.08 mg/mL for ST, and 0.04-0.07 mg/mL for YT. BH IPW-3 had the strongest reducing power (0.41 mg/mL) and superoxide dismutase-like activity (1.68 mg/mL). The angiotensin-I converting enzyme inhibitory activity of IPW-3 was the highest for ST (1.52 mg/mL), followed by BH and YT. The common predominant amino acids in the IPWs were the essential amino acids Val, Leu, Lys, and Arg and the non-essential amino acids Ser, Glu, and Ala.