• Fisheries and Aquatic Sciences
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• v.25 no.6
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• pp.335-349
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• 2022

To optimize the hydrolysis conditions in the production of antioxidant hydrolysates from tuna cooking juice concentrate (TC) to maximize the 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity, TC containing 48.91% protein was hydrolyzed with Alcalase 2.4 L, and response surface methodology (RSM) was applied. The optimum hydrolysis conditions included a 2.2% (w/v) Alcalase concentration and 281 min hydrolysis time, resulting in the highest DPPH radical scavenging activity of 66.49% (0.98 µmol Trolox/mg protein). The analysis of variance for RSM showed that hydrolysis time was an important factor that significantly affected the process (p < 0.05). The effects of different drying methods (freeze drying, hot air drying, and vacuum drying) on the DPPH radical scavenging activity and amino acid (AA) profiles of TC hydrolysate (TCH) were evaluated. Vacuum-dried TCH (VD) exhibited an increase in DPPH radical scavenging activity of 81.28% (1.20 µmol Trolox/mg protein). The VD samples were further fractionated by ultrafiltration. The AA profiles and antioxidant activities in terms of the DPPH radical scavenging activity, 2,2'-azino-bis(3-ethylbenzthiazoline)-6-sulfonic acid (ABTS) radical scavenging activity, ferric reducing antioxidant power, and ferrous ion chelating activity were investigated. Glutamic acid, glycine, arginine, and cysteine were the major AAs found in the TCH fractions. The highest DPPH radical scavenging activity was found in the VD-1 fraction (< 5 kDa). The VD-3 fraction (> 10 kDa) exhibited the highest ABTS radical scavenging activity and ferric reducing antioxidant power. The ferrous ion chelating activity was the highest in VD-1 and VD-2 (5 to 10 kDa). In conclusion, this study provided the optimal conditions to obtain high antioxidant activities through TCH production, and these conditions could provide a basis for the future application of TCH as a functional food ingredient.

• International Journal of Industrial Entomology and Biomaterials
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• v.45 no.2
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• pp.56-69
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• 2022

Silk is a unique natural biopolymer with outstanding biocompatibility, high mechanical strength, and superior optical transparency. Due to its excellent properties, silk has been widely reported as an ideal biomaterial for several biomedical applications. Recently, fluorescent silk protein, a variant of native silk, has been reported as a biophotonic material with the potential for bioimaging and biosensing. Despite the realization of fluorescent silk, the traditional degumming process of fluorescence silk is crude and often results in fluorescence loss. The loss of fluorescent properties is attributed to the sensitivity of silk fibroin to temperature and solvent concentration during degumming. However, there is no comprehensive information on the influence of these processing parameters on fluorescence evolution and decay during fluorescent silk processing. Therefore, we conducted a spectroscopic study on fluorescence decay as a function of temperature, concentration, and duration for fluorescent silk cocoon degumming. Sodium carbonate solution was tested for degumming the fluorescent silk cocoons with different concentrations and temperatures; also, sodium carbonate solution is combined with Alcalase enzyme and triton x-100 to find optimal degumming conditions. Additionally, we conducted a molecular dynamics study to investigate the fundamental effect of temperature on the stability of the fluorescent protein. We observed degumming temperature as the prime source of fluorescent intensity reduction. From the MD study, fluorescence degradation originated from the thermal agitation of fluorescent protein Cα atoms and fluctuations of amino acid residues located in the chromophore region. Overall, degumming fluorescent silk with sodium carbonate and Alcalase enzyme solution at 25 ℃ preserved fluorescence.

• Food Science of Animal Resources
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• v.43 no.4
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• pp.594-611
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• 2023

Whey protein (WP) has nutritional value, but the presence of β-lactoglobulin (β-LG) and α-lactalbumin (α-LA) cause allergic reactions. In this study, hypoallergenic whey protein hydrolyate (HWPH) was prepared by decomposing β-LG and α-LA of WP using exo- and endo-type proteases. The enzyme mixing ratio and reaction conditions were optimized using response surface methodology (RSM). Degradation of α-LA and β-LG was confirmed through gel electrophoresis, and digestion, and absorption rate, and immunostimulatory response were measured using in vitro and in vivo systems. Through RSM analysis, the optimal hydrolysis conditions for degradation of α-LA and β-LG included a 1:1 mixture of Alcalase and Prozyme reacted for 10 h at a 1.0% enzyme concentration relative to substrate. The molecular weight of HWPH was <5 kDa, and leucine was the prominent free amino acid. Both in vitro and in vivo tests showed that digestibility and intestinal permeability were higher in HWPH than in WP. In BALB/c mice, as compared to WP, HWPH reduced allergic reactions by inducing elevated Type 1/Type 2 helper T cell ratio in the blood, splenocytes, and small intestine. Thus, HWPH may be utilized in a variety of low allergenicity products intended for infants, adults, and the elderly.

• Food Science of Animal Resources
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• v.44 no.3
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• pp.723-737
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• 2024

Yeast protein can be a nutritionally suitable auxiliary protein source in livestock food. The breakdown of proteins and thereby generating high-quality peptide, typically provides nutritional benefits. Enzyme hydrolysis has been effectively uesed to generate peptides; however, studies on the potential applications of different types of enzymes to produce yeast protein hydrolysates remain limited. This study investigated the effects of endo- (alcalase and neutrase) and exotype (flavourzyme and prozyme 2000P) enzyme treatments on yeast protein. Endotype enzymes facilitate a higher hydrolysis efficiency in yeast proteins than exotype enzymes. The highest degree of hydrolysis was observed for the protein treated with neutrase, which was followed by alcalase, prozyme 2000P, and flavourzyme. Furthermore, endotype enzyme treated proteins exhibited higher solubility than their exotype counterparts. Notably, the more uniform particle size distribution was observed in endotype treated yeast protein. Moreover, compared with the original yeast protein, the enzymatic protein hydrolysates possessed a higher content of β-sheets structures, indicating their higher structural stability. Regardless of enzyme type, enzyme treated protein possessed a higher total free amino acid content including essential amino acids. Therefore, this study provides significant insights into the production of protein hydrolysates as an alternative protein material.

• Korean journal of food and cookery science
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• v.26 no.1
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• pp.18-25
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• 2010

This study was carried out to investigate the total polyphenol and flavonoid contents and antioxidative activities of enzymatic digests from dried Citrus unshiu and C. grandis peels. The yields of digests from dried C. unshiu and C. grandis peels were high in viscozyme (a carbohydrase) and kojizyme (a protease), and enzymatic digests from dried C. grandis peels appeared highly comparable to those of C. unshiu. Total polyphenol contents were high in ultaflo (a carbohydrase) and alcalase and flavourzyme (proteases), and the digests from dried C. unshiu peels appeared high in comparison to C. grandis. Total flavonoid contents were high in ultaflo, alcalase, and water extract. DPPH radical scavenging activities appeared very high in digests from dried C. grandis peels in comparison to C. unshiu, and was the highest in viscozyme and kojizyme. The viscozyme digest displayed particularly high activity. Hydrogen peroxide scavenging activities increased somewhat with increasing amounts of digests, but displayed very high activity, more than 91%, except kojizyme the digest from dried C. unshiu peel, at 2.0 mg/mL. Alkyl radical scavenging activities increased rapidly with increasing amounts of digest, and all enzyme digests from dried C. unshiu and C. grandis peels displayed very high activities at more than 0.5 mg/mL. Hydroxyl radical scavenging activities increased rapidly with increasing amounts of digests, and all enzymatic digests from dried C. unshiu and C. grandis peels displayed relatively low activities in comparison to other activated oxygen species.

• Proceedings of the Korean Society of Dyers and Finishers Conference
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• 2008.04a
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• pp.22-24
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• 2008

신발 및 피혁 제품의 분쇄는 섬유의 길이와 물리적인 특성을 고려하여 3${\sim}$4mm 정도의 섬유 길이로 절단되는 Niagara beater가 우수하였고, 섬유간 접착력을 부여하는 Binder 물질로는 NR latex와 EVA emulsion이 인장, 인열강도가 우수하여 NR latex와 EVA emulsion이 7:3의 비율로 혼합하여 사용하는 것이 가장 좋은 결과를 나타내었다. 또한 코팅 처리된 신발 재단 폐기물의 경우 Niagara beater에 Alcalase를 투입하는 것이 분쇄시간의 단축에 유리한 경향을 나타내었고, 건조 공정은 90$^{\circ}C$이하로 유지하는 것이 $^{\triangle}$E값의 변화가 거의 없었고 100$^{\circ}C$에서는 $^{\triangle}$E값이 7.55를 나타내어 황변이 발생하였다.

• Textile Coloration and Finishing
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• v.29 no.4
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• pp.181-194
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• 2017

The biodegradability of polylactic acid(PLA) fabrics was evaluated by two methods: enzyme and soil degradation. Three different enzymes were selected to evaluate. Degradation times were measured at optimal enzyme treatment conditions. Biodegradation by enzymatic hydrolysis was compared with soil degradation. As a result, biodegradation created cracks on the fiber surface, which led to fiber thickening and shortening. In addition, new peak was observed at $18.5^{\circ}$ by degradation. Moreover, cracks indicating biofragmentation were confirmed by enzyme and soil degradation. By enzyme and soil degradation, the weight loss of PLA fabrics was occurred, there through, the tensile strength decreased about 25% by enzyme hydrolysis when 21 days after, and 21.67% by soil degradation when 60 days after. Furthermore, the biodegradability of PLA fabrics by enzymatic and soil degradation was investigated and enzymatic degradation was found to be superior to soil degradation of PLA fabrics. Among the three enzymes evaluated for enzymatic degradation, alcalase was the most efficient enzymes. This study established the mechanism of biodegradation of PLA nonwovens, which might prove useful in the textile industry.

• Journal of Life Science
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• v.11 no.2
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• pp.138-143
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• 2001

Marsh calm(Corbicular elatior)with a short-term storage in raw and a law-rate of utilization has been increasing the needs to develop new marsh calm processing products for a temporary mass treatment and long-term distribution, Therefore the processing conditions of marsh calm beverage using proteolytic enzyme hydrolysis were investigated. A partial hydrolysis at 6$0^{\circ}C$ for 1 hour after adding 3% Alcalase as more effective than a hot water extraction to develop taste compounds from the marsh calm. The result of ommission test showed that nucleotides and their related compounds were contributed in the taste of the marsh calm hydrolysates rather than free amino acids. The taste of the hydrolysates was produced by association with these compounds rather than only one compound s the hydrolystes taste differently for the control when one of these compound was omitted. The hydrolysates were fractionated to molecular weight below 500 dalton to eliminate bitter taste and to improve it flavor from the hydrolysates, 0.05% bay leaf was more effective to improve the odor than other herbs.

• Textile Coloration and Finishing
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• v.3 no.4
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• pp.7-12
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• 1991

Wool gabardines were treated with alkaline proteases, and their tensile strerigth and dyeing behavior were obtained. Enzylon ASA 30 and Alcalase 2.5L DX did not show much effect on the weight loss of wool, but Esperase 8.0L decreased the weight of wool to a great extent. Pretreatment of wool with dichloroisocyarturic acid before protease-treatment increased the weight loss of wool considerably. Weight loss was accompanied by serious strength decrease and the use of sodium sulfate in the protease-treatment had not effect on the strength retention, only lowering the weight loss of wool. Protease-treatment of wool increased dyeability considerably, which may be due to the change in the inner structure of wool fiber by protease.

• ALGAE
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• v.18 no.4
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• pp.341-347
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• 2003

The potential antioxidative activity of water-soluble enzymatic hydrolyzates from a kelp, Ecklonia cava was evaluated by free radical scavenging and lipid peroxidation assays. To prepare water-soluble hydrolyzates from E. cava the seaweed was enzymatically hydrolyzed by five carbohydrases (Viscozyme, Celluclast, AMG, Termamyl and Ultraflo) and five proteases (Protamex, Kojizyme, Neutrase, Flavourzyme and Alcalase). Among all the hydrolyzates, Celluclast hydrolyzate effectively scavenged free radicals released from DPPH (1,1-diphenyl-2- pricrylhydrazyl) and recorded around 73% scavenging activity at the concentration of 4 mg ${\cdot}ml^{-1}$. This hydrolyzate was thermally stable and DPPH radical scavenging activity remained 80% or higher at heating temperatures of 40 and 60$^{\circ}C$ up to 12 h and around 80% at 100$^{\circ}C$ up to 8 h. AMG and Ultraflo hydrolyzate inhibited the lipid peroxidation of fish oil as that of $\alpha$-tocopherol. These results suggested that an enzymatic extraction will be an effective way for the production of a potential antioxidant from seaweeds.