• Journal of Sericultural and Entomological Science
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• v.41 no.3
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• pp.211-215
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• 1999

The pure-separation of calcium chloride-treated fibroin hydrolysates could be carried out using gel filtration chromatography. Also, the effect of its enzymatic hydrolysis was investigated in order to find out the enhancement of their functionality. The average molecular weight(Mw), solubility and free amino acid compositions of three hydrolysates samples (calcium chloride, calcium chloride-flavourzyme and calcium chloride-thermoase)were measured to compare their characteristics. The molecular weight of calcium chloride hydrolysate was about Mw 46,800 and it can be reduced to Mw 12,500 and 1,070 upon the enzymatic hydrolysis by flavourzyme and thermoase, repectively. A solubility of calcium chloride-treated samples shows about 60% while calcium chloride/enzyme-treated samples are perfectly soluble (100% solubility). The total amino acid composition of calcium chloride enzymatic hydrolysates are much higher than that of calcium chloride hydrolysate.

• Journal of the Korean Society of Food Science and Nutrition
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• v.39 no.7
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• pp.953-959
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• 2010

We extracted bioactive materials from Codium fragile by enzymatic hydrolysis using four different proteases (Alcalase, Flavourzyme, Neutrase, and Protamex) and seven different carbohydrases (amyloglucosidase (AMG), Celluclast, Dextrozyme, Maltogenase, Promozyme, Termamyl, and Viscozyme), and evaluated their biological activities such as antioxidant, anti-acetylcholinesterase (AChE), and anti-inflammatory effects. All enzymatic hydrolysates showed good DPPH radical scavenging capacities, in particular, Flavourzyme and Promozyme hydrolysates possessed the highest activity. The two hydrolysates also exhibited strong hydrogen peroxide scavenging activity, $Fe^{2+}$ chelating activity, and reducing power in a dose-dependent manner. Furthermore, the two hydrolysates effectively protected DNA damage induced by hydroxyl radical by measuring the conversion of supercoiled DNA to the open circular DNA. All enzymatic hydrolysates also showed high anti-AChE inhibitory activities in a dose-dependent manner, and did not showed any significant cytotoxicity on RAW264.7 cells (p<0.05). In addition, the enzymatic hydrolysates significantly (p<0.05) inhibited lipopolysaccharide induced-nitric oxide production on RAW264.7 cells. These results suggest that the enzymatic extracts from Codium fragile would be good source as an ingredient of functional foods.

• Journal of Fisheries and Marine Sciences Education
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• v.29 no.1
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• pp.108-117
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• 2017

Laver, Porphyra, is distinctive for its high content of proteins and polysaccharides such as porphyran and hemicellulose. The chemical properties of the polysaccharides extracted with different extraction methods such as hot water, dilute acid(pH 4.0) or alkali solution(2N NaOH) were examined to investigate the suitable extraction conditions for porphyran and hemicellulose from laver. For porphyran extraction, dilute acid solution was more preferable to hot water and alkali solution because of its higher 3,6-anhydrogalactose content and lower protein content. However, alkali solution was more suitable to extract the hemicellulose because of higher mannose content indicating the extraction of mannan. To decrease contamination of the polysaccharides with protein, the dried lavers were pretreated with enzymes (Protamex, Flavourzyme, Alcalase, Viscozyme) before hot water extraction. All enzyme pretreatments increased the yield of polysaccharides by compared with control (enzyme unpretreated) and Flavourzyme pretreatment was most effective to decrease protein contamination in the polysaccharide. All viscosities of porphyran solutions pretreated by enzymes were lower compared to the control porphyran solution and showed pseudoplastic behavior with yield stress. In case of alkali extraction of residues obtained after enzyme hydrolysis and hot water extraction, protease pretreatment increased the mannose contents in the polysaccharide while the xylose content was increased by Viscozyme pretreatment.

• ALGAE
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• v.19 no.1
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• pp.59-68
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• 2004

Hizikia fusiformis hydroysates by five carbohydrases (Viscozyme, Celluclast, Termamyl and Ultraflo) and five proteases (Protamex, Kojizyme, Neutrase, Flavourzyme and Alcalase) were investigated for their extraction efficacy (yield and total total polyphenolic content) and antioxidative activity (DPPH radical and hydrogen peroxide scavenging activity). Termamyl and Ultraflo of the carbohydrases and Flavourzyme and Alcalase of proteases were selected by their high eficacy of extraction and antioxidative activity. Selected enzymes were used to investigate the optimum enzymatic reaction time and dosage (enzyme/substrate ratio) suitable for hydorolysis. Optimum reaction time for the enzymatic hydrolysis was 3 days and optimum dosage of hydrolysis was observed as 5%. Simultaneously, Ultraflo of the two carbohydrases and Alcalse of the two proteases were selected as the most effective enzymes. Combination of Ultraflo and Alcalase under optimum hydrolysis conditions could intensify the extraction efficacy of antioxidative materials form H. fusiformis. The hydrolysate obtained by combining the enzymes was separated into four different molecular weight fractions (<1kD, 1-10 kD, 10-30 kD and >30 kD) and recorded the polyphenolic content distribution and respective antioxidative ability. The fraction <1kD was identified as less effective and those fractions > 1kD indicated comparatively higher antioxidative activities related to their polyphenolic content.

• Journal of the Korean Society of Food Science and Nutrition
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• v.42 no.7
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• pp.1162-1166
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• 2013

Proteins from sunflower seeds were hydrolyzed with Alcalase and Flavourzyme to isolate iron-binding peptides. The optimal hydrolysis conditions were determined. Hydrolysates were filtered under a 3 kDa membrane and iron-binding peptides separated from the hydrolysates using ion exchange and gel permeation chromatographic methods. A fraction with the highest iron-binding activity (Fe/peptide, 0.69), F22, was obtained. These results suggest that fractions isolated from sunflower seed protein hydrolysates can be applied toward the production of iron supplements.

• Food Science of Animal Resources
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• v.40 no.2
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• pp.172-182
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• 2020

In the present study, we determined the degree of hydrolysis (DH) of porcine blood plasma proteins, albumin, and globulin hydrolyzed by six proteases (alcalase, neutrase, flavourzyme, protamex, trypsin, and papain) for various reaction times. Moreover, antimicrobial activities of hydrolysates against five pathogenic microorganisms (Bacillus cereus, Staphylococcus aureus, Salmonella Typhimurium, Escherichia coli, and Shigella flexneri) were investigated. Alcalase, trypsin, and papain hydrolysates of the three porcine blood proteins showed higher DH values than hydrolysates produced by the other three proteases. DH of the three porcine blood proteins hydrolyzed by the six proteases failed to increase after 2 h of hydrolysis. In antimicrobial tests, hydrolysates (hydrolysis time of 2 h) showed antibacterial activity only against B. cereus. Albumin hydrolysates showed higher antimicrobial activity than globulin and plasma hydrolysates. Albumin hydrolysates obtained with flavourzyme, protamex, and trypsin showed higher antimicrobial activity than those obtained with the other three proteases.

• Korean Journal of Food Science and Technology
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• v.31 no.3
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• pp.727-733
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• 1999

Endo- and exoproteases were used to hydrolyze Alaska pollack processing scrap. In 2 stage hydrolysis, the optimal conditions by Protamex were: temperature, $45.8^{\circ}C$; pH, 6.73; enzyme concentration, 0.11%; time, 105.5 min, whereas those by Flavourzyme were: temperature, $42.0^{\circ}C$; pH, 6.54; enzyme concentration, 0.28%; time, 20.4 hrs. But, the optimal conditions of 1 stage hydrolysis by equal proportion of Protamex and Flavourzyme were: temperature, $52.9^{\circ}C$; pH, 6.3; enzyme concentration, 0.46%; time 10.9 hrs. The contents of carbohydrate and ash were higher in the 2 stage hydrolyzate than the 1 stage, while that of crude lipid was in the reverse order. There were no significant differences in the contents of moisture and crude protein between both methods. The contents of total creatine and IMP, and viable cell counts were higher in the 1 stage hydrolyzate than the 2 stage, while the contents of TMAO, TMA, and Hx was in the reverse order. But, there were no significant differences in the contents of amino-N and color between both methods. The free amino acid contents of the 1 and 2 stage hydrolyzate were 2,741.77 and 3,529.47 mg/100 mL, respectively.

• Journal of Ginseng Research
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• v.34 no.4
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• pp.321-326
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• 2010

Enzymatic treatment conditions for red ginseng residue (RGR) were investigated to apply RGR as a microbial medium. Polysaccharide hydrolyase and protease were screened to obtain high solid and carbohydrate yields, and a good degree of carbohydrate hydrolysis. The optimal dosage and reaction time for Viscozyme, the chosen polysaccharide hydrolyase, were found to be 1.0% (w/w) and 3 h, respectively. Of the tested proteases, Flavourzyme, whose optimal dosage was 0.5% (w/w), was selected. Co-treatment with the optimal dosages of Flavourzyme and Viscozyme increased solid yield, carbohydrate yield, and degree of carbohydrate hydrolysis by 76%, 65%, and 1,865%, respectively, over levels in non-treated RGR. The culture characteristics of Leuconostoc mesenteroides strain KACC 91459P grown in enzymatically hydrolyzed red ginseng residue (ERGR) and RGR suspensions were compared. After cultivation for 6 h, the viable cell counts of both cell suspensions rapidly increased to $1.3{\times}10^9$ colony-forming units (CFU)/g. Moreover, while the viable cell population drastically decreased to $2.4{\times}10^6\;CFU/g$ for cells grown in RGR medium, it was maintained in cells fermented in ERGR medium for 24 h.

• Preventive Nutrition and Food Science
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• v.13 no.3
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• pp.166-175
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• 2008

In this study, we focused on natural water-soluble antioxidants from the Jeju benthic diatoms, Achnanthes longipes, Navicula sp. and Amphora coffeaeformis. They were prepared by enzymatic digestion using five carbohydrases (Viscozyme, Celluclast, AMG, Termamyl and Ultraflo) and five proteases (Protamex, Kojizyme, Neutrase, Flavourzyme and Alcalase) and their potential antioxidant activity was assessed. Among the enzymatic digests, Neutrase digest from A. coffeaeformis exhibited the highest effect in DPPH radical scavenging. Flavourzyme (48.7%), Viscozyme (47.4%) and Celluclast (45.7%) digests from Navicula sp. exhibited higher $O^{{\cdot}-}_2$ radical scavenging activity. Viscozyme digest from A. coffeaeformis (45.9%) possessed the highest effects in hydroxyl radical scavenging. Termamyl (89.3%) and Protamex (88.8%) digests from A. coffeaeformis had strong metal chelating activity. Lipid peroxidation was significantly inhibited in Termamyl and Kojizyme digests from A. longipes, AMG and Termamyl digests from Navicula sp. and Kojizyme digest from A. coffeaeformisi. These data suggest that enzymatic digests of the Jeju benthic diatoms might be valuable sources of antioxidant which can be applied in food and pharmaceutical industry.

• Preventive Nutrition and Food Science
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• v.20 no.3
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• pp.176-182
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• 2015

Abalone protein was hydrolyzed by enzymatic hydrolysis and the optimal enzyme/substrate (E/S) ratios were determined. Abalone protein hydrolysates (APH) produced by Protamex at E/S ratio of 1:100 showed angiotensin I converting enzyme inhibitory activity with $IC_{50}$ of 0.46 mg/mL, and APH obtained by Flavourzyme at E/S ratio of 1:100 possessed the oxygen radical absorbance capacity value of $457.6{\mu}M$ trolox equivalent/mg sample. Flavourzyme abalone protein hydrolysates (FAPH) also exhibited $H_2O_2$ scavenging activity with $IC_{50}$ of 0.48 mg/mL and $Fe^{2+}$+ chelating activity with $IC_{50}$ of 2.26 mg/mL as well as high reducing power. FAPH significantly (P<0.05) protected $H_2O_2$-induced hepatic cell damage in cultured hepatocytes, and the cell viability was restored to 90.27% in the presence of FAPH. FAPH exhibited 46.20% intracellular ROS scavenging activity and 57.89% lipid peroxidation inhibition activity in cultured hepatocytes. Overall, APH may be useful as an ingredient for functional foods.