• Title, Summary, Keyword: Alcalase

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Enzymatic Treatment of Polyamide Fiber by Alcalase (알칼라제를 이용한 폴리아미드 섬유의 효소가공)

  • Song, Yu-Sun;Song, Wha-Soon
    • Journal of the Korean Society of Clothing and Textiles
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    • v.35 no.8
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    • pp.1006-1013
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    • 2011
  • An enzymatic treatment method using alcalase was introduced to improve the moisture characteristic of the polyamide fiber. The alcalase treatment conditions such as the pH, treatment temperature, enzyme concentration, and treatment time were optimized by measuring the amino groups. The changes in the weight loss, tensile strength, moisture regain, water contact angle (WCA), and water absorption rate of the polyamide fiber with the changes in the alcalase treatment conditions were evaluated. The optimum alcalase treatment conditions for polyamide fiber were found to be a treatment temperature of 50oC, a treatment time of 50 minutes, an alcalase concentration of 10% (owf), and a pH of 7.0. The ethylenediaminetetraacetic acid (EDTA) and L-cysteine accelerated the activity of the enzyme; however, they did not have an effect on the amino group production of the fiber surface. The alcalase treatment of the polyamide fiber improved the fiber's moisture regain, WCA, and absorption rate due to the amino group on the fiber surface. The results showed that the alcalase treatment of polyamide fiber is an effective method to improve the moisture characteristic of the polyamide fiber.

Effect of Enzymatic Hydrolysis by Proteases on Antioxidant Activity of Chungkukjang (단백질 분해 효소 처리가 청국장의 항산화 활성에 미치는 영향)

  • Park, Min-Kyung
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.40 no.2
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    • pp.327-333
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    • 2011
  • Chungkukjang and soybean powder were enzymatically hydrolyzed with 20, 100 and 500 mAU of 3 commercially available proteases (alcalase 2.4L, protamex and neutrase 0.8L) at $50^{\circ}C$ for 120 min. The degree of hydrolysis and antioxidant activities of hydrolysates were comparably evaluated. Alcalase and protamex yielded higher content of peptide compared to neutrase in both Chungkukjang and soybean powder hydrolyzed samples. Both Chungkukjang and soybean hydrolysates showed also greater increases of antioxidant activities compared to those prepared with neutrase. The rates of increment of DPPH, ABTS and hydroxyl radical scavenging activities were similar between Chungkukjang and soybean powder hydrolyzates. These results show that alcalase and protamex are not specific for Chungkukjang but enhance its antioxidant activity.

Optimization of Proteolytic Enzyme Treatment for the Production of Spirulina Extract (단백질 분해 효소를 이용한 스피루리나 추출물 제조 공정 최적화)

  • In, Man-Jin
    • Journal of the Korea Academia-Industrial cooperation Society
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    • v.9 no.2
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    • pp.550-555
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    • 2008
  • An efficient production method of spirulina extract was developed by enzymatic treatment using proteolytic enzymes. The suitable dosage of Tunicase, a cell lytic enzyme, was used to be 2.0% (w/w). To maximize solid recovery and spirulina extraction (SE) index, which indicates nucleic acid-related substances content, the dosage of Alcalase, commercially available pretense, was found to be 1.0% (w/w). By simultaneous treatments using optimal dosages of Tunicase and Alcalase, the highest SE index and solid recovery were obtained. The SE index and solid recovery of simultaneous treatments were notably enhanced by 100% ($11.4%\;{\rightarrow}\;22.8%$) and 56% ($45.2%\;{\rightarrow}\;70.7%$), respectively, than those of the non-treated extracts.

A Study on Iron Binding Peptides from Casein Hydrolysates (Casein 가수분해물 소재 철분결합 Peptide에 관한 연구)

  • Choi, In-Wook;Kim, Ki-Sung;Lim, Sang-Dong;Kim, Hee-Soo
    • Korean Journal of Food Science and Technology
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    • v.29 no.5
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    • pp.1052-1056
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    • 1997
  • When casein was hydrolyzed by trypsin, alcalase, neutrase, protamax, and S. aureus type V8, peptides $(100\;{\mu}g/mL)$ which were produced by trypsin and alcalase solubilized $6.42\;and\;2.37\;{\mu}g/mL)$ of added irons at pH 6, respectively, while peptides which were produced by other proteases solubilized less than $1\;{\mu}g/mL$. Peptides produced by trypsin and alcalase were fractionated to 10 fractions on a reverse phase column and each fraction was tested for its iron solubilizing ability at pH 6. Among peptides produced by trypsin, fraction 5 showed the highest iron solubilizing ability $(2.33\;{\mu}g/mL)$. In the case of alcalase, fraction 7 showed the highest iron solubilizing ability $(1.56\;{\mu}g/mL)$. To isolate iron binding peptides from peptides produced by trypsin and alcalase, immobilized iron affinity chromatography which irons were chelated to imino diacetic acids in chelating sepharose fast flow were utilized. Our results showed that immobilized iron affinity chromatography was an effective method to isolate iron binding peptides produced by either trypsin or alcalase from milk casein.

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Development of High Purity Purification Method of Chondroitin Sulfate Extracted from Skate Cartilage (홍어 연골로부터 추출된 콘드로이틴 황산의 고순도 정제방법 개발)

  • Jeong, Kap-Seop
    • Journal of the Korea Academia-Industrial cooperation Society
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    • v.17 no.6
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    • pp.9-17
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    • 2016
  • A purification method was established for high-purity chondroitin sulfate from skate cartilage. Hydrolytic extraction of skate backbone cartilage was investigated with the proteases alcalase and protamex, and the extraction contents of chondroitin sulfate were measured with several physicochemical processes. The yield of extract from skate cartilage with $40^{\circ}Brix$ concentration was 23.3% with 2% alcalase hydrolysis, which was decreased to 8.47% and 3.37% with the first and second additional ethanol purifications, respectively. The yield was 16.62% with one ethanol purification after hydrolysis with a mixture of 1% alcalase and 1% protamex. The content of chondroitin sulfate was measured as 39.88-45.08% with different ratios of ethanol solvent. The content was 42.92% at a solvent ratio of 1:1 with alcalase protease and 45.08% with a ratio of 1:2 using a protease mixture of alcalase and protamex. The molecular weight range of chondroitin sulfate was about 110-310 thousand Da, and the purity of chondroitin sulfate was 24.87-49.92% with a mixture of alcalase and protamex in GPC analysis. The maximum purity of chondroitin sulfate was 53.93% after ultrafiltration. The odor strength of chondroitin sulfate was decreased by 33% and 38% after ethanol purification and additional filtration with activated carbon, respectively. The odor concentration of ammonia and TMA from chondroitin sulfate was decreased by 52.1% and 37.89% with activated carbon filtration and two ethanol purifications, respectively, but it was necessary to eliminate the odor components efficiently using additional physicochemical processes.

Production of Iron-Binding Peptides from Colostral Whey by Enzymatic Hydrolysis

  • Kim, Sang-Bum;Ku, Min-Jung;Cho, Won-Mo;Ki, Kwang-Seok;Kim, Hyeon-Shup;Nam, Myoung-Soo
    • Food Science of Animal Resources
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    • v.30 no.6
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    • pp.923-929
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    • 2010
  • Colostral whey prepared from colostrum (pooled from first six post-partum milkings) was heated for 10 min at $100^{\circ}C$ Heated colostral whey was incubated with 1% enzymes (protein equivalent basis) for 15, 30, 60, 90, and 120 min at $50^{\circ}C$. Papain, pepsin, trypsin, and alcalase produced different degrees of hydrolysis (DH), 10.66%, 12.42%, 10.83%, and 25.31%, respectively, at an incubation time of 120 min. The SDS-PAGE reveals that significant amounts of bovine serum albumin (BSA), ${\beta}$-lactoglobulin (${\beta}$-LG), and ${\alpha}$-lactalbumin (${\alpha}$-LA) survived papain digestion. In contrast, pepsin completely removed BSA but not ${\beta}$-LG present in heated colostral whey. Alcalase completely eliminated BSA, ${\beta}$-LG, and ${\alpha}$-LA. This differential hydrolysis was confirmed by reversed-phase HPLC analysis. Using ion-exchange chromatography, fraction-1 (F-1) was obtained from alcalase hydrolysate at a NaCl gradient concentration of 0.25 M. Reversed-phase HPLC chromatograms of alcalase F-1 showed numerous small peaks, which probably indicate that a variety of new peptides were produced. Iron content of alcalase F-1 was 28.94 ppm, which was the highest among all enzyme fractions, whereas iron content of colostral whey was 36.56 ppm. Main amino acids contained in alcalase F-1 were Thr (15.45%), Glu (14.12%), and Ser (10.39%). Therefore, alcalase can be used to generate good iron-binding peptides in heated colostral whey, and the resulting iron-binding peptides could be suitable as a value-added food ingredient for food supplements.

Development of Bioactive Substances from Fishery Processing by-products in Jeju (제주 수산가공부산물 유래 기능성 소재 탐색)

  • Kang, Nalae;Lee, WonWoo;Ko, Ju-Young;Kim, Hyun-Soo;Kim, Junseong;Ahn, Yong-Seok;Ko, Chang-Ik;Jeong, Joon Bum;Jeon, You-Jin
    • Journal of Marine Bioscience and Biotechnology
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    • v.6 no.2
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    • pp.62-67
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    • 2014
  • In this study, we investigated the bioactive substances of the Alcalase hydrolysate obtained from fishery processing by-products in Jeju by measuring bioactivities including radical scavenging acitivty, cytoprotective activity against 2,2-azobis-(2-amidino-propane) dihydrochloride (AAPH), and ACE inhibitory activity. This study is important because of utilization of unused fishery processing by-products in Jeju. The Alcalase hydrolysate was prepared through the hot water extraction and enzymatic hydrolysis, and then further separation of the Alcalase hydrolysate was performed by ultrafiltration using 10 kDa molecular weight cut-off membrane. The Alcalase hydrolysate showed the relatively higher DPPH and peroxyl radical scavenging activity ($IC_{50}$ value; 1.30 mg/ml and 0.888 mg/ml, respectively). Also, the Alcalase hydrolysate showed the ACE inhibitory activity with 1.87 mg/ml of $IC_{50}$ value. These biological activities are increased over 1.2 or 2.5 times through the ultrafiltration of the Alcalase hydrolysate. Therefore, the Alcalase hydrolysate obtained from fishery processing by-products in Jeju and the different molecular weight fractions should be given consideration for food and cosmetics ingredient. Furthermore, this research on the utility of fishery processing by-products might be a useful tool into the industry.

Preparation of Egg White Liquid Hydrolysate (ELH) and Its Radical-Scavenging Activity

  • Noh, Dong Ouk;Suh, Hyung Joo
    • Preventive Nutrition and Food Science
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    • v.20 no.3
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    • pp.183-189
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    • 2015
  • In the present study, an optimum protease was selected to hydrolyze the egg white liquid protein for the antioxidant peptides. Alcalase treatment yielded the highest amount of ${\alpha}$-amino groups (15.27 mg/mL), while the control (no enzymatic hydrolysis) showed the lowest amount of ${\alpha}$-amino groups (1.53 mg/mL). Alcalase also gave the highest degree of hydrolysis (DH) value (43.2%) and was more efficient for egg white liquid hydrolysis than the other enzymes. The Alcalase hydrolysate had the highest radical-scavenging activity (82.5%) at a concentration of 5.0 mg/mL. The conditions for enzymatic hydrolysis of egg white liquid with Alcalase were selected as substrate : water ratio of 2:1. Five percent Alacalse treatment did not show significant (P>0.05) increases of DH and ${\alpha}$-amino nitrogen content after 24 hhydrolysis. Thirty two hour-hydrolysis with 5% Alcalase is sufficient to make antioxidative egg white liquid hydrolysate from egg white liquid. DPPH and ABTS radical-scavenging activities were significantly (P<0.05) higher after enzymatic digestion. These results suggest that active peptides released from egg-white protein are effective radical-scavengers. Thus, this approach may be useful for the preparation of potent antioxidant products.

Improvement on the Quality and Functionality of Red Tanner Crab Cooking Drip Using Commercial Enzymes (효소분해의 의한 붉은 대게 자숙액의 품질 및 기능성 개선)

  • Kang, Kyung-Tae;Heu, Min-Soo;Kim, Jin-Soo
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.36 no.8
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    • pp.1022-1030
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    • 2007
  • For the improvement on the quality and functionality of red tanner crab cooking drip, the preparation of hydrolysates from red crab cooking drip using commercial enzymes (Alcalase, Flavourzyme, Neutrase and Protamex) was attempted and its taste, nutritional and functional characteristics were also investigated. According to the results of heavy metal contents and proximate composition, red tanner crab cooking drip (RTCCD) could be used as a food resource. From the results of the trichloroacetic acid soluble index (TSI), angiotensin I converting enzyme (ACE) inhibiting activity and antioxidative activity, RTCCD hydrolysates incubated with Alcalase for 2 hrs was superior to the other one-step hydrolysates. There were no differences in the ACE inhibiting activity and antioxidative activity between one-step hydrolysates, which was incubated with Alcalase for 2 hrs, and two-step hydrolysates sequentially incubated with Alcalase and other enzymes. Alcalase-treated hydrolysates was similar in proximate composition and Hunter color value, while high in free amino acid content compared with crab cooking drip. Total amino acid content of Alcalase-treated hydrolysates was 11.9 g/100 mL and the major amino acids were glutamic acid (10.2%), proline (10.1%) and glycine (10.7%).

Hydrolysis of 7S and 11S Soy Proteins by Commercial Proteases (단백분해효소(蛋白分解酵素)에 의한 대두(大豆) 7S 및 11S 단백질(蛋白質)의 가수분해(加水分解))

  • Kang, Yeung-Joo;Lee, Ki-Chun;Park, Yeung-Ho
    • Korean Journal of Food Science and Technology
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    • v.20 no.3
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    • pp.338-343
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    • 1988
  • Selected kinetic parameters and degree of hydrolysis(DH) were measured using commercial proteases(trypsin, alcalase and pronase) to study the affinity of these enzymes to 7S and 11S soy proteins. Electrophoretic patterns of the hydrolysates were also investigated. In general, the order of affinity between the proteins and the proteases was 11S(protein-rich fraction)and 7S PRF for unheated proteins, and 7S PRF and 11S PRF for preheated proteins. Substrate inhibition was present at a substrate concentration of 1.5% or higher when preheated protein was used as the substrate. The maximum DH values of alcalase were obtained from 7S PRF(60%) and 11S PRF(80%) at 1 hr hydrolysis, respectively. Trypsin hydrolyses did not affect 11S soy protein but the acidic subunits in contrast to alcalase and pronase hydrolyses which changed almost all subunits. Alcalase hydrolysis induced distinct changes on 2S soy protein.

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