• Title/Summary/Keyword: alcalase

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Properties of hydrolyzed α-lactalbumin, β-lactoglobulin and bovine serum albumin by the alcalase and its immune-modulation activity in Raw 264.7 cell

  • Yu, Jae Min;Son, Ji Yoon;Renchinkhand, Gerelyuya;Kim, Kwang-Yeon;Sim, Jae Young;Nam, Myoung Soo
    • Korean Journal of Agricultural Science
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    • v.47 no.3
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    • pp.459-470
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    • 2020
  • This study investigated the effects of the proteolytic hydrolysates of α-lactalbumin (LA), β-lactoglobulin (LG) and bovine serum albumin (BSA) by alcalase on inflammatory cytokines. The proteolytic hydrolysates were separated into two fraction of peptides, ≤ 10,000 Da and > 10,000 Da, respectively, because various low molecular weight peptides were generated during the hydrolysis reaction time. Among the hydrolysate peptides, BSA (all types), β-LG (> 10,000 Da), and α-LA (> 10,000 Da) showed an inhibitory activity against thymic stromal lymphopoietin (TSLP) mRNA expression in lipopolysaccharide-induced RAW264.7 murine macrophages. α-LA (> 10,000 Da), β-LG (hydrolysates), and BSA (> 10,000 Da) showed an inhibitory activity against tumor necrosis factor (TNF)-α expression. α-LA (all types), β-LG (hydrolysates, > 10,000 Da), and BSA (> 10,000 Da) showed an inhibitory activity against interleukin-6 (IL-6) expression. α-LA (> 10,000 Da), β-LG (> 10,000 Da), and BSA (all types) showed an inhibitory activity against inducible nitric oxide synthase (iNOS) expression. α-LA (> 10,000 Da), β-LG (> 10,000 Da), and BSA (all types) showed an inhibitory activity against cyclooxygenase (COX)-2 expression. The lowest level of TNF-α production was measured with α-LA (> 10,000 Da) and β-LG (> 10,000 Da) for all types, and a similar low level was measured for all types of BSA. The highest level of IL- 6 production was measured with α-LA (≤ 10,000 Da) among α-LA, β-LG, and IL-6. The low level of NO production was similar with α-LA, β-LG, and BSA but not with α-LA (≤ 10,000 Da). These potential peptides from whey protein hydrolysates could be used for food, medicinal, and industrial applications.

Antioxidant Potential of Enzymatic Extracts from Blueberry (Vaccinium corymbosum L.) (블루베리 (Vaccinium corymbosum L.) 유래 효소 추출물의 항산화성)

  • Senevirathne Mahinda;Jeon You-Jin;Ha Jin-Hwan;Cho Somi K.;Kim Soo-Hyun
    • Journal of Life Science
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    • v.16 no.1
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    • pp.49-57
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    • 2006
  • Enzymatic extracts were prepared from the blueberry (Vaccinium corymbosum L.) collected in Jeju, Korea. Five carbohydrases namely AMG, Celluclast, Termamyl, Ultraflo and Viscozyme, and five proteases namely Alcalase, Flavourzyme, Kojizyme, Neutrase and Protamex were used to prepare the enzymatic extracts. Antioxidant properties of each extracts were studied using stable 1,1-diphenyl 2-picrylhydrazyl (DPPH), reactive oxygen species (ROS), nitric oxide (NO) scavenging, metal chelating assays and lipid peroxidation inhibitory activity in hemoglobin-induced linoleic acid system. The phenolic content of all enzymatic extracts was in the range of 517.85-597.96 mg/100 g dried sample. DPPH and NO${\cdot}$scavenging, and metal chelating assays exhibited prominent activities. Viscozyme showed the highest DPPH activity $(0.046{\pm}0.002\;mg/mL)$ while AMG Showed the highest activity in NO${\cdot}$scavenging $(0.339{\pm}0.011\;mg/mL)$. All the extracts exhibited strong metal chelating activities. Blueberry enzymatic extracts also showed relatively good activity in hydrogen peroxide scavenging. AMG showed the highest lipid peroxidation inhibitory activity $(0.28{\pm}0.01\;mg/mL)$ in hemoglobin-induced linoleic acid system. In this results, the blueberry, which has potential antioxidant components, may be a good candidate as a natural antioxidant source.

Reduction of Antigenicity of Bovine Casein by Microbial Enzymes (미생물효소에 의한 우유 casein의 항원성 저감화)

  • Choe, Hyeon-Seok;Ahn, Jong-Nam;Jeong, Seok-Geun;Ham, Jun-Sang;In, Yeong-Min;Kim, Dong-Un
    • Journal of Dairy Science and Biotechnology
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    • v.21 no.2
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    • pp.97-104
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    • 2003
  • It is extremely important to destroy the antigenicity of milk proteins for dietetic treatment of infants with milk allergy. Enzymatic digestion of milk protein is not only effective for destroying antigenicity, but it also is less liable to alter the nutritive value. Bovine casein was hydrolyzed with eight different commercial proteases derived from bacterias or fungi, either individually or in combination to eliminate protein allergenicity. The average molecular weight of casein hyrdolysates determined by size exclusion chromatography is about 550${\sim}$2,300 dalton range. Antigenicity of the casein hyrdolysates was not detected by heterologous passive cutaneous anaphylaxis in guinea pig-rabbit antiserum system. The inhibition test on the enzyme-linked immunosorbent assay(ELISA) showed that the antigenicity of casein hydrolysates is lowed up to 1/8,000 than that of intact bovine casein. As the enzyme reaction was carried out by the combination of bacterial and fungal protease, casein hydrolysates showed much lower bitterness and antigenicity. It suggests that these hydrolysates will be applied to many kinds of foods including the development of hypo-allergenic infant formula.

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Characteristics of protein from red crab (Chionoecetes japonicus) shell by commercial proteases (효소적 가수분해에 의한 홍게껍질 단백질의 특성)

  • Noh, Kyung-Hee;Min, Kwan-Hee;Seo, Bo-Young;Kim, So-Hee;Seo, Young-Wan;Song, Young-Sun
    • Journal of Nutrition and Health
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    • v.45 no.5
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    • pp.429-436
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    • 2012
  • This study was performed to examine the characteristics of protein of red crab (Chionoecetes japonicus) shell powder hydrolyzed by commercial proteases. Red crab shell was digested by commercial proteases, such as Protamex (P), Neutrase (N), Flavourzyme (F), Alcalase (A), Protease M (PM) and Protease A (PA). Protein yield analyzed by Biuret assay, absorbance at 280 nm and brix revealed that PA was the enzyme having the highest proteolytic activity. SDS PAGE showed that molecular weight of proteins produced by protease treatments was various and below 150 kDa. Combinational treatment of proteases (PA + P, PA + PM, PA + F, PA + A) was tried whether these increase protein hydrolysis from red crab shell powder compared to a PA single treatment. Soluble protein content was similar, but amino acid concentration by combinational treatments was higher than PA single treatment [PA + P 247.4 mg/g > PA + F (206.4 mg/g) > PA + A (133.4 mg/g) > PA + PM (59.1 mg/g) > PA (54.9 mg/g)]. Amino acid composition by combinational treatments was slightly different. Most abundant essential amino acids were phenylalanine, glycine, alanine, and leucine, whereas tyrosine and cystine were not detected.

Preparation and Functional Properties of Enzymatic Oyster Hydrolysates (굴 효소 가수분해물의 제조 및 기능특성)

  • Chung, In-Kwon;Kim, Hye-Suk;Kang, Kyung-Tae;Choi, Yeung-Joon;Choi, Jong-Duck;Kim, Jin-Soo;Heu, Min-Soo
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.35 no.7
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    • pp.919-925
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    • 2006
  • The study was carried out to prepare oyster hydrolysates by using Alcalase, Flavourzyme, Neutrase, Protamex, pepsin and trypsin, and to investigate its functional properties. The ACE inhibitory activity and antioxidant activity of enzymatic oyster hydrolysates did not increase with hydrolysis time. Among enzymatic oyster hydrolysates, oyster hydrolysates incubated with Protamex for 1 hr (OHP) showed the most excellent ACE inhibitory activity and antioxidant activity, and their $IC_{50}$ values were 1.16 mg/mL and 1.49 mg/mL, respectively. However, all enzymatic oyster hydrolysates were not detected in antimicrobial activity.

Optimization and Flavor Quality of Enzymatic Hydrolysate from Dark Muscle of Skipjack

  • Jang, H.J.;Kim, M.C.;Jung, E.M.;Shin, E.C.;Lee, S.H.;Lee, S.J.;Kim, S.B.;Lee, Y.B.
    • Preventive Nutrition and Food Science
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    • v.10 no.1
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    • pp.11-16
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    • 2005
  • Enzymatic hydrolysis of dark muscle of skipjack was optimized by using response surface methodology. Three factors of independent values were pH (4.2 to 9.8), time (0.6 to 3.4 hrs) and temperature (34℃ to 76℃), and independent values were optical density and brix. The optimum conditions for enzymatic hydrolysis were pH 7.0 to 8.0, 55℃ and 3 hrs. The headspace volatile compounds of reaction flavors using the enzymatic hydrolysate, cysteine and xylose were identified by using the combination of a canister system, gas chromatography and mass selective detector. Among 67 compounds, we identified 8 sulfur-containing compounds and 7 furans which were thought to be highly related to meat-like flavors.

Attenuating Development of Cardiovascular Hypertrophy with Hydrolysate of Chicken Leg Bone Protein in Spontaneously Hypertensive Rats

  • Cheng, Fu-Yuan;Wan, Tien-Chun;Liu, Yu-Tse;Lai, Kung-Ming;Lin, Liang-Chuan;Sakata, Ryoichi
    • Asian-Australasian Journal of Animal Sciences
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    • v.21 no.5
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    • pp.732-737
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    • 2008
  • This study developed a natural ingredient as a functional food possessing properties of attenuation of hypertension and cardiovascular hypertrophy. In a previous study hydrolysates obtained from chicken leg bone protein using Alcalase strongly inhibited angiotensin I converting enzyme (ACE) in vitro. In particular, hydrolysate (A4H) from four hours of incubation exhibited the highest ACE inhibitory activity (IC50 = 0.545 mg/ml). A4H was selected as a potent ACE inhibitor and orally administrated to spontaneously hypertensive rats (SHR) for eight weeks to investigate attenuating effects on age-related development of hypertension and cardiovascular hypertrophy. Results showed that treatment with A4H of SHRs attenuated the development of hypertension as effectively as the clinical antihypertensive drug captopril. Moreover, a significantly lower heart to body weight ratio and thinness of coronary arterial wall was observed in SHRs that had been treated with A4H or captopril. The results suggest that A4H can be utilized in developing an ACE inhibitor as a potential ingredient of functional foods to alleviate hypertension and cardiovascular hypertrophy.

Characterization of an antioxidant peptide from katsuobushi (dried bonito) protein hydrolysates

  • Lee, Jung Kwon;Jeon, Joong-Kyun;Byun, Hee-Guk
    • Journal of Marine Bioscience and Biotechnology
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    • v.7 no.1
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    • pp.19-27
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    • 2015
  • The objective of the current study was to evaluate the inhibitory and antioxidant activities of powdered katsuobushi (dried bonito) protein hydrolysates and their corresponding fractions. The powdered katsuobushi (dried bonito) hydrolysates were obtained by enzymatic hydrolysis using Alcalase, ${\alpha}$-chymotrypsin, Neutrase, pepsin, papain, and trypsin. The antioxidant efficacy of the respective hydrolysates were evaluated using 2,2-diphenyl-1-picrylhydrazyl (DPPH), hydroxyl, superoxide, and alkyl radical-scavenging activities. Among the hydrolysates, the peptic-derived hydrolysate exhibited the highest antioxidant activity compared to other enzymatic hydrolysates. Therefore, the peptic-derived hydrolysate was further analyzed, and was found to contain an active peptide with an amino acid sequence identified as Pro-Met-Pro-Leu-Asn-Ser-Cys (756 Da). The purified peptides from powdered katsuobushi (dried bonito) had an $EC_{50}$ value of $105.82{\mu}M$, and exhibited an inhibitory effect against DNA oxidation induced by hydroxyl radicals. Taken together, these results suggests that powdered katsuobushi (dried bonito) could be used as a natural antioxidant in functional foods and prevent oxidation reactions in food processing.

Enzymatical Hydrolysis of Low-Usefulness Marine Resources (이용도가 낮은 수산자원의 효소적 가수분해 조건)

  • 배태진
    • The Korean Journal of Food And Nutrition
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    • v.11 no.4
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    • pp.394-401
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    • 1998
  • In present work, the development of processing for various fermented sea foods using low-usefulness marine resources were investigated. The optimum temperatures of autolysis were 35$^{\circ}C$ for hair tail, 45$^{\circ}C$ for gizzard shad, 30$^{\circ}C$ for kangdale, 30$^{\circ}C$ for pen shell and 30$^{\circ}C$ for oyster and when alcalse(Novo Co.) were added, optimum temperatures were 60$^{\circ}C$, 50$^{\circ}C$, 50$^{\circ}C$, 50$^{\circ}C$ and 50$^{\circ}C$, respectively, and protease N, P. (Pacific chem. enzyme mixture 2,000) were 55$^{\circ}C$, 60$^{\circ}C$, 50$^{\circ}C$, 50$^{\circ}C$ and 50$^{\circ}C$, respectively. Especially although exozymes and endozymes reacted at same time, hydrolysis rate of raw materials got to maximum at optimum temperatures of exozymes. The facts showed that exozymes dominated the hydrolysis reached max8imum at pH 9.0, and optimum hydrolysis time of all raw materials were 6 hours. And the optimum concentrations of exozymes were about 3.0% for hair tail, 4.5% for gizzard shad, 3.5% for kangdale, 3.0% for pen shell and 3.0% for oyster, respectively.

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Rapid Processing of Hydrolyzed Sauce Using Low-Usefulness Fish and Shellfish (이용도가 낮은 어패류의 가수분해물을 이용한 속성액젓의 제조)

  • 배태진;최옥수
    • The Korean Journal of Food And Nutrition
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    • v.11 no.4
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    • pp.402-408
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    • 1998
  • A rapid processing method for fermented sauce of favorable flavor was investigated with low-usefulness marine resources. Hydrolyzed at optimal conditions for 6 hours usuing alcalase, and separated by molecularporous membrane. It's very effective for remove bitter taste at below M.W. 100 dalton, and effective at below M.W.500 dalton. Added 2% invert sugar in fermented sauce at below M.W.500 dalton, and thermal treatment at 100$^{\circ}C$ for 30 minutes were improved flavor. Chemical composition of fermented sauce using hair tail were 80.7% of moisture, 2.2% of carbohydrate, 1.8% of total nitrogen, 1.6% of amino nitrogen and pH was 6.5. The ratio of amino nitrogen in total nitrogen was 77.8%. And chemical composition of fermented sauce used gizzard shad, kangdale, pen shell and oyster were similar to fermented sauce used hair tail. Total nitrogen were above 1.8% and the ratio of amino nitrogen in total nitrogen was 77.7∼84.2% in all fermented sauce. Amino acid contents in fermented sauce used hair tail, gizzard shad, kangdale, pen shell and oyster were 4,318.1mg%, 4,681.3mg%, 3,156.2mg% and 4,175.0mg%, respectively. And the predominant free amino acid were glutamic acid, lysine and glycine in all fermented sauce.

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