• 제목/요약/키워드: enzymatic hydrolyzed

검색결과 203건 처리시간 0.021초

효소분해가 감쥬스의 이화학적 특성에 미치는 영향 (Effect on Enzymatic Hydrolysis on the Physicochemical Properties of Persimmon Juice)

  • 전윤기;최희숙;차보숙;오훈일;김우정
    • 한국식품과학회지
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    • 제29권2호
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    • pp.198-203
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    • 1997
  • 마쇄한 감 puree에 2종류의 상업적 다른 탄수화물 분해효소인 Viscozyme과 Celluclast를 처리하여 얻은 감쥬스의 추출수율, 점도, 색, 적정산도, 당에 미치는 영향을 조사하였다. Arabinase, cellulase, xylanase, hemicellulase와 ${\beta}-glucanase$의 효소활성을 가진 Viscozyme으로 $50^{\circ}C$에서 10분간 가수분해할 때 추출수율, L값, 환원당은 현저히 증가하였고 점도는 감소하였다. 감쥬스의 추출수율은 Viscozyme으로 처리시 42.8%에서 80%로 증가하는 반면 Celluclast는 73.3%로 증가하였다. 한편 관능적 특성중 감맛과 감내, 주홍색과 주황색은 Viscozyme으로 60분간 가수분해한 쥬스에서 크게 향상되었다.

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Enzymatic hydrolysis of insoluble silk sericin by Alcalase

  • Jung, Hye-Young;Bae, Do-Gyu
    • 한국잠사곤충학회지
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    • 제42권1호
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    • pp.48-57
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    • 2000
  • This study was undertaken to figure out the effects of hydrolysis conditions on the solubility of insoluble sericin, molecular weight distribution and thermal characteristics of hydrolysates in enzymatic hydrolysis by Alcalase 2.5L. It was indicated that the optimum treatment temperature and pH for the insoluble sericin were 50$\^{C}$ and 11, respectively. When the insoluble sericin was hydrolyzed with a various treatment conditions, the solubility of all hydrolysates were represented above 85% at given conditions. As the enzyme concentration increased, the solubility increased roughly, but the solubility increasement ratio was less above 2% enzyme concentration. As the treatment time increased, the solubility was also increased. It was showed in the molecular weight distribution of hydrolysates treated various enzyme concentrations and treatment times that when enzyme concentrations were 0.5, 2, 3%, the peaks of the distribution curve were shifted to left side which meant low molecular weight and was distributed much quantity with shifted to be left side, but treatment time was 6 hr. the peak was shifted to right side. When enzyme concentration was 5% and treatment time was below 2 hr., the peaks were shifted to right side, but treatment time was above 4hr. the peak was shifted to left side. The number-average molecular weights were distributed from 300 to 800 and those were decreased when treatment time was up to 4 hr., but increased a little when treatment time was 6hr. It was showed in the DSC curves of hydrolysates treated with treatment time of 0.5, 1, 2, 4, 6 hr. fixed 1% o.w.s enzyme concentration and control that the endothermic peak was observed near at 200$\^{C}$. The denaturation peak of the hydrolysates depending on treatment times had a tendency to shift to higher temperature. But, when the treatment time was 6 hr., the peak was shifted to lower temperature comparing another hydrolysates.

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Antioxidant and ACE Inhibiting Activities of the Rockfish Sebastes hubbsi Skin Gelatin Hydrolysates Produced by Sequential Two-step Enzymatic Hydrolysis

  • Kim, Hyung-Jun;Park, Kwon-Hyun;Shin, Jun-Ho;Lee, Ji-Sun;Heu, Min-Soo;Lee, Dong-Ho;Kim, Jin-Soo
    • Fisheries and Aquatic Sciences
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    • 제14권1호
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    • pp.1-10
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    • 2011
  • This study was conducted to obtain hydrolysates with potent antioxidative activity from rockfish skin gelatin. Gelatin was extracted under high temperature/high pressure using a two-step enzymatic hydrolysis with commercial enzymes such as Alcalase, Flavourzyme, Neutrase, and Protamex. The second rockfish-skin gelatin hydrolysate (SRSGH) was prepared by further incubating the first gelatin hydrolysate (FRSGH), which had been hydrolyzed with Alcalase for 1-h (FRSGH-A1), with Flavourzyme for 2-h (SRSGH-F2). The second gelatin hydrolysate showed higher antioxidative activity of 3.72 as measured by a Metrohm Rancimat and superior angiotensin I-converting enzyme (ACE) inhibiting activity of 0.82 mg/mL. Compared with the gelatin, the relative proportion in SRSGH-F2 was markedly decreased in the 100-kDa peak, whereas it was increased in that less than 100-kDa. The amino acid composition of SRSGH-F2 was rich in glycine (25.9%), proline (10.8%), alanine (9.1%), and glutamic acid (9.1%). In contrast, it was poor in cystine (not detected), methionine (1.6%), tyrosine (0.4%), hydroxylysine (0.9%), and histidine (0.9%). In recent years, demand for natural functional foods has been increasing, and SRSGH-F2 can be used as a functional food ingredient in the food industries. However, further detailed studies on SRSGH-F2 with regard to its antioxidant activity in vivo and the various antioxidant mechanisms are needed.

Haematococcus pluvialis로부터 Haematococcus 추출물 제조 공정에서 효소 처리가 추출 효율과 항산화 활성에 미치는 영향 (Effect of Enzyme Treatments on the Extraction Efficacy and Antioxidant Activity of Haematococcus Extract from Haematococcus pluvialis)

  • 인만진
    • 한국산학기술학회논문지
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    • 제10권1호
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    • pp.194-199
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    • 2009
  • 우수한 항산화제로 알려진 astaxanthin을 함유한 H. pluvialis 균체로부터 작용기작이 상이한 exe형과 endo형의 단백질 분해 효소와 복합 다당류 분해 효소를 이용하여 식품용 haematococcus추출물을 효율적으로 제조할 수 있는 방법을 조사하였다. 상업용 단백질 분해 효소로는 Alcalase (endo형)와 Flavourzyme (exe형)을 복합 다당류 분해효소로는 Viscozyme을 사용하였다. 단백질 분해 효소는 endo형과 exe형을 병용하는 것이 추출물의 astaxanthin 함량을 증가시켰다. Viscozyme과 함께 2종류의 단백질 분해 효소를 사용하는 경우에는 Alcalase와 Flavourzyme을 병용하여 1차로 처리한 후 Viscozyme을 2차로 사용하는 2단계 가수분해 방법이 적절하였다. 이 조건에서 astaxanthin 함량은 효소를 사용하지 않은 대조구에 비하여 320% ($529{\mu}g/g{\rightarrow}2,256{\mu}g/g$) 이상 향상되었다. 또한 DPPH법으로 조사한 항산화 활성은 astaxanthin 함량에 비례하여 증가하였으며, 1차로 Alcalase와 Flavourzyme을 병용하여 처리한 후 2차로 Viscozyme을 사용하는 조건에서 가장 우수하였다.

건조 방법에 따른 홍해삼(Stipchopus japonicus) 효소 가수분해물의 지방 축적 억제 효과 (Inhibition of Lipid Accumulation in 3T3-L1 Adipocytes by Different Enzymatic Hydrolysates of Dried Red Sea Cucumber Stichopus japonicus)

  • 김서영;오재영;김은아;허수진;김길남;전유진
    • 한국수산과학회지
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    • 제53권5호
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    • pp.707-716
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    • 2020
  • Red sea cucumber Stichopus japonicus, was dried using three methods-far-infrared ray, vacuum, and freeze drying and then enzymatically hydrolyzed using nine proteases: Alcalase, Flavourzyme, Kojizyme, Neutrase, Protamex, trypsin, α-chymotrypsin, and papain. In addition, the potential ability of hydrolysates to inhibit lipid accumulation in 3T3-L1 adipocytes was evaluated. The yield of hydrolysates from red sea cucumbers dried using each method was higher than that of the distilled water extract, and protein contents were either similar or higher. The hydrolysates that exhibited inhibitory effects on lipid accumulation, as demonstrated via Oil red O staining, were those obtained by far-infrared ray drying coupled with Alcalase, Flavourzyme, Kojizyme, or Neutrase treatment. In addition to the advantages of far-infrared drying and the characteristics of Flavourzyme, the Flavourzyme hydrolysate of far-infrared-dried red sea cucumber showed the highest inhibitory effect on lipid accumulation. In addition, this hydrolysate significantly decreased the expression of the protein factor fatty acid-binding protein 4, which is related to the late differentiation of 3T3-L1 adipocytes. Taken together, these results suggest that Flavourzyme hydrolysates from farinfrared-dried red sea cucumber may be used as a functional food and/or a pharmaceutical ingredient for the inhibition of lipid accumulation.

분지 베타 글루칸의 저분자화 기술 연구 (Study on the Process to Decrease the molecular Weight of $\beta$-[1,6]-branched $\beta$-[1,3]-D-Glucans)

  • 신현재;이동철
    • KSBB Journal
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    • 제18권5호
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    • pp.352-355
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    • 2003
  • 분자량이 1 MDa 이상인 $\beta$-(1,6)-branched $\beta$-(1,3)-glucan의 효과적인 저분자화 방법을 물리적인 방법, 화학적인 방법, 효소적인 방법으로 나누어 고찰하였다. 물리적인 방법인 초음파처리의 경우엔, 저분자화가 진행됨에 따라 감소하는 저분자화의 효율로 인하여 산업적으로 일정 수준이하의 BBG을 수득하기에 난점이 있으며, 또한 3차 구조의 변성 문제도 주목해야 할 것이다. 화학적인 산 처리법의 경우, 분자량 100,000 Da 이하의 BBG을 산업적으로 수득하기에는 유리할 수 있으나, 약리적 효능에 결정적인 $\beta$-(1,6)-branch의 파괴가 단점이라 할 수 있다. 효소적인 방법이야말로 triple helix 3차 구조의 변성 문제나 $\beta$-(1,6)-branch의 감소 문제를 피하며, 효과적으로 분자량을 감소시킬 수 있음이 확인되었으나, 아직 분지도가 높은 $\beta$-(1,6)-branched $\beta$-(1,3)-glucan까지 효과적으로 가수분해 할 수 있는 효소를 screening 하지는 못하였다.

전자선 조사와 4-메틸모포린-N-옥사이드 용액을 이용한 볏짚의 전처리 방법 (A Facile Pretreatment Method for Rice Straw using Electron Beam Irradiation and 4-methylmorpholine-N-oxide Solution)

  • 이병민;이진영;강필현;전준표
    • 한국미생물·생명공학회지
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    • 제43권1호
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    • pp.16-21
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    • 2015
  • 2세대 바이오매스 볏짚을 이용하여 전자선 조사 후 NMMO 처리 공정을 수행하고 이를 분석하였다. 볏짚은 전자선 500 kGy 조사 후 NMMO 처리를 한 경우 72시간의 효소당화를 거쳐 글루코스 60.8%와 자일로스 9.7% 포함 약 83.8% 정도의 당수율을 보였다. 이 전처리 공정은 유해한 화학물질을 사용하지 않아서 친환경적이며 전자선 조사와 NMMO 처리의 시너지 효과가 있음을 알 수 있었다. 그러나 전자선 조사량이 너무 높다는 단점이 있으며 추후에는 낮은 전자선 조사량과 여러 가지 단일공정을 통합한 새로운 복합전처리 방법 연구의 필요성이 있다. 따라서 이 단점을 보완한다면 전자선 조사라는 친환경적 방법과 더불어 NMMO 용액의 재활용성을 이유로 바이오에탄올 생산 등의 산업현장에의 적용 가능성이 높다는 것을 알 수 있었다.

Characteristics of Morphological and Physiological Changes during the Autolysis Process of Saccharomyces cerevisiae FX-2

  • Li, Xiao;Shi, Xiaodan;Zou, Man;Luo, Yudi;Tan, Yali;Wu, Yexu;Chen, Lin;Li, Pei
    • 한국미생물·생명공학회지
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    • 제43권3호
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    • pp.249-258
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    • 2015
  • In this paper, the autolysis process of Saccharomyces cerevisiae FX-2 (S. cerevisiae FX-2) via, a variety of endogenous enzyme, was investigated systematically by analyzing changes in physicochemical parameters in autolysate, surface morphology and the internal structure of the yeast cells. As an explicit conclusion, the arisen autolysis depended on the pH and the optimal pH was found to be 5.5. Based on the experimental data and the characteristics of mycelia morphology, a hypothesis is put forward that simple proteins in yeast vacuolar are firstly degraded for utilization, and then more membrane-bound proteins are hydrolyzed to release hydrolytic enzymes, which arouse an enzymatic reaction to induce the collapse of the cell wall into the cytoplasm.

김 단백질 가수분해물의 Angiotensin Ⅰ 전환효소 저해 활성 (Angiotensin Ⅰ Converting Enzyme(ACE) Inhibitory Activities of Laver(Porphyra tenera) Protein Hydrolysates)

  • 김영명;도정룡;인재평;박종혁
    • 한국식품영양학회지
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    • 제18권1호
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    • pp.11-18
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    • 2005
  • Angiotensin Ⅰ converting enzyme(ACE) inhibitory activities of laver(Porphyra tenera) protein hydrolysates were investigated by enzymes used for hydrolysis, molecular fractions and drying methods. For the enzymatic hydrolysis, crude laver protein, separated by filtration of water extract of dried laver extracted with 20 times(w/v) water for 3 hours at boiling temperature, were hydrolyzed with three commercial protease, Pepsin, alcalase and maxazyme NNP at optimal conditions. The yield of hydrolysis and ACE inhibitory activities of which were high in order of pepsin, alcalase and maxazyme NNP. ACE inhibitory activities of laver hydrolysates by molecular levels were high in order of 3 kDa > 10 kDa > 3∼10 kDa, and the IC/sub 50/ ACE inhibitory activities by molecular lebels were 4 mg/mL(3 kDa), 5 mg/mL(total hydrolysate), and 20 mg/mL(10 kDa), respectively. The storage stability of dried laver hydrolysates at 20℃ were strongly affected by drying methods, hot air dried of which were much stabler than freeze-dried one.

Purification, Characterization and Chemical Modification of the Xylanase from Alkali-tolerant Bacillus sp. YA-14

  • Park, Young-Seo;Yum, Do-Young;Hahm, Byoung-Kwon;Bai, Dong-Hoon;Yu, Ju-Hyun
    • Journal of Microbiology and Biotechnology
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    • 제4권1호
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    • pp.41-48
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    • 1994
  • The xylanase from alkali-tolerant Bacillus sp. YA-14 was purified to homogeneity by CM-cellulose, Sephadex G-50, and hydroxyapatite column chromatographies. The molecular weight of the purified enzyme was estimated to be 20, 000 Da by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The purified enzyme slightly hydrolyzed carboxymethyl cellulose and Avicel, but did not hydrolyze soluble starch, dextran, pullulan, and ${\rho}-nitrophenyl-{\beta}$-D-xylopyranoside. The maximum degree of hydrolysis by enzyme for birchwood xylan and oat spelts xylan were 47 and 40%, respectively. The Michaelis constants for birchwood xylan and oat spelts xylan were calculated to be 3.03 mg/ml and 5.0 mg/ml, respectively. The activity of the xylanase was inhibited reversibly by $HgCl_2$, and showed competitive inhibition by N-bromosuccinimide, which probably indicates the involvement of tryptophan residue in the active center of the enzyme. The Xylanase was identified to be xylose-producing endo-type xylanase and did not show the enzymatic activities which cleave the branch point of the xylan structure.

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