• 제목/요약/키워드: $\alpha$-and $\beta$-amylase

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김치원료의 amylase, protease, peroxidase, ascorbic acid oxidase 활성 (Amylase, Pretease, Peroxidase and Ascorbic Acid Oxidase Activity of Kimchi Ingredients)

  • 김현정;이정진;최미정;최신양
    • 한국식품과학회지
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    • 제30권6호
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    • pp.1333-1338
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    • 1998
  • 본 연구에서는 김치재료 중 존재하는 각종 효소의 특성을 이용한 김치의 품질개선을 위한 기초자료를 제시하고자 몇 가지의 대표적인 가수분해효소와 산화효소의 활성을 조사하였다. 가수분해효소로는 발효원으로 사용되고 균체증식에 필수적인 당 및 아미노산의 생산에 관여하는 amylase와 protease를 연구하였으며, 산화효소로는 이취발생과 vitamin C의 산화에 관여하는 peroxidase 및 ascorbic acid oxidase 활성을 조사하였다. 시료 1 g중 존재하는 효소활성은 ${\alpha}-amylase$의 경우 멸치젓, 고춧가루, 새우젓, 굴에서, ${\beta}-amylase$는 멸치젓, 굴, 무에서 높게 나타났다. Protease의 경우는 멸치젓, 새우젓, 고춧가루에서 높게 나타났으며, peroxidase와 ascorbic acid oxidase는 각각 무, 오이, 파 및 멸치젓, 고춧가루, 새우젓에서 높게 나타나 김치재료중 발효식품인 멸치젓과 새우젓이 전반적으로 높은 가수분해 및 산화활성을 나타내었고, 고춧가루는 가수분해효소 활성이, 무, 오이는 산화효소 활성이 높게 나타났다.

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한국산 벌꿀의 효소활성에 관한 연구 (The Study on the Enzyme Activities in Korean Bee Honey)

  • 김성자
    • 한국환경보건학회지
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    • 제4권1호
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    • pp.47-50
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    • 1977
  • This report is intended to describe as brief as possible the result of study on purity of the Korean Bee Honey. Purity of bee honey was measured by scaling the enzyme activities of two different honey groups: such as, the standard group and control group each including the samples of honey originated from the resource of acarcia, chestnut or miscellaneous origin. The samples of honey were collected from different sources: to wit, honey belonging to the standard group were collected from the township of Seoboo, Yangju county, Kyunggido province, Korea, while honey belonging to the control group were collected from the street side shops, market or the companies producing the secondary food from honey. The results of this study were summarized as follow: 1. It was found that honey belonging to the standard group contained less moisture than those belonging to the control group. Republic of Korea Ministry of Health and Social Affairs Food Control Regulation stipulates that honey must contain moisture less than 20%. The samples of' both groups contained moisture more than 20%, although honey belonging to the control group were relatively more so than honey belonging to the standard group. 2. Honey belonging to the standard group were found stronger in sugar reduction activities than those belonging to the control group. It was also noted that honey of acracia origin was strongest in reduction activities of the three different origin in the same group. 3. $\alpha$-Amylase and $\beta$-amylase were discovered to have activated more strongly in honey belonging to the standard group than those belonging to the control group. The enzyme activitie, varied depending on the origin of plant where honey comes from. For instance, honey of miscellaneous origin indicated the strongest activities in $\alpha$-amylase while honey of chestnut origirt indicated strongest in $\beta$-amylase.

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대맥종자의 Amylase 생성에 미치는 Gibberellic Acid의 촉진효과와 Indole-3-acetic Acid의 억제효과의 해석 (Studies on Gibberellic Acid-promoted and Indole-3-acetic Acid-repressed Amylase Synthesis of Barley Seeds)

  • 채인기
    • Journal of Plant Biology
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    • 제20권2호
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    • pp.91-101
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    • 1977
  • Using barley seeds (Hordeum sativum Jess, var.), the influences of gibberellic acid (GA) and indole-3-acetic acid(IAA) on the amylase synthesis and that of the nucleic acid metabolism were investigated. 1. With the deembrynized barley seeds, the increase of amylase treated with a $10^{-5}M$ of GA and the decrease of amylase treated with $10^{-5}M$IAA were matched by a proportionate increase and decrease in the amount of RNA. The influence of the hormones on the RNA synthesis has appeared immediately after the treatment but on the amylase synthesis it has appeared 8 hours later. But no influence on the DNA synthesis was observed on both hormones. 2. The amylase from deembryonized barley seeds treated with GA and IAA have been fractionated by gel filteration on Sephadex G-100. The amylase components showed four fractions on both enzymes treated with GA and IAA. Fraction I(FI) was differed from fraction Ⅵ(FIV) in Km value and the effects of temperature, pH and metal ions. On the basis of their emzymatic properties, it was considered that the FI was $\beta$-amylase and FIV was $\alpha$-amylase. The influences of GA and IAA on each fractions appeared to be similar but on the amylase units per souble protein, IAA inhibited the production of amylase FIV while it promoted that of amylase FI. 3. An experiment was conducted to determine whether IAA inhibits GA-promoted amylase synthesis competitively or non-competitively. Using a Lineweaver-Burk plot, it was clear that IAA was acting in a non-competitive fashion. From this, IAA was probably not competing with GA at the same site, but it was acting at some other site which resutled in partial blocking of the action of GA on the amylase synthesis.

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Hypoglycemic and Angiotension Converting Enzyme Inhibitory Effect of Water and Ethanol Extracts from Haesongi Mushroom (Hypsizigus marmoreus)

  • Jung, Eun-Bong;Jo, Jin-Ho;Cho, Seung-Mock
    • Food Science and Biotechnology
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    • 제18권2호
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    • pp.541-545
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    • 2009
  • Water and ethanol extracts were prepared from the haesongi mushroom (Hypsizigus marmoreus) to measure functional components. The ability of the extracts to inhibit angiotensin-converting enzyme (ACE) and their hypoglycemic effects were also determined; the latter was measured by $\alpha$-amylase and glucosidase inhibition. Extraction yield, protein content, total phenol, and $\beta$-glucan in the water extracts were 55.86, 17.71, 1.89, and 21.93%, respectively. The respective values for the ethanol extracts were lower than those for water extracts. Both water and ethanol extracts showed dosedependent ACE inhibition, the effect of the former being greater. The water extract inhibited ACE activity by 95.34% at 40 mg/mL. The $IC_{50}$ values of the water extracts were 63.32 and 0.41 mg/mL for $\alpha$-amylase and glucosidase, respectively. Thus, the water extracts had a greater hypoglycemic effect than the ethanol extracts. From these results, water is a better solvent than ethanol to extract from the haesongi mushroom functional components that show ACE inhibition and have hypoglycemic effects.

Enzyme Activities of the Fruit Body of Ramaria botrytis DGUM 29001

  • Lee, Tae-Hee;Han, Yeong-Hwan
    • Mycobiology
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    • 제29권3호
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    • pp.173-175
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    • 2001
  • The fruit body of Ramaria botrytis DGUM 29001 was used to determine enzyme activities of fruit body. The specific activity of laccase was the highest(6.5 unit/mg$\cdot$protein) and that of $\alpha$-amylase and xylanase was relatively high. However, little or no enzyme activity of $\beta$-glucosidase, CMCase, exo-$\beta$-1,4-glucanase, chitinase, lipase and protease was found.

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송이균사(Tricholoma matsutake) 배양액의 세포외 효소 활성 (The Extracellular Enzyme Activities in Culture Broth of Tricholoma matsutake)

  • 이창윤;홍운표;정명준;한영환
    • 한국균학회지
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    • 제26권4호통권87호
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    • pp.496-501
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    • 1998
  • 송이균사(Tricholoma matsutake DGUM 26001, DGUM 26101, DGUM 26210, FRI 91024)를 사용하여 균사의 효소활성을 측정하였다. $24^{\circ}C$에서 30일간 배양후 그 여액을 조효소 용액으로 사용하였을 때, ${\alpha}-amylase$ 효소의 평균 비활성은 6142.3 unit/mg protein이었다. 배양여액 중의 xylanase의 세포의 효소활성은 상대적으로 높았으나, ${\beta}-glucosidase$, ligninase, CMCase, chitinase, pretense및 lipase의 효소활성은 낮거나 거의 없었다.

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팽윤 Extrusion 전분을 기질로 한 불균일상 효소반응계에서의 Maltose 생성 반응 특성 (Characteristics of Maltose Formation in Heterogeneous Enzyme Reaction System Utilizing Swollen Extrusion Starch as a Substrate)

  • 김동선;박동찬;조명진;이용현
    • 한국미생물·생명공학회지
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    • 제22권3호
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    • pp.283-289
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    • 1994
  • The production of maltose utilizing swollen extrusion starch seems to have many technical advantages, such as, high reaction rate and high yield, production of high purity concentrated maltose, and low energy consumption, over the conventional method utilizing liquefied starch. The characteristics of maltose formation in heterogeneous enzyme reaction system comtaining swollen extrusion starch was investigated using fungal $\alpha $-amylase. The influence of extrusion conditions on structure of extruded starch, such as, degree of gelatinization, water absorption index, and water solubility index was analyzed. The relationship between the structural features and maltose forming reaction was investigated, and the result was analyzed in terms of surface reaction of insoluble extruded swollen starch. The characteristics of maltose formation from swollen sxtrusion starch was compared using endo-type fungal $\alpha $-amylase and exo-type $\beta $anylase, and the structural trasformation of extruded starch was also observed to clarify the reaction mechanism.

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인삼백 첨가가 알콜발효용균의효소생성에 미치는 영향 (Effect of Red Ginseng Residue on Various Enzyme Production of Alcohol Fermentation Koji)

  • 김상달;도재호;이종철
    • Journal of Ginseng Research
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    • 제6권2호
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    • pp.131-137
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    • 1982
  • The effect of red ginseng residue on the several enzyme activities of the koji and alcohol fermentation were investigated. The koji showed maximum values of amylase and cellulase activity when it was prepared by 30% red ginseng residue and 70% wheat bran, and of protease activity when it was prepared by 40% red ginseng residue and 60% wheat bran-${\alpha}$ amylase activity of the koji during its fermentation was increased rapidly until 4 days and there after it was increased slowly, but ${\beta}$-amylase was rapidly increased after 3 days fermentation. During the preparation of the koji, the acidic, neutral protease and cellulase activities showed the maximum value after 3 days fermentation and the alkaline protease showed the maximum value within 4-6 days fermentation. On the otherhand, fermented broth, containing 6%(v/v) alcohol, could be obtained when the substrate was saccharified by the koji, based on 25% red ginseng residue and 75% wheat bran, prior to alcohol fermentation.

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재배상황버섯의 장내 세균 유해효소 및 알파글루코시다제 저해효과 (Effect of Artificially Cultured Phellinus linteus on Harmful Intestinal Bacterial Enzymes and Rat Intestinal ${\alpha}-glucosidases$)

  • 김동현;최혁재;배은아;한명주;박순영
    • 한국식품위생안전성학회지
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    • 제13권1호
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    • pp.20-23
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    • 1998
  • 재배 상황버섯의 유산균 증식 효과를 측정한 결과 B. breve에 대한 증식 효과와 배양배지의 pHwj하 효과가 우수했다. 사람 및 흰주의 장내 세균을 버섯추출물 함유 배니에서 배양시 배지의 pH저하 효과가 우수할뿐만아니라 ${\beta}-glucosidase$의 효소 활성을 억제하였다. 그외에도 대장암 및 방광암 등의 원이효소로 주목되고 있는 사람 및 흰쥐의 장내 세균총 효소인 ${\beta}-glucosidases$ 및 tryptophanase 효소 활성을 억제하였다. 이외에도 인슐린 비의존형 당뇨병의 치료제로 사용되는 acarbose보다는 약하지만 maltase, sucrase 및 알파아밀라제를 효과적으로 저해하였다.

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Purification, Characterization, and Partial Primary Sequence of a Major-Maltotriose-producing $\alpha$-Amylase, ScAmy43, from Sclerotinia sclerotiorum

  • Ben Abdelmalek-Khedher, Imen;Urdad, Maria Camino;Limam, Ferid;Schmitter, Jean Marie;Marzouki, M. Nejib;Bressollier, Philippe
    • Journal of Microbiology and Biotechnology
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    • 제18권9호
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    • pp.1555-1563
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    • 2008
  • A novel $\alpha$-amylase ($\alpha$-1,4-$\alpha$-D-glucan glucanohydrolase, E.C. 3.2.1.1), ScAmy43, was found in the culture medium of the phytopathogenic fungus Sclerotinia sclerotiorum grown on oats flour. Purified to homogeneity, ScAmy43 appeared as a 43 kDa monomeric enzyme, as estimated by SDS-PAGE and Superdex 75 gel filtration. The MALDI peptide mass fingerprint of ScAmy43 tryptic digest as well as internal sequence analyses indicate that the enzyme has an original primary structure when compared with other fungal a-amylases. However, the sequence of the 12 N-terminal residues is homologous with those of Aspergillus awamori and Aspergillus kawachii amylases, suggesting that the new enzyme belongs to the same GH13 glycosyl hydrolase family. Assayed with soluble starch as substrate, this enzyme displayed optimal activity at pH 4 and $55^{\circ}C$ with an apparent $K_m$ value of 1.66 mg/ml and $V_{max}$ of 0.1${\mu}mol$glucose $min^{-1}$ $ml^{-1}$. ScAmy43 activity was strongly inhibited by $Cu^{2+}$, $Mn^{2+}$, and $Ba^{2+}$, moderately by $Fe^{2+}$, and was only weakly affected by $Ca^{2+}$ addition. However, since EDTA and EGTA did not inhibit ScAmy43 activity, this enzyme is probably not a metalloprotein. DTT and $\beta$-mercaptoethanol strongly increased the enzyme activity. Starting with soluble starch as substrate, the end products were mainly maltotriose, suggesting for this enzyme an endo action.