• Title/Summary/Keyword: a-amylase activity

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Screening of Biological Activities in Fern Plants Native to Jeju Island (제주도에 자생하는 양치식물의 생리활성 검색)

  • Oh, Soon-Ja;Hong, Sung-Soo;Kim, Yeon-Hee;Koh, Seok-Chan
    • Korean Journal of Plant Resources
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    • v.21 no.1
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    • pp.12-18
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    • 2008
  • Antioxidative activity and inhibitory activity of angiotensin I converting enzyme(ACE), aminopeptidase N(APN) and $\alpha$-amylase were investigated in the methanol extracts from 25 fern plants native to Jeju Island, in order to screen the plant species containing bioactive materials for functional foods or medicines. The antioxidative activity was higher in Cytomium fortunei(41.9%) and Rumohra standishii(34.1%) than in leaves of Thea sinensis(30.9%), a small tree for antioxidative beverage. Inhibitory activities of ACE and APN were relatively high in Cytomium fortunei as 26.7% and 28.2% respectively. $\alpha$-Amylase inhibitory activity was higher than 50% in 10 species. Particularly, Cytomium fortunei(87.4%) and Dryopteris erythrosora(71.6%) showed the inhibitory activities higher than those of other form plants. Of 25 fern plants investigated here, Cytomium fortunei showed not only the highest antioxidative activity but also the highest inhibitory activity of ACE, APN and $\alpha$-amylase. It suggests that Cytomium fortunei could be potentially used as a resource of bioactive materials for fuctional foods or medicines.

Studies on Improved Amylases Developed by Protoplast Fusion of Aspergillus species

  • Adeleye, Tolulope Modupe;Kareem, Sharafadeen Olateju;Olufunmilayo, Bankole Mobolaji;Atanda, Olusegun;Osho, Michael Bamitale;Dairo, Olawale
    • Microbiology and Biotechnology Letters
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    • v.49 no.1
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    • pp.45-56
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    • 2021
  • Improved amylases were developed from protoplast fusants of two amylase-producing Aspergillus species. Twenty regenerated fusants were screened for amylase production using Remazol Brilliant Blue agar. Crude enzyme extracts produced by solid state fermentation of rice bran were assayed for activity. Three variable factors (temperature, pH and enzyme type) were optimized to increase the amylase activity of the parents and selected fusants using rice bran medium and solid state fermentation. Analysis of this optimization was completed using the Central Composite Design (CCD) of the Response Surface Methodology (RSM). Amylase activity assays conducted at room temperature and 80℃ demonstrated that Aspergillus designates, T5 (920.21 U/ml, 966.67 U/ml), T13 (430 U/ml, 1011.11 U/ml) and T14 (500.63 U/ml, 1012.00 U/ml) all exhibited improved function making them the preferred fusants. Amylases produced from these fusants were observed to be active over the entire pH range evaluated in this study. Fusants T5 and T14 demonstrated optimal activity under acidic and alkaline conditions, respectively. Fusants T13 and T14 produced the most amylase at 72 h while parents TA, TC and fusant T5 produced the most amylase after 96 h of incubation. Response surface methodology examinations revealed that the enzyme from fusant T5 was the optimal enzyme demonstrating the highest activity (1055.17 U/ml) at pH 4 and a temperature of 40℃. This enzyme lost activity with further increases in temperature. Starch hydrolysis using fusant T5 gave the highest yield of glucose (1.6158 g/100 ml). The significant activities of the selected fusants at 28 ± 2℃ and 80℃ and the higher sugar yields from cassava starch hydrolysis over their parental strains indicate that it is possible to improve amylase activity using the protoplast fusion technique.

A study on dextrinogenic amylase in the aspergillus niger group (Aspergillus niger group의 dextrinogenic amylase에 관한 연구)

  • 김상재;이배함;이용욱
    • Korean Journal of Microbiology
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    • v.9 no.4
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    • pp.155-162
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    • 1971
  • A comparison of dextrinogenic amylase activities in the Asp. niger group was made with their crude and ethanol dialized enzymes before and after heating at high temperature (60-$65^{\circ}C$). The results obtained are as follows ; 1. THe dextrinogenic amylase activity of crude enzymes of Asp. kawachii and Asp. foetidus was strong, but Asp. phoernicis, Asp. carbonarius and Asp.japonicus showed weak activity. The others showed medial grades of activity. 2. The ethanol dialized enzymes of Asp. kawachii, Asp. foetidus and Asp. japonicus was very sesitive to high temperature (60 or $65^{\circ}C$) and their enzymatic activities were diminished greatly. The others did not show diminution of enzymatic activity at 60 or 65.deg.C, but diminished greatly at 70 or $75^{\circ}C$. 3. The ethanol dialized enzymes of the Asp.niger group heated to 65.deg.C was more sensitive at pH 6.0 and 6.5 than at pH 4.5, 5.0 and 5.5. 4. Tested strains in the Asp.niger group were subdivided into 4 subgroups by their dextrinogenic amylase activities before and after heating at 60 or $65^{\circ}C$. The first group showed a medial grade of activity before heating and no diminution of their enzymatic activities after heating. Asp. niger, Asp.pulverulentus, Asp. awamori and Asp. usmii were included in this group. The second group had strong enzymatic activity before heating, but diminished greatly after heating. Asp rawachii and Asp. phoenicis were included in this group. The fourth group showed very weak enzymatic activity before heating, and was inactivated easily by heating. Asp.oryzae of the Asp. flavus group showed a very strong dextrinogenic amylase activity before heating. After the heat treatment, however, its enzymatic activity was diminished greatly.

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Immobilization of α-amylase from Exiguobacterium sp. DAU5 on Chitosan and Chitosan-carbon Bead: Its Properties

  • Fang, Shujun;Chang, Jie;Lee, Yong-Suk;Hwang, Eun-Jung;Heo, Jae Bok;Choi, Yong-Lark
    • Journal of Applied Biological Chemistry
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    • v.59 no.1
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    • pp.75-81
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    • 2016
  • Glutaraldehyde was used as a cross-linking agent for immobilization of purified ${\alpha}$-amylase from Exiguobacterium sp. DAU5. Befitting concentration of glutaradehyde and cross-linking time is the key to preparation of cross-linking chitosan beads. Based on optimized immobilization condition for ${\alpha}$-amylase, an overall yield of 56% with specific activity of 2,240 U/g on chitosan beads and 58% with specific activity of 2,320 U/g on chitosan-carbon beads was obtained. The optimal temperature and pH of each immobilized enzyme activity were $50^{\circ}C$ and 50 mM glycine-NaOH buffer pH 8.5, respectively. Those retained more than 75 and 90% of its maximal enzyme activity at pH 7.0-9.5 and after incubation at $50^{\circ}C$ for 1 h, respectively. In addition, the immobilization product showed higher organic-solvent tolerance than free enzymes. The mode of hydrolyzing soluble starch revealed that the ${\alpha}$-amylase possessed high hydrolyzing activity. These results indicate that chitosan is good support and has broad application prospects of enzyme immobilization.

Identification and Characterization of Useful Fungi with ${\alpha}$-Amylase Activity from the Korean Traditional Nuruk

  • Kim, Hye-Ryun;Kim, Jae-Ho;Bai, Dong-Hoon;Ahn, Byung-Hak
    • Mycobiology
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    • v.39 no.4
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    • pp.278-282
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    • 2011
  • The objective of this study was to find useful fungi with ${\alpha}$-amylase activity from the Korean traditional nuruk for the quality of traditional Korean alcoholic beverage. In this study, 165 samples of traditional nuruk were collected from 170 regions throughout Korea and the fungi were isolated to a total of 384 strains. In order to investigate the effect of microflora on nuruk, ${\alpha}$-amylase activity, saccharogenic power (SP), starch hydrolysis activity and acid producing activity were evaluated. Ten strains were selected by ${\alpha}$-amylase activity, which ranged from 458.47 to 1,202.75 U/g. The size of the discolored zone for the starch hydrolysis activity of each fungus ranged from 0.3 to 2 cm. The SP of the 10 strains ranged from 228.8 to 433.4 SP. Of the 10 stains, three were identified as Aspergillus oryzae, two as Aspergillus flavus, two as Lichtheimia sp., one as Rhizopus oryzae and two as other strains. The total aflatoxins present in the nuruks were examined using enzyme-linked immunosorbent assay. The 10 nuruks had less than 1.11 ppb of aflatoxins.

Total Sugars, $\alpha$-amylase Activity, and Germination after Priming of Normal and Aged Rice Seeds

  • Lee, Suk-Soon;Kim, Jae-Hyeun
    • KOREAN JOURNAL OF CROP SCIENCE
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    • v.45 no.2
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    • pp.108-111
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    • 2000
  • Osmoconditioning and hardening effects for the seed germination of normal and naturally aged rice seeds were studied through analyzing the total sugars and $\alpha$-amylase activity. The normal seeds which used to have high germination rate accelerated germination with the osmoconditioning at the suboptimal temperature of 17$^{\circ}C$. On the other hand, the aged seeds did not affect germination rate at $25^{\circ}C$, while increased germination rate and accelerated germination a little at 17$^{\circ}C$, Hardening of aged seeds increased germination rate by 10-15% compared with control seeds at both 17 and $25^{\circ}C$ and accelerated germination. Total sugar content and $\alpha$-amylase activity of normal seeds were higher than did aged seeds. The aged seeds with treatment of osmoconditioning and hardening increased total sugar content and $\alpha$--amylase activity, but hardening was more effective than osmoconditioning. The $\alpha$--amylase activity was positively correlated with the total sugar content and germination rate.

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In Vitro α-Amylase, α-Glucosidase, Pancreatic Lipase, Xanthine Oxidase Inhibiting Activity of Agaricus bisporus Extracts

  • Jung Han Kim;Myoung Jun Jang;Youn Jin Park
    • Mycobiology
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    • v.51 no.1
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    • pp.60-66
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    • 2023
  • In this study, the α-amylase inhibitory activity, α-glucosidase inhibitory activity, pancreatic lipase inhibitory activity, and Xanthine Oxidase inhibitory activity of the fruiting body extracts of 5 varieties of Agaricus bisporus (AB) were confirmed. First, the α-amylase inhibitory activity of AB12, AB13, AB18, AB34, and AB40 methanol extracts was lower than that of acarbose, a positive control, in all concentration ranges. The α-glucosidase inhibitory activity of the AB40, AB13, and AB12 methanol extracts at the extract concentration of 1.0 mg/mL was 80.5%, 81.3%, and 78.5%, respectively, similar to that of acarbose, a positive control. The pancreatic lipase inhibitory activity of the methanol extract of Agaricus bisporus fruiting body was significantly lower than that of the positive control orlistat in the concentration range of 50~1.000 (mg/mL). The Xanthine Oxidase inhibitory activity was 0.5~8.0 mg/mL of each extract, which was significantly lower than that of the positive control allopurinol in the same concentration range. However, the Xanthine Oxidase inhibitory activity of AB13 and AB40 at 8.0 mg/mL was about 70%, which was higher than that of other mushrooms. In conclusion, five kinds of Agaricus bisporus fruiting bodies seem to have inhibitory effects on enzymes such as α-amylase, α-glucosidase, pancreatic lipase, and Xanthine Oxidase that degrade starch and protein. In particular, it has an inhibitory effect and a reduction effect on xanthine oxidase that causes gout, so it is expected that it can be developed and used as a food or health supplement with health functional properties through future research.

Inhibitory Effects of Ginseng Seed Oil on α-Glucosidase and α-Amylase Activity (인삼종자오일의 α-Glucosidase 및 α-Amylase 저해작용)

  • Ahn, Chang Ho;Nam, Yun Min;Kim, Shin Jung;Yang, Byung Wook;Kim, Hyoung Chun;Ko, Sung Kwon
    • Korean Journal of Pharmacognosy
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    • v.47 no.1
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    • pp.24-28
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    • 2016
  • This study was to evaluate the effect of ginseng (Panax ginseng) seed oil on the ${\alpha}$-glucosidase and ${\alpha}$-amylase. Each ginseng seed oils (HE, SE, EE) exhibited a significant inhibitory effect (p<0.001) at all concentrations (10 and 20 mg/ml) on ${\alpha}$-glucosidase activity. HE is the highest inhibitory activity (86.92%) at a concentration of 20 mg/ml, SE and EE showed an inhibitory effect of 77.13% and 65.83%, respectively. And also, Each ginseng seed oils (HE, SE, EE) exhibited a significant inhibitory effect (p<0.001) at all concentrations (1 and 2 mg/ml) on ${\alpha}$-amylase activity. HE is the highest inhibitory activity (89.68%) at a concentration of 2 mg/ml, SE and EE showed an inhibitory effect of 76.99% and 65.70%, respectively.

Gene Cloning and Characterization of an ${\alpha}$-Amylase from Alteromonas macleodii B7 for Enteromorpha Polysaccharide Degradation

  • Han, Xuefeng;Lin, Bokun;Ru, Ganji;Zhang, Zhibiao;Liu, Yan;Hu, Zhong
    • Journal of Microbiology and Biotechnology
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    • v.24 no.2
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    • pp.254-263
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    • 2014
  • Enteromorpha polysaccharides (EP) extracted from green algae have displayed a wide variety of biological activities. However, their high molecular weight leads to a high viscosity and low solubility, and therefore, greatly restrains their application. To solve this problem, bacteria from the surface of Enteromorpha were screened, and an Alteromonas macleodii strain B7 was found to be able to decrease the molecular weight of EP in culture media. Proteins harvested from the supernatant of the A. macleodii B7 culture were subjected to native gel electrophoresis, and a band corresponding to the Enteromorpha polysaccharide lyase (EPL) was detected by activity staining. The enzyme identity was subsequently confirmed by MALDI-TOF/TOF mass spectrometry as the putative ${\alpha}$-amylase reported in A. macleodii ATCC 27126. The amylase gene (amySTU) from A. macleodii B7 was cloned into Escherichia coli, resulting in high-level expression of the recombinant enzyme with EP-degrading activity. AmySTU was found to be cold-adapted; however, its optimal enzyme activity was detected at $40^{\circ}C$. The ${\alpha}$-amylase was highly stable over a broad pH range (5.5-10) with the optimal pH at 7.5-8.0. The highest enzyme activity was detected when NaCl concentration was 2%, which dropped by 50% when the NaCl concentration was increased to 16%, showing an excellent nature of halotolerance. Furthermore, the amylase activity was not significantly affected by tested surfactants or the presence of some organic solvents. Therefore, the A. macleodii strain B7 and its ${\alpha}$-amylase can be useful in lowering EP molecular weight and in starch processing.

Inhibitory Effects of Proanthocyanidin Extracted from Distylium racemosum on ${\alpha}-Amylase$ and ${\alpha}-Glucosidase$ Activities (조록나무 Proanthocyanidin의 ${\alpha}-Amylase$${\alpha}-Glucosidase$에 대한 저해 효과)

  • Ahn, Jin-Kwon;Park, Young-Ki;Park, So-Young;Kim, Yong-Mu;Rhee, Hae-Ik;Lee, Wi-Young
    • Korean Journal of Pharmacognosy
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    • v.35 no.4 s.139
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    • pp.271-275
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    • 2004
  • Distylium racemosum Sieb. Et Zucc contains some compounds inhibit -amylase activity in experimental conditions. The inhibitory test showed that 50% acetone extracts from the bark and leaves of the plant strongly inhibited salivary -amylase activity. Proanthocyanidin(PA) which has strong inhibitory activity was extracted from the leaves by chromatography on Sephadex LH-20. The inhibitory activities and the inhibition kinetics of the PA were studied against three kinds of enzymes: human salivary ${\alpha}-Amylase$ (SAA), pork pancreatin ${\alpha}-Amylase$ (PAA) and yeast ${\alpha}-Glucosidase$ (AG). Then the activities of PA against SAA, PAA and AG were compared with those of acarbose, a commercial agent. The inhibitory activities of PA were stronger than those of acarbose. Inhibition kinetics of the PA showed competitive inhibition for SAA and PAA, and non competitive inhibition for GA.