• Title/Summary/Keyword: Thermal Inactivation

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Application of Saccharomyces rouxii for the Production of Non-alcoholic Beer

  • Sohrabvandi, Sarah;Razavi, Seyed Hadi;Mousavi, Seyed Mohammad;Mortazavian, Amir;Rezaei, Karamathollah
    • Food Science and Biotechnology
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    • v.18 no.5
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    • pp.1132-1137
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    • 2009
  • Successive application of Saccharomyces cerevisiae DSM 70424 and Saccharomyces rouxii DSM 2535 or DSM 2531 in the production of non-alcoholic beer was investigated. The aim of the study was to consider the impact of the 2 mentioned strains of S. rouxii on the reduction of alcohol content in wort fermented at 12 or $24^{\circ}C$ for 96 hr, applying periodic aeration. The 2 S. rouxii strains were added at the $48^{th}$ hr of fermentation after thermal inactivation of S. cerevisiae cells. The greatest alcohol decrease rate was observed for the treatment containing S. rouxii DSM 2535-fermented at $24^{\circ}C$ (from 1.56 to 0.36%). The concentration of acetaldehyde, diacetyl, and 2,3-pentandione, that have a key role in appearance of 'wort' and 'buttery' off flavors, were significantly lower in S. rouxii-containing treatments fermented at $24^{\circ}C$. S. rouxii-containing treatment fermented at $24^{\circ}C$ showed slightly lower overall flavor acceptability compared to S. cerevisiae-containing treatment fermented at the same temperature. Such score was improved for the products obtained at $12^{\circ}C$.

Separation and Characterization of Endo-Polygalacturonase from Aspergillus niger (Aspergillus niger가 생산(生産)하는 Endo-Polygalacturonase의 분리(分離)와 특성(特性))

  • Park, Kyong-Bin;Park, Kwan-Hwa
    • Korean Journal of Food Science and Technology
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    • v.16 no.1
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    • pp.41-46
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    • 1984
  • The pectic enzymes produced from Aspergillus niger were separated into three fractions (F-A, F-I and F-II) by means of Sephadex and DEAF-Sephadex column chromatography. Each enzyme fraction was characterized by determining viscosity change and reducing surgar of the pectic acid-enzyme mixture and analyzing thin layer chromatogram of the reaction products. F-I rapidly reduced the viscosity of pectic acid solution and released reducing groups in a random manner so that appeared to be an endo-polygalacturonase (endo-PG). The optimum pH of endo-PG for viscosity reducing activity was 4.2 and that for releasing reducing surgar was 4.7. In the thermal inactivation of endo-PG of $30-45^{\circ}C$, the enthalpy of activation was 217.3 kj/mole and z-value was $7.5^{\circ}C$. F-II and F-A were determined as endo-polymethylgalacturonase and exo-polygalacturonase, respectively.

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Amplicilin biosynthesis by immobilized enzyme

  • Kim, Young-Sik;Ryu, Dewy-D.Y.
    • Archives of Pharmacal Research
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    • v.3 no.1
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    • pp.7-12
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    • 1980
  • Ampliciline was synthesized from 6-amino-pencillanic acid (6-APA) and D-.alpha. phenylglycine methyl ester by using amplicilin synthesizing enzyme from Peudomonas melanogenum (IAM 1655). The whole cell enzyme was immobilized by entrapping it in the polyacrylamide gel lattices. The polymer used in the enzyme entrapment was made from 150 mg per ml of acrylamide monomer and 8 mg per ml of N, N'-methylenebisacrylamide. About 200 mg/whole cell enzyme was mixed in the polymer for entrapment. The maximal activity retention after immobilization was 56%. The optimal pH values for the whole cell enzyme and the immobilized whole cell enzyme were 6.0 and 5.9, respectively. The optimal temperature for the enzyme activity were the same for both type of preparations. The enzyme stabilities against pH and heat increased for immobilized whole cell enzyme. Immobilized cell was more stable especially in the acidic condition while both type were found to be very suceptible to thermal inactivation at a temperature above 4.deg.C. The kinetic constants obtained from Lineweaver-Burk plot based on two substate reaction mechanism showed somewhat higher value for immobilized whole cell enzyme as compared to the whole cell enzyme : the Km value for 6-APA were 7.0 mM and 12.5 mM while Km values for phenylglycine methyl ester were 4.5 mM and 8.2 mM, respectively. Using the immobilized whole cell enzyme packed in a column reactor, the productivity of ampiciline was studied by varying the flow rate of substrate solution. At the space velocity, SV, 0.14 hr$^{-1}$ the conversion was 45%. Operational stability found in terms of half life was 30 hr at SV = 0.2 hr.

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Characteristics and Action Pattern of Alkaline Protease produced from Aspergillus fumigatus (Aspergillus fumigatus이 생산하는 Alkaline protease의 특성과 작용양상)

  • Cha, Woen-Suep;Choi, Cheong
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.18 no.3
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    • pp.348-355
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    • 1989
  • This experiment was conducted to investigate the characteristics of alkaline protease from Aspergillus fumigatus which was isolated from soil as a superior strain for the production of the alkaline protease. The optimum temperature for enzyme activity was $50^{\circ}C$ and optimum pH was 9.0. The enzyme was stable at pH 8.0 to 10.0 and thermal inactivation was shown $30^{\circ}C$. The activity of the enzyme was increased by the addition of $Mn^{++},\;Cu^{++},\;Ba^{++},\;Mg^{++},\;$wheras it was inhibitied by $K^+,\;Fe^{+++},\;Ag^+,\;Pb^{++},\;Na^+,\;Ca^{++},\;Hg^+,\;Zn^{++}$. EDTA. 2, 4-DNP, ${\varepsilon}-amino$ caproic acid did not show inhibitory effect on the proteolytic activity of alkaline protease but P-chloromercuribenzoic acid inhibited the enzyme activity, indicating that reactive sulfhydryl group is required for the enzymatic activity. The reaction of this enzyme followed typical Michael-Menten Kinetics with the Km value of $8.33{\times}10^{-4}mole/{\ell}$ with the Vmax of $47.62{\mu}g/min$. This enzyme had stronger proteolytic activity than trypsin on substrate such as casin and hemoglibin.

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The Biochemical Characterization of D-Hydroxyisovalerate Dehydrogenase, a Key Enzyme in the Biosynthesis of Enniatins

  • Lee, Chan; Zocher, Rainer
    • BMB Reports
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    • v.29 no.6
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    • pp.493-499
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    • 1996
  • The biochemical properties of purified D-hydruxyisovalerate dehydrogenase from Fusarium sambucinum was elucidated. D-Hydroxyisovalerate dehydrogenase produced solely D-hydroxyisovalerate from 2-ketoisovalerate. The isoelectric point of the purified enzyme was 7.0. The enzyme was highly specific with 2-ketoisovalerate ($K_{m}=0.188$ mM, $V_{max}=8.814$ mmol/min mg) and 2-keto-3-methyl-n-valerate ($K_{m}=0.4$ mM, $V_{max}=1.851$ mmol/min mg) for the reductive reaction. This was also seen by comparing D-hydroxyisovalerate ($K_{m}=1.667$ mM, $V_{max}=0.407$ mmol/min mg) and D-hydroxy-3-methyl-n-valerate ($K_{m}=6.7$ mM, $V_{max}=0.648$ mmol/min mg) for the oxidative reaction. Thiol blocking reagents, such as iodoacetamide, N-ethylmaleimide and p-chloromecuribenzoate inhibited about 80% of enzyme activity at 0.02 mM, 50 mM and 50 mM, respectively. The enzyme activity was also inhibited by the addition of 0.1 mM of various metal ions, such as $Fe^{2+}$ (67%), $Cu^{2+}$ (88%), $Zn^{2+}$ t (76%) and $Mg^{2+}$ (9%). The enzyme was stable over three months in 50 mM potassium phosphate buffer (pH 5~7) at $-80^{\circ}C$. However the purified enzyme lost 30% of its activity in the same buffer after 24 h at $4^{\circ}C$. The studies about thermal inactivation of D-hydroxyisovalerate dehydrogenase exhibit 209.2 kJ/M of activation enthalpy and 0.35 kJ/mol K of activation entropy.

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Hydrolysis of Cellulose by Immobilized Cellulase in a Packed Bed Reactor (충진층 반응기에서 고정화 cellulase에 의한 셀룰로스 가수 분해)

  • Kang, Byung Chul;Lee, Jong Baek
    • Journal of Life Science
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    • v.23 no.11
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    • pp.1365-1370
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    • 2013
  • Immobilized cellulase on weak ion exchange resin showed a typical Langmuir adsorption isotherm. Immobilized cellulase had better stability with respect to pH and temperature than free cellulase. Kinetics of thermal inactivation on free and immobilized cellulase followed first order rate, and immobilized cellulase had a longer half-life than free cellulase. The initial rate method was used to characterize the kinetic parameters of free and immobilized enzyme. The Michaelis-Menten constant $K_m$ was higher for the immobilized enzyme than it was for the free enzyme. The effect of the recirculation rate on cellulose degradation was studied in a recycling packed-bed reactor. In a continuous packed-bed reactor, the increasing flow rate of cellulose decreased the conversion efficiency of cellulose at different input lactose concentrations. Continuous operation for five days was conducted to investigate the stability of long term operation. The retained activity of the immobilized enzymes was 48% after seven days of operation.

Inactivation of Human Norovirus GII. 4 on Oyster Crassostrea gigas by Electron Beam Irradiation (전자선 조사에 의한 신선굴(Crassostrea gigas) 중 휴먼노로바이러스 GII. 4의 저감화)

  • Kim, Ji Yoon;Jeon, Eun Bi;Choi, Man-Seok;Park, Shin Young
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.54 no.1
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    • pp.16-22
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    • 2021
  • This study investigated the reduction in human norovirus (HNV) GII. 4 count in pacific oyster Crassostrea gigas using electron beam irradiation. Infectious HNV GII. 4 was detected using RT-qPCR (real time reverse transcription-quantitative polymerase chain reaction) with PMA (propidium monoazide)/sarkosyl. At electron beam doses 1, 5, 7, and 10 kGy, the count of HNV GII. 4 was 2.74, 2.37, 2.06, and 1.55 log copies/μL (control, 3.01 log copy/μL), respectively, confirming that as the irradiation dose increased, norovirus count reduced significantly (P<0.05). After PMA/sarkosyl treatment, the counts further reduced at the same irradiation dose, and 10 kGy showed significant differences between the non-treated and PMA/sarkosyl-treated samples (P<0.05). The Ed (decimal reduction dose of electron beam) value based on the first-order kinetic model was 7.33 kGy (R2=0.98). No significant difference was observed in the pH values of the control (6.2) and electron beam-irradiated samples at all doses (6.1). For sensory evaluation, the non-treated sample scored the highest in all categories (5.25-6.17), while the samples treated with 10 kGy showed the lowest score (4.67-5.33), although without statistical significance (P>0.05). Overall, our results suggest that 7 kGy electron beam is sufficient for the non-thermal sterilization of oysters without causing significant changes in quality.

Anti-inflammatory and Anti-nociceptive Effects of Ethyl Acetate Fraction of Lindera glauca (감태나무 에틸아세테이트 분획의 항염증 및 진통 효과)

  • Kim, Jong Soo;Kang, Bo Hye;Park, Seung Ju;Yang, Woo In;Kim, Myung Soo;Lee, Byung Soo;Cha, Dong Seok;Lee, Se Youn;Kwon, Jin;Jeon, Hoon
    • Korean Journal of Pharmacognosy
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    • v.53 no.1
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    • pp.49-56
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    • 2022
  • The present study was designed to evaluate the anti-inflammatory and anti-nociceptive potential of the ethyl acetate fraction of Lindera glauca (ELG). We found that ELG significantly suppressed NO production through decreased enzyme activity and expression of iNOS in the IFN-γ/LPS-activated murine peritoneal macrophages. The treatment of ELG also down-regulated the expression of COX-2. Our western blot data revealed that inhibitory effects of ELG on these pro-inflammatory mediators were attributed to inactivation of NF-κB. In addition, ELG-fed mice showed a marked decrease in paw edema induced by subplantar injection of trypsin, suggesting in vivo anti-inflammatory potential of ELG. We further investigated the anti-nociceptive properties of ELG using thermal and chemical nociception model. We found that ELG has a strong anti-nociceptive activities in both central and peripheral mechanism. An additional combination test with naloxone revealed that opioid receptor was not involved in the ELG-mediated anti-nociception. In conclusion, ELG may possibly be used as valuable anti-inflammatory and anti-nociceptive agent for the treatment of inflammatory diseases and pains.

Studies on the Production of Enzymes by Thermophilic Actinomycetes (PART II) Some Properties of $\alpha$-Amylase from Thermophilic Actinomycetes (고온성 방선균에 의한 순소생산에 관한 연구 (제2보) $\alpha$-Amylase의 효소학적 성질)

  • Yang, Han-Chul;Park, Yong-Jin;Cho, Hong-Yeon
    • Microbiology and Biotechnology Letters
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    • v.4 no.3
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    • pp.91-97
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    • 1976
  • During the course of studies on the production and utilization of thermostable ${\alpha}$-amylase from a thormophilic actinomycete species isolated from soil, partial characterization of the ${\alpha}$-amylase has been (arried out. The optimum pH for the dextrinogenic activity of the enzyme was found to be 6.5 and the maximum reaction rate was achieved at a temperature range of 55$^{\circ}$ to 65$^{\circ}C$. Calcium ion was recognized to have a slight effect in activating the enzyme, while heavy metal salts especially ferrous and cupric ions showed a remarkable inhibition effect. The enzyme was best protected iron thermal denaturation at pH 8.0 with tris-HCI buffer;inactivation was rapid at higher or lower pH values. Furthermore, its thermal stability was greatly increased by calcium ion, particulary at the final concentration of 1${\times}$10$\^$-2/ mole in the reaction mixture. The Km value for the ${\alpha}$-amylase was calculated to be 2.17${\times}$10$\^$-4/g per $m\ell$ and the energy of activation for the dextrinogenic reaction to be 12,000${\pm}$580 ㎈ per mole.

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Effect of Supercritical Carbon Dioxide Treatment on Quality of Citrus juice (초임계 이산화탄소 처리가 감귤쥬스 품질에 미치는 영향)

  • Jwa, Mi-Kyung;Lim, Sang-Bin;Yang, Young-Tack;Koh, Jeong-Sam
    • Korean Journal of Food Science and Technology
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    • v.28 no.4
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    • pp.750-755
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    • 1996
  • Citrus juice was treated with supercritical carbon dioxide $(SC-CO_{2})$ and the effect of temperature and pressure on quality of citrus juice was determined. Pectinesterase (PE) was inactivated by $(SC-CO_{2})$ below temperatures necessary for thermal inactivation. There was no significant change in the pH, Brix and total acidity of citrus juice before and after $(SC-CO_{2})$ treatment, but brightness was improved. More ascorbic acid was retained during $(SC-CO_{2})$ treatment of citrus juice than thermal treatment $(93^{\circ}C/0.66\;min)$.During storage of supercritically treated citrus juice at $4^{\circ}C$, activity of PE was reversible. Sensory evaluation showed that color, flavor, taste and overall acceptance of $(SC-CO_{2})$ treated juice were not significantly different from untreated juice. This method offers potentially beneficial processing avenues for citrus juice and other juices, especially in the area of minimally processed products.

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