• Title/Summary/Keyword: debittering

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Downstream Process for the Production of Yeast Extract Using Brewer's Yeast Cells

  • In Man-Jin;Kim Dong Chung;Chae Hee Jeong
    • Biotechnology and Bioprocess Engineering:BBE
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    • v.10 no.1
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    • pp.85-90
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    • 2005
  • A downstream process was developed for the production of yeast extract from brewer's yeast cells. Various downstream processing conditions including clarification, debittering, and the Maillard reaction were considered in the development of the process. This simple and economic clarification process used flocculating agents, specifically calcium chloride ($1\%$). After the clarification step, a Maillard reaction is initiated as a flavor-enhancing step. By investigating the effects of several operation parameters, including the type of sugar added, sugar dosage, glycine addition, and temperature, on the degree of browning (DB), giucose addition and reaction temperature were found to have significant effects on DB. A synthetic adsorption resin (HP20) was used for the debittering process, which induced a compositional change of the hydrophobic amino acids in the yeast hydrolysate, thereby reducing the bitter taste. The overall dry matter yield and protein yield for the entire process, including the downstream process proposed for the production of brewer's yeast extract were 50 and $50\%$, respectively.

Partial Purification and Characterization of Limonoate Dehydrogenase from Rhodococcus fascians for the Degradation of Limonin

  • Puri, Munish;Kaur, Lakhwinder;Marwaha, Satwinder-Singh
    • Journal of Microbiology and Biotechnology
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    • v.12 no.4
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    • pp.669-673
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    • 2002
  • An extracellular limonoate dehydrogenase was purified 10-fold from a cell-free extract of Rhodococcus fascians by ammonium sulfate precipitation, dialysis, and ultrafiltration. This purified dehydrogenase catalyzed the conversion of limonoate to 17-dehydrolimonoate. The enzyme showed optimum activity at pH 8.0 and $40^{\circ}C$, with $K_m$ value of 0.9$\muM$, and requires Zn ions and sulfhydryl groups for catalytic action. The enzyme activity was inhibited by $Hg^{2+}\;and\;NaN_3$ ions. The degradation of limonin (66%) in Kinnow mandarin juice was successfully demonstrated with partially purified limonoate dehydrogenase. With scale-up preparation of limonoate dehydrogenase, a successful debittering operation of fruit juices appears feasible.

Production of Yeast Extract by a Combined Method of Autolysis and Enzymatic Hydrolysis (자기소화와 효소가수분해 방법을 병용한 효모 추출물의 제조)

  • 인만진;채희정
    • KSBB Journal
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    • v.19 no.4
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    • pp.245-249
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    • 2004
  • A combined method of autolysis and enzymatic hydrolysis of baker's yeast was developed for the production of yeast extract, which is widely used as a natural food ingredient. From statistical analysis, NaCl and ethanol addition were found to be significantly effective factors in autolysis of yeast. The optimum dosages of salt and ethanol were 3% and 1%, respectively. Heat treatment and the use of cell lytic enzyme were not significantly effecting on the autolysis. Yeast hydrolysate was prepared by autolysis, followed by enzymatic hydrolysis using proteases, nuclease and deaminase. Additionally, the hydrolysate was processed by downstream process including Maillard reaction and debittering. The total dry matter yield and total nitrogen yield for the process were 76% and 59%, respectively. Compared to a process using brewer's yeast, when baker's yeast was used as a raw material, a higher recovery yield was obtained.

Debittering of Enzymatic Hydrolysate Using Exopeptidase Active Fractions from the Argentina Shortfin Squid Illex argentinus Hepatopancreas (원양산 오징어(Illex argentinus) 간췌장 유래 Exopeptidase 분획물의 쓴맛개선 효과)

  • Kim, Jin-Soo;Kim, Min Ji;Kim, Ki Hyun;Kang, Sang In;Park, Sung Hwan;Lee, Hyun Ji;Heu, Min Soo
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.47 no.2
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    • pp.135-143
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    • 2014
  • Exopeptidase active fractions from the hepatopancreas of the Argentina shortfin squid Illex argentinus, were obtained with acetone (AC 30-40%), ammonium sulfate (AS 60-70% saturation), anion exchange chromatography (AE-II, 0.2 M NaCl) and gel filtration chromatography (GF-I, 30-50 kDa) fractionation methods. A bitter peptide solution that has a bitterness equivalent to that of 2% glycylphenylalanine and prepared by tryptic hydrolysis of milk casein, was treated with the exopeptidase active fractions. The GF-I fraction was the best based on aminopeptidase activity (35.3 U/mg), percentage of recovery (30.7%) and a sensory evaluation (1.7). The amount of released amino acids increased as incubation time increased, and the bitterness of the enzyme reaction mixtures decreased. Incubation with the GF-I fraction for 24 h resulted in the hydrolysis of several peptides as revealed by the reverse-phase high performance liguid chromatography profile, with three peaks (3, 5 and 6) decreasing in area (%) and three peaks (1, 2 and 4) increasing in area (%). Therefore, the GF-I fraction appeared to be ideally suited to reduce bitterness in protein hydrolysates by catalyzing the hydrolysis of bitter peptides.

Debittering of Citrus Products Using ${\beta}-Cyclodextrin$ Polymer and Ultrafiltration Process (${\beta}-Cyclodextrin$ 중합체와 한외여과 공정을 이용한 감귤류의 쓴맛 성분 제거)

  • Woo, Gun-Jo;Ha, Seung-Mi
    • Korean Journal of Food Science and Technology
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    • v.29 no.2
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    • pp.302-308
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    • 1997
  • ${\beta}-Cyclodextrin\;({\beta}-CD)$ polymers were prepared using epichlorohydrin as a cross linking agent. The polymers were separated into ${\beta}-CD$ soluble polymer $({\beta}-CD\;SP)$ and ${\beta}-CD$ insoluble polymer $({\beta}-CD\;ISP)$ on a 10,000 molecular weight cut-off membrane (YM 10). Optimum separation conditions in the YM 10 were: transmembrane pressure 51.7 kPa, separation temperature $35^{\circ}C$, and volume concentration ratio 10. The flux was $0.025\;mL/cm^{2}/min$ under the optimum conditions. Gel permeation chromatography indicated that ${\beta}-CD\;SP\;and\;{\beta}-CD\;ISP$ had a degree of polymerization of $2{\sim}8$ and over 10, respectively. The formation of an inclusion complex with hydrophobic compounds such as 4-dimethylaminoazobenzene, methyl red, and naringin was compared among ${\beta}-CD,\;{\beta}-CD\;SP\;and\;{\beta}-CD\;ISP$. The molar absorptivity for the two chromatic compounds was increased and the absorption peak was shifted in the presence of ${\beta}-CD$ polymers. Naringin, the principal flavonoid bitter tasting component of citrus fruit, had a low water solubility. The solubility of naringin was increased through the formation of an inclusion complex with ${\beta}-CD$ polymers. There was no significant difference in the formation of an inclusion complex between ${\beta}-CD\;SP\;and\;{\beta}-CD\;ISP$. Reduction of the bitter components from citrus products was shown to be possible when employing ${\beta}-CD\;SP$, while the usage of ${\beta}-CD$ monomer has been limited due to the low water solubility.

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Lowering the Bitterness of Enzymatic Hydrolysate Using Aminopeptidase-active Fractions from the Common Squid (Todarodes pacificus) Hepatopancreas (살 오징어(Todarodes pacificus) 간췌장으로부터 aminopeptidase 활성 획분의 쓴맛 개선 효과)

  • Kim, Jin-Soo;Kim, Hye-Suk;Lee, Hyun Ji;Park, Sung Hwan;Kim, Ki Hyun;Kang, Sang In;Heu, Min Soo
    • Korean Journal of Food Science and Technology
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    • v.46 no.6
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    • pp.716-722
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    • 2014
  • Aminopeptidase-active fractions from crude extract of the hepatopancreas of a common squid (Todarodes pacificus) were obtained using acetone (AC; 30-40%) and ammonium sulfate precipitation (AS; 60-70% saturation), anion exchange (AE-II; 0.2 M NaCl) and gel filtration chromatography (GF-I; 30-50 kDa), respectively. The debittering capacity of GF-I fraction based on the aminopeptidase activity (89.2 U/mg), recovery (56.6%) and sensory evaluation (1.0) was better than that of other fractions. Release of amino acids increased as incubation time was increased, and the bitterness of the enzyme reaction mixtures decreased. Incubation with the GF-I fraction for 24 h resulted in the hydrolysis of several peptides, as revealed by reverse-phase HPLC profiles. Peaks 3, 5 and 6 showed the decreased area (%), whereas peaks 1, 2 and 4 showed the increased area. The GF-I fractions were found to be suitable for reducing bitterness in protein hydrolysates by catalyzing the hydrolysis of bitter peptides.

Washing for Debittering of Brewers Yeast Slurry (맥주효모 슬러리의 쓴맛을 제거하기 위한 세척)

  • Kim, Jae-Sik
    • Korean Journal of Food Science and Technology
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    • v.33 no.2
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    • pp.205-208
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    • 2001
  • The bitterness of brewers yeast slurry decreased by washing with mild caustic soda solution followed by washing with 0.85% (w/v) NaCl solution The higher concentration of caustic soda was, the lower the bitterness unit(BU) of washed yeast slurry was. The lethal rate of yeast cells increased. When the concentration of caustic soda solution increased from 0.05%(w/v) to 0.25%(w/v), the BU of brewers yeast slurry was decreased from 45 to 3, but yeast cells viability decreased from 93% to 0%. The optimum washing conditions of brewers yeast slurry were as follows: the concentration of caustic soda solution was $0.07{\sim}0.1%$(w/v) and the contact time of brewers yeast slurry with caustic soda was $10{\sim}20$ minutes. The similar washing effect was obtained when the brewers yeast slurry was washed with 20%(v/v) ethanol solution.

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Preparation and Food Characteristics of Seasoned Anchovy Sauce with Improved Bitterness by Treatment of Aminopeptidase Active Fraction Derived from Common Squid Todarodes pacificus Hepatopancreas (살 오징어(Todarodes pacificus) 간췌장 유래 Aminopeptidase 활성획분에 의해 쓴맛이 개선된 멸치 조미소스의 제조 및 식품특성)

  • Yoon, In Seong;Kim, Jin-Soo;Choe, Yu Ri;Sohn, Suk Kyung;Lee, Ji Un;Kang, Sang In;Kwon, In Sang;Heu, Min Soo
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.54 no.6
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    • pp.849-860
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    • 2021
  • This study investigated the preparation of seasoned anchovy sauce (SAS) and its functional characteristics by using aminopeptidase active fractions (AAFs) derived from squid Todarodes pacificus hepatopancreas as a bitter taste improver. As the base of the SAS, a hydrolysate (AAAH) prepared by continuously treating raw anchovies with Alcalase-AAF was used. The high-performance liquid chromatography profile of the AAAH suggested that the action of AAFs decreased the hydrophobicity of the N-terminal peptide related to bitterness in the protein hydrolysates. SAS was prepared by blending with the AAAH and other ingredients. The crude protein (2.5%), carbohydrates (18.4%), amino acid-nitrogen (1,325.1 mg/100 mL), and total free and released amino acids (FRAAs, 700.2 mg/100 mL) of SAS were higher than those of commercial anchovy sauce (CAS). Sensory evaluation revealed that SAS was superior to CAS in flavor, color, and taste. The main FRAAs of SAS were glycine (16.8%), alanine (13.2%), glutamic acid (7.8%), and leucine (7.3%). The amino acids that had a major influence on the taste according to the SAS taste values were glutamic acid, aspartic acid, alanine, and histidine. The angiotensin-converting enzyme inhibitory (2.21 mg/mL) and antioxidant activities (3.58 mg/mL) of SAS were superior to those of CAS.