• Title/Summary/Keyword: enzyme hydrolysis

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Analysis of Angiotensin I Converting Enzyme Inhibitory Activity of Oligosacchride Extracted from Capsosiphon fulvescens (매생이 유래 올리고당의 추출 분리 및 Angiotensin I Converting Enzyme 저해능 분석)

  • Kim, Hyun-Woo;Lee, Jung-Heon
    • KSBB Journal
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    • v.28 no.2
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    • pp.131-136
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    • 2013
  • The hydrolysates prepared with various enzyme digestion of Capsosiphon fulvescens were used to measure the inhibitory effects against angiotensin I converting enzyme (ACE). The commercially available enzymes such as Celluclast, Viscozyme, Lysing enzyme, Flavourzyme, Alcalase and Pectinex were used to digest C. fulvescens and produce hydrolysates. The maximum ACE inhibitory activity was observed using Alcalase hydrolysis (72.9%). The optimal conditions of Alcalase extraction were pH 8.0 and extraction time for 12 hr. The hydrolysates were fractionated using preparative-LC and anion-exchange chromatography on DEAE-cellulose and the fraction B and B-2 were isolated. The ACE inhibitory activity of fraction B-2 by anion-exchange chromatography was 82.6%. The molecular weight of fraction B-2 estimated using size exclusion chromatography was about 1 kDa. The monosaccharide composition of the fraction B-2 was determined to be mannose (1.1%), glucuronic acid (1.3%), galactose (1.3%) and glucose (96.3%).

Multicatalytic Alkaline Serine Pretense from the Psychrotrophic Bacillus amyloliquefaciens S94

  • Son, Eui-Sun;Kim, Jong-Il
    • Journal of Microbiology
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    • v.41 no.1
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    • pp.58-62
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    • 2003
  • An extracellular pretense of Bacillus amyloliquefaciens S94 was purified to apparent homogeneity. The enzyme activity was strongly inhibited by general inhibitor for serine protease, PMSF, suggesting that the enzyme is a serine pretense. The purified enzyme activity was inhibited by leucine peptidase inhibitor, bestatin, suggesting that the enzyme is a leucine endopeptidase. The maximum proteolytic activity against different protein substrates occurred at pH 10, 45$^{\circ}C$ (protein substrate) and pH 8, 45$^{\circ}C$ (synthetic substrate). The purified enzyme was specific in that it readily hydrolyBed substrates with Leu or Lys residues at P$_1$ site. The pretense had characteristics of a cold-adapted protein, which was more active for the hydrolysis of synthetic substrate in the range of 15$^{\circ}C$ to 45$^{\circ}C$, specially at low temperature.

Changes in Characteristics of Brown Rice (Goami) Alcohol Fermentation By-Product by Cellulase (Cellulase처리에 따른 현미(고아미) 알코올발효 부산물의 특성 변화)

  • Woo, Seung-Mi;Jang, Se-Young;Park, Nan-Yong;Kim, Tae-Young;Yeo, Soo-Hwan;Kim, Sang-Burm;Jeong, Yong-Jin
    • Food Science and Preservation
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    • v.15 no.1
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    • pp.99-104
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    • 2008
  • To utilize non-heat treated alcoholic by-products of brown rice (Goami) as food sources, the quality characteristics changes according to the treatment conditions of cellulase were evaluated. Results showed that the increase of hydrolysis temperature correspondingly increased the soluble solids and total sugar amounts in the by-products of Goami, and total dietary fiber amount was found to be around 0.67% Reducing sugar concentration was the highest at the hydrolysis temperature of $70^{\circ}C$. Maltooligosaccharides amounts were detected to be the highest at the hydrolysis temperature of $80^{\circ}C$ and were also, maltopentose and maltopentose were found. In the soluble solid, total dietary fiber, reducing sugar and total sugar according to the cellulase concentration, the content of hydrolysates with enzyme were higher than control, and the content of hydrolysates with enzyme was similar (6.30 and 0.69% 3,600 and 5,500 mg% respectively). The content of maltooligosaccharides was increased with the increase of enzyme concentration, and the content was similar at more than 0.6%(w/w) of enzyme concentration. The soluble solids and total dietary fiber by hydrolysis time were found to be 6.25% and 0.70%, respectively at more than 60 min. of hydrolysis. The content of reducing sugar, total sugar and maltooligosaccharides were increased with the increase of hydrolysis time, and the content was similar at more than 120min. of hydrolysis (3,800, 5,680 and 1,950 mg% respectively). Based upon these results, the byproducts of Goami are expected to be valuable as various food sources showing the highest dietary fiber and maltooligosaccharides contents by the hydrolysis at $80^{\circ}C$ for 120 min. with the addition of 0.6%(w/w) of cellulase.

Optimization of Hydrolysis Using Oyster and Oyster Cooking Drip (굴과 굴 자숙액을 이용한 가수분해 조건의 최적화)

  • Ryu, Tae-hyun;Kim, Jin-hee;Shin, Jiyoung;Kim, Sung-hoon;Yang, Ji-young
    • Journal of Life Science
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    • v.25 no.7
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    • pp.795-800
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    • 2015
  • Oyster is a nutritionally good food ingredient. Also, oyster is used to make source for taste and flavor. This study tried to investigate optimal condition of hydrolysis of oyster and oyster cooking drip for better amino acid content to make good taste and flavor. And then this study characterized hydrolysate of oyster and oyster cooking drip. Enzymes are Acalase, Flavourzyme, Neutrase, and Protamax. The optimal condition for the highest enzyme activity is given by the company. Under the best condition of each enzymes, they react with the homogenized oyster and oyster cooking drip for 0.5, 1.0, 1.5, 2, 4, 6 hr. The degree of oysters’ hydrolysis is 13.2±0.1%. But, in the case of using enzyme, the rate of hydrolysis sharply increased as time went on during 2 hr. After 8 hr, the rate is 36.9~40.5%. Protamax showed 27.4±0.4% of hydrolysis rate in 2 hr. And the degree of oyster cooking drop hydrolysis is 42.7±0.1%. The highest of hydrolysate concentration is 72.1±0.1% using protamax. In the case of oyster, it has a similar tendency of all enzymes. Otherwise, the hydrolysate of oyster cooking drip had a difference among the enzymes. Composition of free amino acid of hydrolysate using protamax was investigated how much time showed highest rate of hydrolysis to find best amino acid composition. Hydrolysis using Protamax during 6 hr is selected for best condition.

The Assessment of Hand for Enzyme Hydrolyzed Denim Fabrics(Part IV) -Effect of Fiber Content - (셀룰라아제 처리된 데님직물의 태에 관한 연구(제4보) - 섬유의 조성에 따른 주관적인 태 평가-)

  • 김경애;이미식;김정희
    • Journal of the Korean Society of Clothing and Textiles
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    • v.26 no.1
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    • pp.144-151
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    • 2002
  • The assessment of hand of the denim fabrics finished by enzymatic hydrolysis will be discussed in this study. The subjective hand and the preference of the denim fabrics finished by enzymatic hydrolysis were evaluated using the developed scale(Part I). The factors affecting consumer's taste for denim fabrics were analyzed by statistics using SAS program. Also, the enzymatic of hydrolysis on the properties of denim fabrics were evaluated by subjective hand measurements. The results are as follows; Regarding the surface properties and the weight, Tencel was evaluated to be the finest, the smoothest, the most flexible, the warmest, the most refined, the sleekest, the flossiest, the lightest the softest, and the thinnest among the four kinds of fabrics. The other fabrics in the order of cotton/Tencel, cotton, cotton/PP were evaluated to qualify the listed touches. Tencel was evaluated to be the loosest and the weakest among the four kinds of denim. Cotton was evaluated to have the driest touch. In addition, the fabrics were evaluated to be more elastic and less wrinkly in the order of Tencel > cotton > cotton/Tencel > cotton/ PP. For the hand preference, the fabrics were ranked in the order of Tencel, cotton, cotton/Tencel, cotton/PP, where tencel is the moat preferred. Cotton/Tencel and cotton/PP showed negative values in the hand and the color preference, meaning that the evaluators disliked their touches. Hand preference of enzyme hydrolyzed cotton/Tencel and cotton/PP denims do not seem to appeal to Korean people.

Cloning, Sequencing, and Expression of the Gene Encoding a Multidomain Endo-$\beta$-1,4-Xylanase from Paenibacillus curdlanolyticus B-6, and Characterization of the Recombinant Enzyme

  • Waeonukul, Rattiya;Pason, Patthra;Kyu, Khin Lay;Sakka, Kazuo;Kosug, Akihiko;Mori, Yutaka;Ratanakhanokchai, Khanok
    • Journal of Microbiology and Biotechnology
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    • v.19 no.3
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    • pp.277-285
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    • 2009
  • The nucleotide sequence of the Paenibacillus curdlanolyticus B-6 xyn10A gene, encoding a xylanase Xyn10A, consists of 3,828 nucleotides encoding a protein of 1,276 amino acids with a predicted molecular mass of 142,726 Da. Sequence analysis indicated that Xyn10A is a multidomain enzyme comprising nine domains in the following order: three family 22 carbohydrate-binding modules (CBMs), a family 10 catalytic domain of glycosyl hydrolases (xylanase), a family 9 CBM, a glycine-rich region, and three surface layer homology (SLH) domains. Xyn10A was purified from a recombinant Escherichia coli by a single step of affinity purification on cellulose. It could effectively hydrolyze agricultural wastes and pure insoluble xylans, especially low substituted insoluble xylan. The hydrolysis products were a series of short-chain xylooligosaccharides, indicating that the purified enzyme was an endo-$\beta$-1,4-xylanase. Xyn10A bound to various insoluble polysaccharides including Avicel, $\alpha$-cellulose, insoluble birchwood and oat spelt xylans, chitin, and starches, and the cell wall fragments of P. curdlanolyticus B-6, indicating that both the CBM and the SLH domains are fully functioning in the Xyn10A. Removal of the CBMs from Xyn10A strongly reduced the ability of plant cell wall hydrolysis. These results suggested that the CBMs of Xyn10A play an important role in the hydrolysis of plant cell walls.

Reaction Optimization for Enzymatic Synthesis of Astragalin (효소를 이용한 아스트라갈린 합성 반응의 최적화)

  • Lee, Seul Bi;Chung, Dae-won
    • Applied Chemistry for Engineering
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    • v.23 no.4
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    • pp.394-398
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    • 2012
  • Astragalin (AS), kaempferol monoglycoside, is classified as a polyphenol, and a minute quantity of AS is known to be present in several plants. Recently, it was reported that AS can be prepared by the partial hydrolysis of camelliaside A (CamA) and camelliaside B (CamB) in the tea seed extract (TSE) in the presence of a commercial enzyme complex such as Mash. In this paper, the effects of reaction temperature, amount of enzyme, and the substrate concentration on the reactivity were investigated. As the reaction temperature or the amount of enzyme increased, the reaction rate to produce AS increased, however, the hydrolysis of AS into KR was also enhanced. As a conclusion, the reaction, when 2 mL of Mash to 1 g of TSE was applied with a substrate concentration of 15% at $50^{\circ}C$, was found to be optimum, based on the reaction rate and the selectivity to AS.

Optimization for Enzymatic Hydrolysis of Mannitol (만니톨의 효소 가수분해 반응 조건 최적화)

  • Park, Eun-Young;Kim, Yong-Jin;Jeong, Seung-Mi;Lee, Dong-Hoon
    • KSBB Journal
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    • v.28 no.2
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    • pp.65-73
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    • 2013
  • This study aimed to investigate the enzymatic hydrolysis of mannitol using Viscozyme$^{(R)}$ L, Celluclast$^{(R)}$ 1.5 L, Saczyme$^{(R)}$, Novozym$^{(R)}$, Fungamyl$^{(R)}$ 800 L, Driselase$^{(R)}$ Basidiomycetes sp., and Alginate Lyase, and to optimize of reaction conditions for production of reducing sugar. Response surface methodology (RSM) based on central composite rotatable design was used to study effects of the independent variables such as enzyme (1-9% v/w), reaction time (10-30 h), pH (3.0-7.0) and reaction temperature ($30-70^{\circ}C$) on production of reducing sugar from mannitol. The coefficient of determination ($R^2$) of $Y_1$ (yield of reducing sugar by Viscozyme$^{(R)}$ L) and $Y_3$ (yield of reducing sugar by Saczyme$^{(R)}$) for the dependent variable regression equation was analyzed as 0.985 and 0.814. And the p-value of $Y_1$ and $Y_3$ showing 0.000 and 0.001 within 1% (p < 0.01), respectively, was very significant. The optimum conditions for production of reducing sugar with Viscozyme$^{(R)}$ L were 9.0 % (v/w) amount of enzyme, 30.0 hours of reaction time, pH 4.5 and $30.0^{\circ}C$ of reaction temperature, and those with Saczyme$^{(R)}$ were 9.0% (v/w) of amount of enzyme dosage, 30.0 h of reaction time, pH 7.0 and $30.0^{\circ}C$ of reaction temperature, consequently, the predicted reducing sugar yields were 22.5 and 27.9 mg/g-mannitol, respectively.

Two-step Acid Hydrolysis Method for Producing Fermentable Sugar from Lignocellulosic Biomass (발효당 생산을 위한 목질계 바이오매스의 2단 산당화)

  • Park, Jang Han;Kim, Jun Seok
    • Korean Chemical Engineering Research
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    • v.54 no.1
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    • pp.1-5
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    • 2016
  • For obtain fermentable sugar, we conducted acid hydrolysis with lignocellulosic biomass without enzyme. The lignocellulosic biomass used pinus rigida and Palm residues (EFB; empty fruit bunches). In the acid hydrolysis, we consider the hydrolysis condition to reduce a denatured sugar. So this study was conducted 2-step acid hydrolysis. First-step hydrolysis used high concentration (72 wt%) sulfuric acid at $80^{\circ}C$. At the condition, we obtained 11.49 wt%, 32 wt% glucose conversion for pinus rigida and EFB. After the step, the liquor was dilute until 9~15 wt% acid concentration and conducted second hydrolysis at $50{\sim}120^{\circ}C$. In the second hydrolysis, we obtained maximum glucose conversion (pinus rigida 86.8 wt% (39 g/L) and EFB 95.3 wt% (32.4 g/L)) at 9 wt% acid concentration and $120^{\circ}C$ for 80 min. All samples through the process are analyzed on the basis of mass balance.

Preparation and Characterization of the Hydrolyzed Protein from Shaving Scraps of Leather Waste Containing Chromium by the Combination Treatment with Alkaline Inducing Agent and Alkaline Proteolytic Enzyme (Alkaline Inducing Agent 및 Alkaline Proteolytic Enzyme 혼용처리에 의한 Shaving Scraps 가수분해 단백질의 제조 및 특성)

  • Kim, Won-Ju;Cho, Ju-Sik;Lee, Hong-Jae;Heo, Jong-Soo
    • Journal of the Korea Organic Resources Recycling Association
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    • v.6 no.1
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    • pp.1-12
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    • 1998
  • To examine the possibility of protein recycling of shaving scraps containing chromium generated from manufacturing process of leather, the optimum hydrolysis conditions and the withdrawal methods of low molecular weight protein for using the liquid fertilizer sources by investigation of solubilities of hydrolyzed protein, inorganic nutrients contents and molecular weight distributions of hydrolyzed protein from shaving scraps treated with mixed alkaline inducing agents and mixed alkaline proteolytic enzymes including MgO were investigated. In hydrolysis of shaving scraps treated with mixed alkaline inducing agents, the solubility of shaving scraps were clearly different with 65~85% according to the sorts of the inducing agents, and the degree of hydrolysis was high in the order of NaOH, $Ca(OH)_2$ and KOH. The average molecular weights of withdrawal hydrolyzed protein were 10, 40 and 80 KD treated with NaOH, $Ca(OH)_2$ and KOH, respectively. And the chromium contents was about 15 ppm. In hydrolysis of shaving scraps treated with mixed alkaline proteolytic enzymes, the bility of shaving scraps were high in the order of alcalase, esperase and savinase. In c of treating 0.5% alcalase, the low molecular weight of hydrolyzed protein could be withdrawn. The solubility of the hydrolyzed protein was about 85%, the average molecular weight of the protein was below 1 KD and chrome content of the protein was below 10 ppm.

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