• Title/Summary/Keyword: hydrolases

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Characteristics of salt-tolerant pretense purified from the fermented anchovy sauce

  • Kim, Woo-Jae;Kim, Sang-Moo
    • Proceedings of the Korean Society of Fisheries Technology Conference
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    • 2001.10a
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    • pp.91-92
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    • 2001
  • Enzymes have been used as processing aids in the manufacture of food products to improve their quality, solubility and stability for centuries. About 50% of the enzymes used as industrial processing aids are protein hydrolases which have been used in a number of industrial application including laundry detergents, feed, leather treatment, silk degumming, cheese making, chill proofing, meat tenderzing, fermented sauces, and pharmaceuticals. (omitted)

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Purification of Porcine Leukocyte Lysosomal Hydrolases (Porcine Leukocyte Lysosomal Hydrolase의 정제에 관(關)한 연구(硏究))

  • Cho, Moo-Je
    • Applied Biological Chemistry
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    • v.20 no.1
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    • pp.136-141
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    • 1977
  • DEAE-Cellulose, Sephadex column chromatography and polyacrylamide gel electrophoresis were used to purify acid phosphatase, aryl sulfatases, ${\beta}-glucuronidase$ and cathepsin D in n-butyl alcohol extracts of porcine leukocyte Iysosomes. The degree of purification was quite high for all enzymes studied and some could be identified by histochemical reactions.

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ADP-Ribosylation: Activation, Recognition, and Removal

  • Li, Nan;Chen, Junjie
    • Molecules and Cells
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    • v.37 no.1
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    • pp.9-16
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    • 2014
  • ADP-ribosylation is a type of posttranslational modification catalyzed by members of the poly(ADP-ribose) (PAR) polymerase superfamily. ADP-ribosylation is initiated by PARPs, recognized by PAR binding proteins, and removed by PARG and other ADP-ribose hydrolases. These three groups of proteins work together to regulate the cellular and molecular response of PAR signaling, which is critical for a wide range of cellular and physiological functions.

Cloning and Characterization of a ${\beta}$-Glucosidase from Marine Microbial Metagenome with Excellent Glucose Tolerance

  • Fang, Zemin;Fang, Wei;Liu, Juanjuan;Hong, Yuzhi;Peng, Hui;Zhang, Xuecheng;Sun, Baolin;Xiao, Yazhong
    • Journal of Microbiology and Biotechnology
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    • v.20 no.9
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    • pp.1351-1358
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    • 2010
  • The demand for ${\beta}$-glucosidases insensitive to product inhibition is increasing in modern biotechnology, for these enzymes would improve the process of saccharification of lignocellulosic materials. In this study, a ${\beta}$-glucosidase gene that encodes a 442-amino-acid protein was isolated from a marine microbial metagenomic library by functional screening and named as bgl1A. The protein was identified to be a member of the glycoside hydrolases 1 family, and was recombinantly expressed, purified, and biochemically characterized. The recombinant ${\beta}$-glucosidase, Bgl1A, exhibited a high level of stability in the presence of various cations and high concentrations of NaCl. Interestingly, it was activated by glucose at concentrations lower than 400 mM. With glucose further increasing, the enzyme activity of Bgl1A was gradually inhibited, but remained 50% of the original value in even as high as 1,000 mM glucose. These findings indicate that Bgl1A might be a potent candidate for industrial applications.

Nucleotide Sequence of a Bacteriolytic Enzyme Gene from Alkalophilic Bacillus sp.

  • Jung, Myeong-Ho;Ohk, Seung-Ho;Yum, Do-Young;Kong, In-Soo;Bai, Dong-Hoon
    • Journal of Microbiology and Biotechnology
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    • v.3 no.2
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    • pp.73-77
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    • 1993
  • The nucleotide sequence of Bacillus sp. bacteriolytic enzyme gene, lytP and its flanking regions were determined. A unique open reading frame for a protein of Mw. 27, 000, and a putative terminator sequence, were found behind a concensus ribosome binding site located 8 nt upstream from ATG start codon. The primary amino acid sequence deduced from nucleotide sequence revealed a putative protein of 255 amino acid residues with an Mw. of 27, 420. No significant homology could be found between the amino acid sequence of Bacillus sp. bacteriolytic enzyme and that of other cell wall hydrolases.

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Production of Chiral Epoxides: Epoxide Hydrolase-catalyzed Enantioselective Hydrolysis

  • Choi, Won-Jae;Choi, Cha-Yong
    • Biotechnology and Bioprocess Engineering:BBE
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    • v.10 no.3
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    • pp.167-179
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    • 2005
  • Chiral epoxides are highly valuable intermediates, used for the synthesis of pharmaceutical drugs and agrochemicals. They have broad scope of market demand because of their applications. A major challenge in modern organic chemistry is to generate such compounds in high yields, with high stereo- and regio-selectivities. Epoxide hydrolases (EH) are promising biocatalysts for the preparation of chiral epoxides and vicinal diols. They exhibit high enantioselectivity for their substrates, and can be effectively used in the resolution of racemic epoxides through enantioselective hydrolysis. The selective hydrolysis of a racemic epoxide can produce both the corresponding diols and the unreacted epoxides with high enantiomeric excess (ee) value. The potential of microbial EH to produce chiral epoxides and vicinal diol has prompted researchers to explore their use in the synthesis of epoxides and diols with high ee values.

Overproduction of Lactic Bacterial Enzymes and Bioactive Components

  • Lee, Byong-H.
    • 한국유가공학회:학술대회논문집
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    • 2002.04a
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    • pp.45-55
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    • 2002
  • Recent developments in the application of molecular biology to food grade lactic acid bacteria (LAB) have shown that it could be feasible to engineer metabolic pathways to either enhance specific metabolic fluxes or to divert metabolites for the production of different or new end products. This engineering requires detailed knowledge of enzymes involved in metabolism and regulation within the targeted organism but little works have been done in this area. During biochemical and molecular characterisation of lactic bacterial enzymes, some of probiotic Lactobacillus and Bifidobacterium species were found to be very useful for food, nutraceutical and pharmaceutical industries. The enzymes are usually intracellular and the yields are very low to be useful for industrial applications. Among many enzymes and proteins of lactic bacteria studied, some of our gene cloning achievements have contributed to overproduction of lactic bacterial enzymes such as peptidases, esterases, lactases, bile salt hydrolases and linoleate isomerases for foods and nutraceuticals.

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Effects of Enzymatic Hydrolysis and Concentrations of Sugar and Salt on Kimchi Juice Fermentation of Outer Leaves of Chinese Cabbage (배추 겉잎을 이용한 김치쥬스 제조시 효소분해, 당, 소금농도가 발효에 미치는 영향)

  • 전윤기;윤석권;김우정
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.26 no.5
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    • pp.788-793
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    • 1997
  • Addition of sugar, enzymatic hydrolysis and salt concentration were evaluated for their effects on the changes in some characteristics of Kimchi juice during fermentation. The Kimchi juice was prepared by brining and grinding of outer layer leaves of chinese cabbage, one of the wastes products of Kimchi processing, followed by fermentation proceeded significantly faster. Addition of sucrose or glucose at the ange of 0.5~2.0 % also improved the fermentation but the concentration effect was little. Enzymatic hydrolysis on the brined cabbage prior to fermentation with a commercial polysaccharides hydrolases also increased the fermentation. However the solid concentration in Kimchi juice was rather decreased by higher concentration of NaCl and enzymatic hydrolysis. The reducing sugar content showed a rapid decrease from 24 hours of fermentation and the effect of enzymatic hydrolysis was little.

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Isolation and identification of Bacillus sp, GS Producing Xylanase (Xylanase생산성 Bacillus sp. GS의 분리 및 동정)

  • An, Jun-Bae;Park, Heon-Guk;Lee, Gye-Ho
    • The Korean Journal of Food And Nutrition
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    • v.7 no.1
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    • pp.8-15
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    • 1994
  • To utilize hemicellulosic biomass efficiently, the microorganism producing xylanase was isolated from fermented sawdust. It was a Gram positive, aerobic and rod shape bacterium. It had endospore and secreted strong hydrolases, such as amylase and protease. Through morphological, cultural and physiological tests, it was identified as Bacillus sp. GS. To increase the productivity of xylanase from Bacillus sp. GS, the enzyme production medium was optimized. The composition of the medium and incubation conditions were like follows xylan 1.25%, yeast extract 0.1%, NaN030.2%, K2HP04 0.1%, MgSO4 0.02%, mineral salt 0.005%, pH 6.5, incubation temperature 37$^{\circ}C$.

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