• Title/Summary/Keyword: hydrolases

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Chemical Properties of Porcine Leukocyte Lysosomal Hydrolases (Porcine Leukocyte Lysosomal Hydrolases의 화학적성질(化學的性質)에 관(關)한 연구(硏究))

  • Cho, Moo-Je
    • Applied Biological Chemistry
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    • v.20 no.2
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    • pp.175-181
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    • 1977
  • Lysosomal enzyme latency was demonstrated for hydrolases from porcine leukocyte by suspending sediment sfrom differential centrifugation in 0.125 to 0.250 M sucrose. Specific activities pH optima and activation energies were determined for hydrolases distributed in various sedimentation fractions and for enzymes solubilized by n-butyl alcohol extraction. Specific activities of the hydrolases revealed the heterogeneity of the Iysosomal fractions relative to enzyme content. pH optima identified the enzyme as acid hydrolases with optima for cathepsin D and aryl sulfatase also at pH 6.8. Activation energies of some hydrolases were low revealing that these enzymes could function efficiently during low temperature aging of meat.

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Prediction of optimum pH of hydrolases

  • Sung, Nak-Gyu;Yoo, Young-Je
    • 한국생물공학회:학술대회논문집
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    • 2000.11a
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    • pp.571-574
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    • 2000
  • Hydrolase is a group of the most widely used enzymes in industrial biological processes. Generally, their activities are easily changed with pH. With this characteristics, research for the optimal pH of hydrolases is required to obtain the optimization of process conditions. We selected xylanase, lysozyme, glucoamylase and barnase as model enzymes. To predict optimum pH of hydrolases, the calculation program based on Tanford-Kirkwood(TK) model was used. Results show that charge difference of catalytic residues is an important parameter deciding optimum pH and when charge difference of catalytic residues is maximum, optimum pH of the hydrolase establishes.

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Characterization of cell wall hydrolases induced by sugar starvation

  • Lee, Eun-Jeong;Koizumi, Nozomu
    • Proceedings of the Korean Society of Plant Biotechnology Conference
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    • 2005.11a
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    • pp.371-374
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    • 2005
  • In our previous work in transcriptional regulation of sugar, expression of genes encoding putative glycosyl hydrolases in Arabidopsis was induced by sugar starvation. They were annotated as b-galactosidase (At5g56870), ${\beta}-xylosidase$ (At5g49360) and ${\beta}-glucosidase$ (At3g60140), which belong to glycosyl hydrolase family that has a catalytic domain of polysaccharides. From the primary structure of deduced amino acid sequence, they were predicted to localize to cell wall. Further investigation of these cell wall hydrolases implicated that cell wall polysaccharides provide metabolizable sugars to nutrient allocation under sugar starvation.

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A MALDI-MS-based Glucan Hydrolase Assay Method for Whole-cell Biocatalysis

  • Ahn, Da-Hee;Park, Han-Gyu;Song, Won-Suk;Kim, Seong-Min;Jo, Sung-Hyun;Yang, Yung-Hun;Kim, Yun-Gon
    • Microbiology and Biotechnology Letters
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    • v.47 no.1
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    • pp.69-77
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    • 2019
  • Screening microorganisms that can produce glucan hydrolases for industrial, environmental, and biomedical applications is important. Herein, we describe a novel approach to perform glucan hydrolase screening-based on analysis of matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) spectra-which involves degradation of the oligo- and polysaccharides. As a proof-of-concept study, glucan hydrolases that could break down glucans made of several glucose units were used to demonstrate the MALDI-MS-based enzyme assay. First, the enzyme activities of ${\alpha}$-amylase and cellulase on a mixture of glucan oligosaccharides were successfully discriminated, where changes of the MALDI-MS profiles directly reflected the glucan hydrolase activities. Next, we validated that this MALDI-MS-based enzyme assay could be applied to glucan polysaccharides (i.e., pullulan, lichenan, and schizophyllan). Finally, the bacterial glucan hydrolase activities were screened on 96-well plate-based platforms, using cell lysates or samples of secreted enzyme. Our results demonstrated that the MALDI-MS-based enzyme assay system would be useful for investigating bacterial glucoside hydrolases in a high-throughput manner.

Changes in Haemolymph Proteins, Hydrolases, and Inorganic tons of Heliothis assulta Injected with Bacillus thuringiensis (Bacillus thuringiensis의 주입에 따른 담배나방의 혈림프 단백질, 가수분해효소 및 무기이온의 변화)

  • 유종명;조시형;황석연;이형철
    • Journal of the Korean Society of Tobacco Science
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    • v.16 no.1
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    • pp.90-96
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    • 1994
  • Changes in haemolymph proteins, hydrolases such as esterase(EST), acid phosphatase(ACP) and alkaline phosphatase(ALP) , and inorganic ion(Na+, K+ and Cl- ) contents were induced by the injection of Bacillus thuringiengis into haemocoel of the last instar larva of Heliothis assulta. Protein concentration of haemolymph was increased until 24 hrs after injection, and decreased thereafter. Among the 8 basic protein bands identified through acid - polyacrylamide gel electrophoresis(PAGE), 2 bands(bands a and b) became stronger by the bacterial infection. Activities of EST and ALP increased until 12 hrs after injection and then fell down, whereas ACP activity was decreased continuously with time after injection. Contents of inorganic ions were all increased by the bacterial injection, showing slow rate of increase in the chloride ion, but rapid in the sodium and potassium ions.

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Complete genome sequence of Paenibacillus konkukensis sp. nov. SK3146 as a potential probiotic strain

  • Jung, Hae-In;Park, Sungkwon;Niu, Kai-Min;Lee, Sang-Won;Kothari, Damini;Yi, Kwon Jung;Kim, Soo-Ki
    • Journal of Animal Science and Technology
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    • v.63 no.3
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    • pp.666-670
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    • 2021
  • Paenibacillus konkukensis sp. nov., SK3146 is a novel strain isolated from a pig feed. Here, we present complete genome sequence of SK3146. The genome consists of a single circular genome measuring 7,968,964 bp in size with an average guanine + cytosine (G+C) content of 53.4%. Genomic annotation revealed that the strain encodes 151 proteins related to hydrolases (EC3), which was higher than those in Bacillus subtilis and Escherichia coli. Diverse kinds of hydrolases including galactosidase, glucosidase, cellulase, lipase, xylanase, and protease were found in the genome of SK3146, coupled with one bacteriocin encoding gene. The complete genome sequence of P. konkukensis SK3146 indicates the immense probiotic potential of the strain with nutrient digestibility and antimicrobial activity functions.