Enzymatic hydrolysis of agar: purification and characterization of β-neoagarotetraose hydrolase from Pseudomonas atlantica

1977 ◽  
Vol 23 (6) ◽  
pp. 672-679 ◽  
Author(s):  
D. Groleau ◽  
W. Yaphe
Keyword(s):  
Cell Wall ◽  
Enzymatic Hydrolysis ◽  
Cytoplasmic Membrane ◽  
Degree Of Polymerization ◽  
Hydrolase Activity ◽  
Wall Region ◽  
Purification And Characterization ◽  
Hydrolysis Of

Agarose is degraded by a β-agarase from Pseudomonas atlantica to neoagarooligosaccharides of degree of polymerization (DP) 4, 6, 8, and 10. A β-neoagarotetraose hydrolase cleaves the central β-linkage in neoagarotetraose and the β-linkage near the nonreducing end in neoagarohexaose and -octaose to yield neoagarobiose. The β-neoagarotetraose hydrolase was localized on or outside the cytoplasmic membrane, in the cell wall region. The enzyme was activated by NaCl, KCl, CaCl2, MnCl2, and MgSO4, has a Km of 3.4 × 10−3 M for neoagarotetraose, was free from β-agarase and α-neoagarobiose hydrolase activity, and showed no transglycosidic activity.

Enzymatic hydrolysis of agar: purification and characterization of neoagarobiose hydrolase and p-nitrophenyl α-galactoside hydrolases

1975 ◽  
Vol 21 (10) ◽  
pp. 1512-1518 ◽  
Author(s):  
D. F. Day ◽  
W. Yaphe
Keyword(s):  
Enzymatic Hydrolysis ◽  
Hydrolytic Enzymes ◽  
Partial Characterization ◽  
Purification And Characterization ◽  
Hydrolysis Of

The mixture of polysaccharides in the gelling component of agar (agarose) is hydrolyzed to D-galactose and 3,6-anhydro-L-galactose by a series of hydrolytic enzymes obtained from Pseudomonas atlantica. The final degradative step in the pathway of agarose decomposition is the hydrolysis of the α-linkage in the dissaccharide neoagarobiose yielding D-galactose and 3,6-anhydro-L-galactose. Pseudomonas atlantica when grown on agar produces two specific enzymes, p-nitrophenyl α-galactose hydrolase and neoagarobiose hydrolase. The purification and partial characterization of both enzymes are presented.

scholarly journals Production, Optimization, Purification and Characterization of Mannanase Produced by Bacillus Subtilis

2020 ◽  
pp. 52-67
Author(s):  
Adebayo-Tayo Bukola Christianah ◽  
Onifade Deborah Ajoke
Keyword(s):  
Bacillus Subtilis ◽  
Soft Tissues ◽  
Gel Filtration ◽  
Processing Parameters ◽  
Degree Of Polymerization ◽  
Production Optimization ◽  
Purification And Characterization ◽  
Fermentation Method ◽  
Hydrolysis Of

Endo-β-1,4-D-mannanase (β-mannanase; EC 3.2.1.78) catalyses the random hydrolysis of mannoglycosidic bonds in mannan-based polysaccharides. These enyzmes are commonly found in nature and are located within the structure of mannans and heteromannans (galactomannan, glucomannan and galactoglucomannan) in the hemicellulose fraction of trees with soft tissues and hard tissues, locust bean seed.  Most β-mannanases degrade mannooligosaccharides down to a degree of polymerization of four. In this study mannanase was produced using a submerged fermentation method from Bacillus subtilis. The effect of growth of the organism and processing parameters on the production of mannanase were determined after which optimization studies were carried out. The enzyme was partially purified using ammonium sulphate, dialysis and gel filtration. The partially purified enzyme was characterized. The result of the study showed that mannanase enzyme from Bacillus subtilis was optimally produced in a medium comprising of galactose, peptone, sugarcane bagasse at a pH of 6.0 and a temperature of 45 oC. The enzyme was most stable and active at pH 10.0 and at a temperature of 40 oC.  and 60 respectively.

scholarly journals Characterization of Glycoside Hydrolase Family 5 Proteins in Schizosaccharomyces pombe

2010 ◽  
Vol 9 (11) ◽  
pp. 1650-1660 ◽  
Author(s):  
Encarnación Dueñas-Santero ◽  
Ana Belén Martín-Cuadrado ◽  
Thierry Fontaine ◽  
Jean-Paul Latgé ◽  
Francisco del Rey ◽  
...  
Keyword(s):  
Cell Wall ◽  
Schizosaccharomyces Pombe ◽  
Protein Characterization ◽  
Wall Material ◽  
Glycoside Hydrolase Family ◽  
Content Type ◽  
Hydrolysis Of ◽  
Controlled Hydrolysis ◽  
Hydrolase Family

ABSTRACT In yeast, enzymes with β-glucanase activity are thought to be necessary in morphogenetic events that require controlled hydrolysis of the cell wall. Comparison of the sequence of the Saccharomyces cerevisiae exo-β(1,3)-glucanase Exg1 with the Schizosaccharomyces pombe genome allowed the identification of three genes that were named exg1 + (locus SPBC1105.05), exg2 + (SPAC12B10.11), and exg3 + (SPBC2D10.05). The three proteins have different localizations: Exg1 is secreted to the periplasmic space, Exg2 is a membrane protein, and Exg3 is a cytoplasmic protein. Characterization of the biochemical activity of the proteins indicated that Exg1 and Exg3 are active only against β(1,6)-glucans while no activity was detected for Exg2. Interestingly, Exg1 cleaves the glucans with an endohydrolytic mode of action. exg1 + showed periodic expression during the cell cycle, with a maximum coinciding with the septation process, and its expression was dependent on the transcription factor Sep1. The Exg1 protein localizes to the septum region in a pattern that was different from that of the endo-β(1,3)-glucanase Eng1. Overexpression of Exg2 resulted in an increase in cell wall material at the poles and in the septum, but the putative catalytic activity of the protein was not required for this effect.

scholarly journals Purification and Characterization of Soluble and Cell Wall-bound Acid .ALPHA.-Glucosidases of Ripe Yellow Banana Pulp.

2001 ◽  
Vol 48 (1) ◽  
pp. 19-25
Author(s):  
Yotaro Konishi ◽  
Mia Harada ◽  
Mie Nakasuji ◽  
Marisa D'Innocenzo ◽  
Franco M. Lajolo
Keyword(s):  
Cell Wall ◽  
Purification And Characterization
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