The effects of mannanase activity on viscosity in different gums

2020 ◽  
Author(s):  
Selime Benemir Erkan ◽  
Ali Ozcan ◽  
Cansu Yilmazer ◽  
Hilal Nur Gurler ◽  
Ercan Karahalil ◽  
...  
Keyword(s):  
Mannanase Activity

scholarly journals Enzyme activity in the micropylar region of Melanoxylon brauna Schott seeds during germination under heat stress conditions

2020 ◽  
Vol 42 ◽  
Author(s):  
Marcone Moreira Santos ◽  
Eduardo Euclydes de Lima e Borges ◽  
Glauciana da Mata Ataíde ◽  
Raquel Maria de Oliveira Pires ◽  
Debora Kelli Rocha
Keyword(s):  
Enzyme Activity ◽  
Heat Stress ◽  
Seed Germination ◽  
Pectin Methylesterase ◽  
Stress Conditions ◽  
Southeastern Brazil ◽  
Experimental Conditions ◽  
Mannanase Activity ◽  
Ecological Importance ◽  
The Many

Abstract: Recent studies indicate that global temperatures will rise substantially in the 21st century, leading to the extinction of several plant species, as plant metabolism and germination are greatly affected by temperature. Melanoxylon brauna, a tree species native to the Atlantic Forest that occurs from northeastern to southeastern Brazil, is one of the many species threatened by global warming. Despite the economic and ecological importance of M. brauna, studies investigating the influence of heat stress on seed germination and biochemical responses are still incipient. This study aimed to evaluate enzyme activity in the micropylar region of M. brauna seeds during germination under heat stress conditions. Endo-β-mannanase, α-galactosidase, polygalacturonase, pectin methylesterase, pectin lyase, total cellulase, 1,3-β-glucosidase, and 1,4-β-glucosidase activities were determined in micropyles of seeds imbibed for 24, 48 and 72 h at 25, 35 and 45 °C. Seed germination was highest at 25 °C. Endo-β-mannanase activity was not detected under any of the experimental conditions, but imbibition temperature had a significant effect on the activity of all other enzymes.

scholarly journals eta-mannanase activity of Trichosporonoides oedocephalis evaluated in different process parameters

2015 ◽  
Vol 9 (4) ◽  
pp. 230-238
Author(s):  
Oladiti Olaniyi Oladipo ◽  
Folasade Ibitoye Oluyemisi ◽  
Olufemi Bankefa Emmanuel
Keyword(s):  
Process Parameters ◽  
Mannanase Activity ◽  
Trichosporonoides Oedocephalis

Structural and Kinetic Dissection of theendo-α-1,2-Mannanase Activity of Bacterial GH99 Glycoside Hydrolases fromBacteroides spp.

2014 ◽  
Vol 21 (5) ◽  
pp. 1966-1977 ◽  
Author(s):  
Zalihe Hakki ◽  
Andrew J. Thompson ◽  
Stephanie Bellmaine ◽  
Gaetano Speciale ◽  
Gideon J. Davies ◽  
...  
Keyword(s):  
Glycoside Hydrolases ◽  
Mannanase Activity

Mannan-Degrading Enzymes fromCellulomonas fimi

1999 ◽  
Vol 65 (6) ◽  
pp. 2598-2605 ◽  
Author(s):  
Dominik Stoll ◽  
Henrik Stålbrand ◽  
R. Antony J. Warren
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Unknown Function ◽  
Glycosyl Hydrolases ◽  
Intracellular Enzyme ◽  
Cellulomonas Fimi ◽  
Catalytic Module ◽  
Mannanase Activity ◽  
Homology Module ◽  
Active Fragments

ABSTRACT The genes man26a and man2A fromCellulomonas fimi encode mannanase 26A (Man26A) and β-mannosidase 2A (Man2A), respectively. Mature Man26A is a secreted, modular protein of 951 amino acids, comprising a catalytic module in family 26 of glycosyl hydrolases, an S-layer homology module, and two modules of unknown function. Exposure of Man26A produced byEscherichia coli to C. fimi protease generates active fragments of the enzyme that correspond to polypeptides with mannanase activity produced by C. fimi during growth on mannans, indicating that it may be the only mannanase produced by the organism. A significant fraction of the Man26A produced by C. fimi remains cell associated. Man2A is an intracellular enzyme comprising a catalytic module in a subfamily of family 2 of the glycosyl hydrolases that at present contains only mammalian β-mannosidases.

scholarly journals Comparative Analyses of Two Thermophilic Enzymes Exhibiting both β-1,4 Mannosidic and β-1,4 Glucosidic Cleavage Activities from Caldanaerobius polysaccharolyticus

2010 ◽  
Vol 192 (16) ◽  
pp. 4111-4121 ◽  
Author(s):  
Yejun Han ◽  
Dylan Dodd ◽  
Charles W. Hespen ◽  
Samuel Ohene-Adjei ◽  
Charles M. Schroeder ◽  
...  
Keyword(s):  
Catalytic Domain ◽  
Biochemical Properties ◽  
Degree Of Polymerization ◽  
Glycoside Hydrolase Family ◽  
Carbohydrate Binding ◽  
Biofuel Industry ◽  
Carbohydrate Binding Modules ◽  
Mannanase Activity ◽  
Hydrolysis Of ◽  
Derivatives Of

ABSTRACT The hydrolysis of polysaccharides containing mannan requires endo-1,4-β-mannanase and 1,4-β-mannosidase activities. In the current report, the biochemical properties of two endo-β-1,4-mannanases (Man5A and Man5B) from Caldanaerobius polysaccharolyticus were studied. Man5A is composed of an N-terminal signal peptide (SP), a catalytic domain, two carbohydrate-binding modules (CBMs), and three surface layer homology (SLH) repeats, whereas Man5B lacks the SP, CBMs, and SLH repeats. To gain insights into how the two glycoside hydrolase family 5 (GH5) enzymes may aid the bacterium in energy acquisition and also the potential application of the two enzymes in the biofuel industry, two derivatives of Man5A (Man5A-TM1 [TM1 stands for truncational mutant 1], which lacks the SP and SLH repeats, and Man5A-TM2, which lacks the SP, CBMs, and SLH repeats) and the wild-type Man5B were biochemically analyzed. The Man5A derivatives displayed endo-1,4-β-mannanase and endo-1,4-β-glucanase activities and hydrolyzed oligosaccharides with a degree of polymerization (DP) of 4 or higher. Man5B exhibited endo-1,4-β-mannanase activity and little endo-1,4-β-glucanase activity; however, this enzyme also exhibited 1,4-β-mannosidase and cellodextrinase activities. Man5A-TM1, compared to either Man5A-TM2 or Man5B, had higher catalytic activity with soluble and insoluble polysaccharides, indicating that the CBMs enhance catalysis of Man5A. Furthermore, Man5A-TM1 acted synergistically with Man5B in the hydrolysis of β-mannan and carboxymethyl cellulose. The versatility of the two enzymes, therefore, makes them a resource for depolymerization of mannan-containing polysaccharides in the biofuel industry. Furthermore, on the basis of the biochemical and genomic data, a molecular mechanism for utilization of mannan-containing nutrients by C. polysaccharolyticus is proposed.

Endo-beta-mannanase activity during dormancy alleviation and germination of white spruce (Picea glauca) seeds

1997 ◽  
Vol 101 (2) ◽  
pp. 405-415 ◽  
Author(s):  
Bruce Downie ◽  
Henk W. M. Hilhorst ◽  
J. Derek Bewley
Keyword(s):  
Picea Glauca ◽  
White Spruce ◽  
Mannanase Activity

scholarly journals Obtaining and characterization of modified mannan from the coffee sludge

2020 ◽  
Vol 22 (93) ◽  
pp. 55-60
Author(s):  
N. Cherno ◽  
K. Naumenko ◽  
L. Gural
Keyword(s):  
Molecular Weight ◽  
Raw Materials ◽  
Monosaccharide Composition ◽  
Water Soluble ◽  
Blood Cholesterol ◽  
Alkaline Solutions ◽  
Food Ingredients ◽  
Monomer Composition ◽  
Coffee Beans ◽  
Mannanase Activity

Mannans are polysaccharides of natural origin. Their main chain consists of residues of D-mannose. They have an immunomodulatory effect, able to induce macrophage activation, inhibit tumor growth and virus development, normalize blood cholesterol, etc. Manooligosaccharides are effective prebiotics The main way to obtain mannan is to extract their alkaline solutions. This makes it impossible to use this polysaccharide in food technologe. This study proposes a biotechnological method of producing water-soluble mannan from coffee sludge. As a source of mannan used a by-product of obtaining instant coffee at the Odessa Combine Food Concentrates which is formed in the processing of coffee beans Arabica. The chemical composition of this coffee sludge was investigated. It is dominated by water-insoluble carbohydrates which are represented by hemicellulose polysaccharides and cellulose. Analysis of the monosaccharide composition of hemicelluloses showed that the hydrolyzate contains mannose, glucose and galactose residues in a ratio of 6: 0,5: 3., which may indicate the presence of galactomannan in their composition. The developed method involves the treatment of the coffee sludge with enzyme preparation with beta-mannanase activity. The process was carried out in aqueous medium at temperature 50 °C, varying the hydromodule in the range of 30… 50, the ratio of enzyme: substrate (1:25, 1:50 and 1:100) for 24…72 hours. This study presents the characteristics of the monomer composition and molecular weight distribution of polysaccharide samples obtained in this way. Only mannose was found in the hydrolyzate of water-soluble mannan. The rational conditions of enzymatic processing of raw materials are determined. The modified mannan is soluble in water. It contains the highest number of target fragments with a molecular weight of about 20 kDa which are considered to be the most physiologically active. Subsequently the modified mannan can be used in nanotechnology functional food ingredients and dietary supplements.

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