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Same Enzyme (same + enzyme)

Distribution by Scientific Domains

Life Sciences	80%

Selected Abstracts

Enzymatic fatty acid exchange in glycero-phospholipids,

EUROPEAN JOURNAL OF LIPID SCIENCE AND TECHNOLOGY, Issue 10 2003
Patrick Adlercreutz
Abstract Lipases can be used to exchange fatty acids in the sn -1 position of glycerophospholipids and phospholipase A2 is useful for the corresponding exchange reaction in the sn -2 position. In both cases, the exchange can be done in a one-step acidolysis process or in a two-step process. In the latter case, the original fatty acid in the desired position is removed by enzymatic hydrolysis or alcoholysis and after isolation of the resulting lysophospholipid, the new fatty acid is introduced, using the same enzyme, in an esterification reaction. Several synthesis examples from the literature are reviewed. Incorporation of a new fatty acid into the sn -1 position is more favourable than incorporation into the sn -2 position because of the magnitudes of the equilibrium constants of the reactions and because lipases can be used at much lower water activity than phospholipase A2. With the consecutive use of both enzymes highly pure products with defined fatty acids in both positions can be obtained. [source]

Characterization of ,- d -glucosidase extracted from soil fractions

EUROPEAN JOURNAL OF SOIL SCIENCE, Issue 2 2000
M. D. Busto
Summary One way to study the state in which stabilized extracellular enzymes persist and are active in the soil is by extraction from the soil, with subsequent fractionation of enzyme,organomineral complexes and characterization of such complexes. In order to investigate the location and characteristics of soil ,-glucosidase, three soil fractions were obtained both from real (undisturbed) soil aggregates and from structural (dispersed in water and physically disrupted) aggregates using two different granulometric procedures. The ,-glucosidase activity of the fraction was then assayed. When the aggregates were dispersed, more than 73% of activity was in the soil microaggregates with diameters of less than 50 ,m (SF50). These aggregates were associated with strongly humified organic matter. Solutions of diluted pyrophosphate at neutral pH liberated active ,-glucosidase from all fractions, although the efficacy of extraction varied according to the type of fraction. The SF50 fraction and aggregates of 2000,100 ,m obtained by sieving (SF2000) showed the greatest ,-glucosidase activity (34.5 and 36.0%, respectively). Micro- and ultrafiltration of SF50 extracts increased the total ,-glucosidase activity, whereas these procedures, applied to the RF2000 fraction, decreased it. Humus,,-glucosidase complexes in the SF50 fraction, between 0.45 ,m and 105 nominal molecular weight limit ( nmwl) (SF50II) and < 105nmwl (SF50III) showed an optimum pH at 5.4, and in the SF50I fraction (> 0.45 ,m) the optimum was 4.0. The stability of ,-glucosidase in the aggregates of the smallest size SF50II and SF50III decreased at acid pHs. The presence of two enzymes (or two forms of the same enzyme) catalysing the same reaction with different values of Michaelis constant and maximum velocity was observed in all but one of the ,-glucosidase complexes extracted and partially purified from the SF50 aggregates. [source]

Control of nitrogen metabolism by Bacillus subtilis glutamine synthetase

MOLECULAR MICROBIOLOGY, Issue 2 2008
Abraham L. Sonenshein
Summary Two recent papers describe the molecular mechanism by which the activity of GlnR, the repressor of the glutamine synthetase operon in Bacillus subtilis, is stimulated by glutamine-bound (i.e. feedback-inhibited) glutamine synthetase (FBI-GS). Remarkably, FBI-GS acts as a molecular chaperone to stabilize the association of GlnR dimers with their DNA binding sites. This mechanism allows the cell to shut off synthesis of GS, and hence of glutamine, when both the enzyme and its product are in excess. FBI-GS also regulates the activity of TnrA, the global regulator of nitrogen metabolism genes, but by a very different mechanism. Thus, the same enzyme,metabolite complex has two different roles in transcriptional regulation. [source]

Significance of location of enzymes on their release during microbial cell disruption

BIOTECHNOLOGY & BIOENGINEERING, Issue 5 2001
B. Balasundaram
Abstract The release kinetics of the enzyme invertase and alcohol dehydrogenase from yeast and penicillin acylase from E. coli during disruption using various techniques has been investigated. The disruption techniques used were sonication, high-pressure homogenization, and hydrodynamic cavitation. The first-order-release kinetics was applied for the determination of release rate of these enzymes and total soluble proteins. Location factor (LF) values were calculated using these release rates. The location of the enzymes as given by the values of location factor coincided well with those reported in the literature. Varying values of location factor for the same enzyme by different disruption techniques gave some indications about the selectivity of release of a target enzyme by different disruption techniques. Varying values of location factor for the same enzyme with the use of a particular equipment or disruption technique at different conditions reveals the degree to which the cell is disrupted. Few plausible applications of this location factor concept have been predicted and these speculations have been examined. This location factor concept has been used for monitoring the heat-induced translocation of ADH and location of penicillin acylase during the growth period of E. coli cells. © 2001 John Wiley & Sons, Inc. Biotechnol Bioeng 75: 607,614, 2001. [source]

Comparative sugar recovery and fermentation data following pretreatment of poplar wood by leading technologies

BIOTECHNOLOGY PROGRESS, Issue 2 2009
Charles E. Wyman
Abstract Through a Biomass Refining Consortium for Applied Fundamentals and Innovation among Auburn University, Dartmouth College, Michigan State University, the National Renewable Energy Laboratory, Purdue University, Texas A&M University, the University of British Columbia, and the University of California at Riverside, leading pretreatment technologies based on ammonia fiber expansion, aqueous ammonia recycle, dilute sulfuric acid, lime, neutral pH, and sulfur dioxide were applied to a single source of poplar wood, and the remaining solids from each technology were hydrolyzed to sugars using the same enzymes. Identical analytical methods and a consistent material balance methodology were employed to develop comparative performance data for each combination of pretreatment and enzymes. Overall, compared to data with corn stover employed previously, the results showed that poplar was more recalcitrant to conversion to sugars and that sugar yields from the combined operations of pretreatment and enzymatic hydrolysis varied more among pretreatments. However, application of more severe pretreatment conditions gave good yields from sulfur dioxide and lime, and a recombinant yeast strain fermented the mixed stream of glucose and xylose sugars released by enzymatic hydrolysis of water washed solids from all pretreatments to ethanol with similarly high yields. An Agricultural and Industrial Advisory Board followed progress and helped steer the research to meet scientific and commercial needs. © 2009 American Institute of Chemical Engineers Biotechnol. Prog., 2009 [source]