Maltose-grown Cells Research Articles

Derepression of a baker’s yeast strain for maltose utilization is associated with severe deregulation of HXT gene expression

We undertook to improve an industrial Saccharomyces cerevisiae strain by derepressing it for maltose utilization in the presence of high glucose concentrations. A mutant was obtained from an industrial S. cerevisiae strain following random UV mutagenesis and selection on maltose/5-thioglucose medium. The mutant acquired the ability to utilize glucose simultaneously with maltose and possibly also sucrose and galactose. Aerobic sugar metabolism was still largely fermentative, but an enhanced respirative metabolism resulted in a 31% higher biomass yield on glucose. Kinetic characterization of glucose transport in the mutant revealed the predominance of the high-affinity component. Northern blot analysis showed that the mutant strain expresses only the HXT6/7 gene irrespective of the glucose concentration in the medium, indicating a severe deregulation in the induction/repression pathways modulating HXT gene expression. Interestingly, maltose-grown cells of the mutant display inverse diauxy in a glucose/maltose mixture, preferring maltose to glucose. In the mutant here reported, the glucose transport step seems to be uncoupled from downstream regulation, because it seems to be unable to sense abundant glucose, via both repression and induction pathways. We report here the isolation of a S. cerevisiae mutant with a novel derepressed phenotype, potentially interesting for the industrial fermentation of mixed sugar substrates.

Impact of Substrate Glycoside Linkage and Elemental Sulfur on Bioenergetics of and Hydrogen Production by the Hyperthermophilic Archaeon Pyrococcus furiosus

Glycoside linkage (cellobiose versus maltose) dramatically influenced bioenergetics to different extents and by different mechanisms in the hyperthermophilic archaeon Pyrococcus furiosus when it was grown in continuous culture at a dilution rate of 0.45 h(-1) at 90 degrees C. In the absence of S(0), cellobiose-grown cells generated twice as much protein and had 50%-higher specific H(2) generation rates than maltose-grown cultures. Addition of S(0) to maltose-grown cultures boosted cell protein production fourfold and shifted gas production completely from H(2) to H(2)S. In contrast, the presence of S(0) in cellobiose-grown cells caused only a 1.3-fold increase in protein production and an incomplete shift from H(2) to H(2)S production, with 2.5 times more H(2) than H(2)S formed. Transcriptional response analysis revealed that many genes and operons known to be involved in alpha- or beta-glucan uptake and processing were up-regulated in an S(0)-independent manner. Most differentially transcribed open reading frames (ORFs) responding to S(0) in cellobiose-grown cells also responded to S(0) in maltose-grown cells; these ORFs included ORFs encoding a membrane-bound oxidoreductase complex (MBX) and two hypothetical proteins (PF2025 and PF2026). However, additional genes (242 genes; 108 genes were up-regulated and 134 genes were down-regulated) were differentially transcribed when S(0) was present in the medium of maltose-grown cells, indicating that there were different cellular responses to the two sugars. These results indicate that carbohydrate characteristics (e.g., glycoside linkage) have a major impact on S(0) metabolism and hydrogen production in P. furiosus. Furthermore, such issues need to be considered in designing and implementing metabolic strategies for production of biofuel by fermentative anaerobes.

Substrate inhibition kinetics of Saccharomyces cerevisiae in fed-batch cultures operated at constant glucose and maltose concentration levels

Fed-batch culture is the mode of operation of choice in industrial baker's yeast fermentation. The particular mode of culture, operated at stable glucose and maltose concentration levels, was employed in this work in order to estimate important kinetic parameters in a process mostly described in the literature as batch or continuous culture. This way, the effects of a continuously falling sugar level during a batch process were avoided and therefore the effects of various (stable) sugar levels on growth kinetics were evaluated. Comparing the kinetics of growth and the inhibition by the substrate in cultures grown on glucose, which is the preferential sugar source for Saccharomyces cerevisiae, and maltose, the most common sugar source in industrial media for baker's yeast production, a milder inhibition effect by the substrate in maltose-grown cells was observed, as well as a higher yield coefficient. The observed sugar inhibition effect in glucostat cultures was taken into account in modeling substrate inhibition kinetics. The inhibition coefficient Ki increased with increasing sugar concentration levels, but it appeared to be unaffected by the type of substrate and almost equal for both substrates at elevated concentration levels.

Sequences in the N-terminal cytoplasmic domain of Saccharomyces cerevisiae maltose permease are required for vacuolar degradation but not glucose-induced internalization

In Saccharomyces cerevisiae, glucose addition to maltose fermenting cells causes a rapid loss of maltose transport activity and ubiquitin-mediated vacuolar proteolysis of maltose permease. GFP-tagged Mal61 maltose permease was used to explore the role of the N-terminal cytoplasmic domain in glucose-induced inactivation. In maltose-grown cells, Mal61/HA-GFP localizes to the cell surface and, surprisingly, to the vacuole. Studies of end3Delta and doa4Delta mutants indicate that a slow constitutive internalization of Mal61/HA-GFP is required for its vacuolar localization. Site-specific mutagenesis of multiple serine/threonine residues in a putative PEST sequence of the N-terminal cytoplasmic domain of maltose permease blocks glucose-induced Mal61p degradation but does not affect the rapid loss of maltose transport activity associated with glucose-induced internalization. The internalized multiple Ser/Thr mutant protein co-localizes with Snf7p in a putative late endosome or E-compartment. Further, alteration of a putative dileucine [D/EExxxLL/I] motif at residues 64-70 causes a significant defect in maltose transport activity and mislocalization to an E-compartment but appears to have little impact on glucose-induced internalization. We conclude that the N-terminal cytoplasmic domain of maltose permease is not the target of the signaling pathways leading to glucose-induced internalization of Mal61 permease but is required for its subsequent delivery to the vacuole for degradation.

Whole-genome DNA microarray analysis of a hyperthermophile and an archaeon: Pyrococcus furiosus grown on carbohydrates or peptides.

The first complete-genome DNA microarray was constructed for a hyperthermophile or a nonhalophilic archaeon by using the 2,065 open reading frames (ORFs) that have been annotated in the genome of Pyrococcus furiosus (optimal growth temperature, 100 degrees C). This was used to determine relative transcript levels in cells grown at 95 degrees C with either peptides or a carbohydrate (maltose) used as the primary carbon source. Approximately 20% (398 of 2065) of the ORFs did not appear to be significantly expressed under either growth condition. Of the remaining 1,667 ORFs, the expression of 125 of them (8%) differed by more than fivefold between the two cultures, and 82 of the 125 (65%) appear to be part of operons, indicating extensive coordinate regulation. Of the 27 operons that are regulated, 5 of them encode (conserved) hypothetical proteins. A total of 18 operons are up-regulated (greater than fivefold) in maltose-grown cells, including those responsible for maltose transport and for the biosynthesis of 12 amino acids, of ornithine, and of citric acid cycle intermediate products. A total of nine operons are up-regulated (greater than fivefold) in peptide-grown cells, including those encoding enzymes involved in the production of acyl and aryl acids and 2-ketoacids, which are used for energy conservation. Analyses of the spent growth media confirmed the production of branched-chain and aromatic acids during growth on peptides. In addition, six nonlinked enzymes in the pathways of sugar metabolism were regulated more than fivefold--three in maltose-grown cells that are unique to the unusual glycolytic pathway and three in peptide-grown cells that are unique to gluconeogenesis. The catalytic activities of 16 metabolic enzymes whose expression appeared to be highly regulated in the two cell types correlated very well with the microarray data. The degree of coordinate regulation revealed by the microarray data was unanticipated and shows that P. furiosus can readily adapt to a change in its primary carbon source.

Aerobic cultivation of Streptococcus zooepidemicus and the role of NADH oxidase

A metabolic flux model was developed for Streptococcus zooepidemicus to compare the metabolism of glucose and maltose during aerobic batch cultivation. Lactic acid was the main product of glucose metabolism whereas acetic acid was the main product of maltose metabolism. This difference was chiefly attributed to the two-fold higher flux through NADH oxidase in maltose-grown cells that enabled the ATP generation rate to remain high despite a slower maltose consumption rate. The two-fold higher flux was matched by a two-fold increase in NADH oxidase activity, 2.53±0.1 μmol NADH min −1 mg −1 protein on maltose versus 1.07±0.04 μmol NADH min −1 mg −1 protein on glucose, indicating that NADH oxidase activity is regulated by the energy status of the cell. Surprisingly, the energy status of the cell had little impact on hyaluronic acid (HA) yield and molecular weight.

Maltose and maltodextrin transport in the thermoacidophilic gram-positive bacterium Alicyclobacillus acidocaldarius is mediated by a high-affinity transport system that includes a maltose binding protein tolerant to low pH.

We have studied the uptake of maltose in the thermoacidophilic gram-positive bacterium Alicyclobacillus acidocaldarius, which grows best at 57 degrees C and pH 3.5. Under these conditions, accumulation of [(14)C]maltose was observed in cells grown with maltose but not in those grown with glucose. At lower temperatures or higher pH values, the transport rates substantially decreased. Uptake of radiolabeled maltose was inhibited by maltotetraose, acarbose, and cyclodextrins but not by lactose, sucrose, or trehalose. The kinetic parameters (K(m) of 0.91 +/- 0.06 microM and V(max) ranging from 0.6 to 3.7 nmol/min/mg of protein) are consistent with a binding protein-dependent ATP binding cassette (ABC) transporter. A corresponding binding protein (MalE) that interacts with maltose with high affinity (K(d) of 1.5 microM) was purified from the culture supernatant of maltose-grown cells. Immunoelectron microscopy revealed distribution of the protein throughout the cell wall. The malE gene was cloned and sequenced. Five additional open reading frames, encoding components of a maltose transport system (MalF and MalG), a putative transcriptional regulator (MalR), a cyclodextrinase (CdaA), and an alpha-glucosidase (GlcA), were identified downstream of malE. The malE gene lacking the DNA sequence that encodes the signal sequence was expressed in Escherichia coli. The purified wild-type and recombinant proteins bind maltose with high affinity over a wide pH range (2.5 to 7) and up to 80 degrees C. Recombinant MalE cross-reacted with an antiserum raised against the wild-type protein, thereby indicating that the latter is the product of the malE gene. The MalE protein might be well suited as a model to study tolerance of proteins to low pH.

High-affinity maltose binding and transport by the thermophilic anaerobe Thermoanaerobacter ethanolicus 39E.

Thermoanaerobacter ethanolicus is a gram-positive thermophile that produces considerable amounts of ethanol from soluble sugars and polymeric substrates, including starch. Growth on maltose, a product of starch hydrolysis, was associated with the production of a prominent membrane-associated protein that had an apparent molecular weight of 43,800 and was not detected in cells grown on xylose or glucose. Filter-binding assays revealed that cell membranes bound maltose with high affinity. Metabolic labeling of T. ethanolicus maltose-grown cells with [(14)C]palmitic acid showed that this protein was posttranslationally acylated. A maltose-binding protein was purified by using an amylose resin affinity column, and the binding constant was 270 nM. Since maltase activity was found only in the cytosol of fractionated cells and unlabeled glucose did not compete with radiolabeled maltose for uptake in whole cells, it appeared that maltose was transported intact. In whole-cell transport assays, the affinity for maltose was approximately 40 nM. Maltotriose and alpha-trehalose competitively inhibited maltose uptake in transport assays, whereas glucose, cellobiose, and a range of disaccharides had little effect. Based on these results, it appears that T. ethanolicus possesses a high-affinity, ABC type transport system that is specific for maltose, maltotriose, and alpha-trehalose.

SUGAR UPTAKE AND SUBSEQUENT ESTER AND HIGHER ALCOHOL PRODUCTION BYSACCHAROMYCES CEREVISIAE

The production of a number of esters and higher alcohols by brewing strains of Saccharomyces cerevisiae, in synthetic media containing only glucose, fructose or maltose as sole carbohydrate source, has been investigated. Results indicated that production of most volatiles was generally lower when maltose was the sugar being fermented, despite maltose-grown cells having higher viabilities and vitalities than glucose or fructose-grown cells. There was no significant difference in the levels of esters and higher alcohols produced during fermentation when glucose or fructose was metabolised, although strain variation was observed. Similar results were obtained when wort was supplemented with either glucose, fructose or maltose. Wort supplemented with maltose produced fewer volatiles, especially higher alcohols, than that which had a hexose sugar added. The activity of ester-synthesising enzymes present in glucose or maltose PYN grown cells was also examined. Similar levels of ethyl acetate and isoamyl acetate were obtained when cells grown in either glucose or maltose PYN were disrupted and ester production monitored. The implications of these results for the fermentation of high-gravity worts are discussed.

Glycogen Formation by the Ruminal Bacterium Prevotella ruminicola

Prevotella ruminicola is an important ruminal bacteria. In maltose-grown cells, nearly 60% of cell dry weight consisted of high-molecular-weight (>2 x 10(sup6)) glycogen. The ratio of glycogen to protein (grams per gram) was relatively low (1.3) during exponential growth, but when cell growth slowed during the transition to the stationary phase, the ratio increased to 1.8. As much as 40% of the maltose was converted to glycogen during cell growth. Glycogen accumulation in glucose-grown cells was threefold lower than that in maltose-grown cells. In continuous cultures provided with maltose, much less glycogen was synthesized at high (>0.2 per h) than at low dilution rates, where maltose was limiting (28 versus 60% of dry weight, respectively). These results indicated that glycogen synthesis was stimulated at low growth rates and was also influenced by the growth substrate. In permeabilized cells, glycogen was synthesized from [(sup14)C]glucose-1-phosphate but not radiolabelled glucose, indicating that glucose-1-phosphate is the initial precursor of glycogen formation. Glycogen accumulation may provide a survival mechanism for P. ruminicola during periods of carbon starvation and may have a role in controlling starch fermentation in the rumen.

The influence of limiting and non-limiting growth conditions on glucose and maltose metabolism in Lactococcus lactis ssp. lactis strains

Three strains of Lactococcus lactis ssp. lactis, a dairy strain 65.1, a type strain ATCC 19435, and a mutant AS 211, were grown on glucose and on maltose under chemostat conditions. When the culture was shifted from glucose-limiting to non-limiting conditions, the product shifted from mixed acids to lactate. Mixed acids were obtained in all maltose cultures; however, an enhanced lactate formation was observed in 19435 and AS 211. An inorganic-phosphate (Pi)-dependent maltose phosphorylase activity was found to be responsible for the initial conversion of maltose. The activation of maltose phosphorylase by Pi was strain-specific. When growth was on maltose under non-limiting conditions, a correlation was found between high initial maltose phosphorylase and β-phosphoglucomutase activities and lactate production. No such correlation was observed in maltose-limited cells. In glucose-grown cells under non-limiting conditions, homo-fermentative lactate formation coincided with high concentrations of fructose 1,6-bisphosphate (Fru1,6P2) and pyruvate (Pyr) and low concentrations of phosphoenolpyruvate (PPyr). Under limiting conditions, mixed acid formation coincided with low concentrations of Fru1,6P2 and Pyr and high concentrations of PPyr. In maltose-grown cells there was no correlation between intracellular intermediary metabolite concentrations and product formation. Therefore, in addition to intracellular intermediary metabolite concentrations, the product formation on maltose is suggested to be regulated by the transport and initial phosphorylating steps.

Repression of glucose uptake in maltose-grown cells ofSaccharomyces bayanus IGC 4565

Repression of glucose uptake in maltose-grown cells ofSaccharomyces bayanus IGC 4565

Glucose fermentation to acetate and alanine in resting cell suspensions ofPyrococcus furiosus: Proposal of a novel glycolytic pathway based on13C labelling data and enzyme activities

Abstract Suspensions of maltose-grown cells of the hyperthermophilic archaeon Pyrococcus furiosus , when incubated at 90°C with 35 mM [1- 13 C]glucose or [3- 13 C]glucose, consumed glucose at a rate of about 10 nmol min −1 (mg protein) −1 . Acetate (10 mM), alanine (3 mM), CO 2 and H 2 were the fermentation products. The 13 C-labelling pattern in alamine and acetate were analyzed. With [1- 13 C]glucose the methyl group of both alanine and acetate was labelled; with [3- 13 C]glucose only the carboxyl group of alanine was labelled whereas acetate was unlabelled. Extracts of maltose-grown cells contained glucose isomerase (12.8 U mg −1 , 100°C), ketohexokinase (0.23 U mg −1 , 100°C), and fructose 1-phosphate aldolase (0.06 U mg −1, 100°C). Enzymes catalyzing the formation of fructose 1,6-bisphosphate from fructose 1-phosphate or fructose 6-phosphate could not be detected. As publihed previously by our group and other authors P. furiosus also contains enzymes of glyceraldehyde conversion to 2-phosphoglycerate according to a non-phosphorylated Entner-Doudoroff pathway, of dihydroxyacetone phosphate conversion to 2-phosphoglycerate according to the Embden-Meyerhof pathway, and of 2-phosphoglycerate conversion - via pyruvate - to acetate and alanine. Based on the enzyme activities in P. furiosus , the following pathway for glucose degradation to alanine and acetate in cell suspensions is proposed which can explain the [ 13 C]glucose labelling data: glucose→ fructose → fructose 1- phosphate → dihydroxyacetone phosphate + glyceraldehyde and further conversion of both trioses to alanine and acetate via pyruvate.

Mechanism of maltose uptake and glucose excretion in Lactobacillus sanfrancisco

Lactobacillus sanfrancisco LTH 2581 can use only glucose and maltose as sources of metabolic energy. In maltose-metabolizing cells of L. sanfrancisco, approximately half of the internally generated glucose appears in the medium. The mechanisms of maltose (and glucose) uptake and glucose excretion have been investigated in cells and in membrane vesicles of L. sanfrancisco in which beef heart cytochrome c oxidase had been incorporated as a proton-motive-force-generating system. In the presence of ascorbate, N,N,N',N'-tetramethyl-p-phenylenediamine (TMPD), and cytochrome c, the hybrid membranes facilitated maltose uptake against a concentration gradient, but accumulation of glucose could not be detected. Similarly, in intact cells of L. sanfrancisco, the nonmetabolizable glucose analog alpha-methylglucoside was taken up only to the equilibration level. Selective dissipation of the components of the proton and sodium motive force in the hybrid membranes indicated that maltose is transported by a proton symport mechanism. Internal [14C]maltose could be chased with external unlabeled maltose (homologous exchange), but heterologous maltose/glucose exchange could not be detected. Membrane vesicles of L. sanfrancisco also catalyzed glucose efflux and homologous glucose exchange. These activities could not be detected in membrane vesicles of glucose-grown cells. The results indicate that maltose-grown cells of L. sanfrancisco express a maltose-H+ symport and glucose uniport system. When maltose is the substrate, the formation of intracellular glucose can be more rapid than the subsequent metabolism, which leads to excretion of glucose via the uniport system.

Identification of the Maltose Transport Protein of Saccharomyces cerevisiae

Identification of the maltose transport protein of Saccharomyces cerevisiae was attempted by searching for maltose-inducible proteins in isolated plasma membranes. Membranes from maltose-grown cells contained two proteins that were absent in glucose-grown cells. The proteins differed in size, but peptide sequence analysis indicated a high degree of homology. The amino-terminal and internal sequences of the largest protein, with an apparent molecular mass of 64 kDa, were determined. These sequences were identical to predicted amino acid sequences in the MAL61 gene product. It is concluded that this protein is the inducible maltose permease of Saccharomyces cerevisiae.

β-Glucose-1-Phosphate, a Possible Mediator for Polysaccharide Formation in Maltose-Assimilating Lactococcus lactis

Homolactic fermentation of glucose and heterolactic fermentation of maltose with Lactococcus lactis 65.1 were confirmed. When moles of glucose were compared, the uptake rates of the two carbon sources were similar. The intracellular concentration of fructose-1,6-diphosphate (FDP) in maltose-assimilating cells was half of that in glucose-assimilating cells. Similarly, formation of FDP and lactate from maltose by extracts of maltose-grown cells was half of that formed from glucose by extracts of glucose-grown cells, indicating a difference in the utilization of the two carbon sources for energy metabolism. Concentrations of adenine nucleotides were similar in both types of cells. Glucose-1-phosphate was found in extracts of maltose-grown cells given maltose and, in addition, an inducible and low beta-specific phosphoglucomutase activity was observed. beta-Glucose-1-phosphate was not metabolized by cell extracts to either FDP or lactate, suggesting an alternative metabolic route. The amount of [C]maltose incorporated into the cell material of maltose-grown cells was four times greater than that of [C]glucose incorporated into the cell material of glucose-grown cells. The intracellular concentration of UTP was lower in maltose-assimilating cells than in glucose-assimilating cells. Cells grown on maltose were more spherical and less fragile than cells grown on glucose.

Amylase secretion by sweet potato, Ipomoea batatas (L.) Lam., cell cultures grown on various carbon sources

Cell cultures of sweet potato grown in media containing sucrose, glucose, maltose, or starch secreted amylase into the growth medium. The growth rate of cells was not appreciably affected by the carbon source employed for growth, although cells grown on sucrose had a slightly longer lag period before exponential growth occurred. Amylase levels inside the cells were not affected by carbon source, but the amount of amylase released into the medium was drastically affected. Maltose-grown cells released the most amylase while sucrose-grown cells released the least. Cells grown in the light released about twice as much amylase as cells grown in the dark when grown on glucose, maltose, or starch. Three amylase electrophoretic forms were found in the storage root tissue from which all cultures were derived. Cells grown in culture exhibited either two or three amylase forms, depending on the carbon source. The slowest migrating root amylase was found only in cells grown on starch. The root amylase having intermediate mobility was present in all cultures, as was a form having higher mobility than the most mobile root form. The fastest migrating electrophoretic form from the root was not present in any of the cells.

Interrelationship of the phage λ receptor protein and maltose transport in mutants of Escherichia coli K12

1. (1) The λ receptor protein in maltose-induced cells of Escherichia coli K12 is a major protein of the outer membrane and therefore amounts to about 100 000 copies per cell. 2. (2) 17 λ-resistant derivatives of the λ-sensitive strain E. coli W3110 were isolated independently; all were impaired in maltose transport and showed a much lower growth rate on maltotriose except one mutant, E. coli W3110/21 which resembled the wild type parent in that it grew equally fast on maltotriose and maltose. All mutants lacked the λ receptor protein. 3. (3) The presence of the maltose-inducible λ receptor protein in the missense mutant E. coli CR63 was demonstrated by SDS-gel electrophoresis of isolated outer membranes. The molecular weight of 47 000 daltons corresponded to the size of the wild type receptor protein. Four derivative strains with additional lamB mutations were obtained by selecting for mutants resistant to a λ phage with an extended host range (λh). They all grew equally fast on maltose and maltotriose but only one contained as much λ receptor protein as the original strain. There was no correlation between the amount of residual receptor protein in these mutants and the initial rate of transport which ranged from 13 to 47% of the transport rate of the parent strain E. coli CR63. 4. (4) Maltose-1-phosphate, trehalose, melibiose, sucrose, raffinose, and cellobiose at 2 mM up to 11 mM concentrations did not compete with maltose uptake. Growth of cells on trehalose of melibiose induced the maltose transport system to 20 or 7%, respectively, of the level observed in maltose-grown cells, measured as initial rate of maltose uptake.

The adsorption of coliphage lambda to its host: Effect of variations in the surface density of receptor and in phage-receptor affinity

When measured in the presence of optimal concentrations of cations (2 × 10 −3 mMg 2+ for instance), the rate of adsorption of phage lambda to cells of Escherichia coli K12 increases only about tenfold when the density of receptor protein at the cell surface increases from about 30 molecules per cell (glucose-grown cells) to 6000 molecules per cell (maltose-grown cells). At low densities of receptor, variations in the concentration of divalent cations affect the rate of phage adsorption in the same way as they affect phage-receptor affinity in vitro. In particular the rate of adsorption is very much decreased when the concentration of Mg 2+ ions is increased to 2 × 10 −2 m. This is not true, however, when the density of receptor is high, in which case an increase in the concentration of Mg 2+ ions to 2 × 10 −2 m only slightly decreases the rate of adsorption. An interpretation for these facts is proposed, which takes into account the geometrical and physical properties of the elements involved, as well as the known characteristics of phage-receptor interaction in vitro. This interpretation relates phage adsorption to the more general problem of membrane-ligand interaction.

The Maltose Metabolism of Trichomonas gallinae (Rivolta, 1878): I. Growth Studies

The effect of glucose and maltose on the growth of Trichomonas gallinae in STS and CPLM medium was compared. T. gallinae was found to grow faster and attain greater cell numbers with maltose in STS medium. Growth rates were the same for both sugars in CPLM medium but greater total num- bers were attained by maltose-grown cells. Cells grown in maltose with both media were found to be larger in cell size and weight. This difference could be detected photometrically. Protein content/cell was not found to differ significantly between the maltose- and glucose-grown cells. Addition of glucose to maltose-STS medium decreases the maltose growth potential. A strain of T. gallinae diauxic to glu- cose and maltose in STS medium is also reported. Several authors have noted that the disaccha- ride maltose gives greater growth to certain trichomonad species than its constituent hexose, glucose. Trussel and Johnson (1941), in de- veloping a medium for Trichomonas vaginalis, found that maltose gave better growth than glucose as the supplemental carbohydrate in terms of cell numbers at 3 to 4 days. Honig- berg and Pierce (1963) reported in abstract (no data) that maltose was more stimulatory for growth than glucose in simplified Trypti- case medium for one strain of Trichomonas