1,720,960 research outputs found
Going Beyond Counting First Authors in Author Co-citation Analysis
Full text linkThe present study examines one of the fundamental aspects of author co-citation analysis (ACA) - the way co-citation
counts are defined. Co-citation counting provides the data on which all subsequent statistical analyses and mappings
are based, and we compare ACA results based on two different types of co-citation counting - the traditional type that
only counts the first one among a cited work's authors on the one hand and a non-traditional type that takes into
account the first 5 authors of a cited work on the other hand. Results indicate that the picture produced through this non-traditional author co-citation counting contains more coherent author groups and is therefore considerably clearer. However, this picture represents fewer specialties in the research field being studied than that produced through the traditional first-author co-citation counting when the same number of top-ranked authors is selected and analyzed. Reasons for these effects are discussed
Variations on the Author
Full text link“Variations on the Author” discusses two of Eduardo Coutinho’s recent films (Um Dia na Vida, from 2010, and Últimas Conversas, posthumously released in 2015) and their contribution to the general question of documentary authorship. The director’s filmography is characterized by a consistent yet self-effacing form of authorial self-inscription: Coutinho often features as an interviewer that rather than express opinions propels discourses; an interviewer that is good at listening. This mode of self-inscription characterizes him as an author who is not expressive but who is nonetheless markedly present on the screen. In Um Dia na Vida, however, Coutinho is completely absent form the image, while Últimas Conversas, on the contrary, includes a confessional prologue that moves the director from the margins to the center of his films. This article examines the ways in which these works stand out in the filmography of a director who offers new insights into the notion of cinematic authorship
Appropriate Similarity Measures for Author Cocitation Analysis
Full text linkWe provide a number of new insights into the methodological discussion about author cocitation analysis. We first argue that the use of the Pearson correlation for measuring the similarity between authors’ cocitation profiles is not very satisfactory. We then discuss what kind of similarity measures may be used as an alternative to the Pearson correlation. We consider three similarity measures in particular. One is the well-known cosine. The other two similarity measures have not been used before in the bibliometric literature. Finally, we show by means of an example that our findings have a high practical relevance.information science;Pearson correlation;cosine;similarity measure;author cocitation analysis
Optimization of Culture Media Parameters of Saccharomyces Cerevisiae PTCC 5209 for Maximized Invertase Enzyme Production
Full text linkBackground and Objective: Invertase enzyme or D-fructofuranosidfructohydrolase EC (3.2.1.26) is a member of the hydrolase family and responsible for the decomposition of sucrose into fructose and glucose. In recent years, extensive research has been carried out to increase the industrial production of invertase enzyme.
Material and Methods: This study focused on maximizing invertase production in Saccharomyces cerevisiae by optimizing culture media conditions. Elements of the culture media were investigated using monofunctional optimization method. Moreover, basic salt culture media, containing compounds such as Na₂HPO₄, K₂HPO₄, MgSO₄ and CaCl₂, were used. Then, growth curve of the yeast was plotted and results showed that the highest growth rate occurred within 38 h and the strongest enzyme activity occurred within 18 h. Optimizing the culture conditions showed that yeast provided the most activity with 1% sucrose as a carbon source, urea and 0.5% meat peptone as nitrogen sources, pH 5, 30 °C and shaking speed of 150 rpm. In this research, 3-l fermentor was used to assess yeast growth and enzyme activity at a larger scale.
Results and Conclusion: Results of this study showed that the highest OD value was included at 48 h and the highest enzyme activity was recorded at 28 and 96 h. The difference between the time of maximum growth and peak enzyme activity indicated the need of careful control of fermentation time to prevent unnecessary biomass accumulation. Therefore, further research in the field of advanced fermentation and optimization of yeast strains can help researchers achieve the highest secretion and enzyme activity.
Keywords: Invertase, Optimization, Saccharomyces cerevisiae PTCC 5209, Yeast fermentation
Introduction
Enzymes are macromolecules that play a critical role in enabling the chemical transformations needed for sustaining biological processes. Enzymes are classified based on the types of reactions they catalyze, reflecting their diverse catalytic activities [1]. Enzymes are used in several industrial processes, including baking, brewing, detergents, fermented products, pharmaceuticals, textiles and leather processing and include a crucial role in the pharmaceutical and diagnostic industries [2]. One of the enzymes that has been most discussed in recent years is the invertase enzyme. Invertase (D-fructofuranosid fructohydrolase, EC 3.2.1.26) catalyzes the hydrolysis of the α-1,4-glycosidic bonds between D-glucose and D-fructose in sucrose and transfers the αβ-D-O-fructofuranoside residue to an acceptor substrate [3]. Thus, invertase functions under high sucrose concentrations showing transferase activity. This dual characteristic classifies it within the group of transferases, referred to as fructosyltransferases (EC 2.4.1.9) [4]. In addition, invertase can hydrolyze other oligosaccharides, including kestose, raffinose and stachyose [5]. Nowadays, invertase is widely used for commercial purposes in various industries such as foods, beverages, pharmaceuticals and biosensors. It facilitates the conversion of sucrose and linked glycosides into simple commercial carbohydrates. Saccharomyces sp. invertase is the most common commercial source, compared to others. Yeast invertase is a β-fructosidase, whereas the fungus produces an α-glucosidase type of invertase. These two types of invertase include various catalytic mechanisms. The β-fructosidase hydrolyzes the sucrose from the fructose end, while the α-glucosidase hydrolyzes sucrose from the glucose end. The two reactions yield a mixture named invert syrup, which consists of glucose and fructose. Due to the high sweetness of fructose, the invert syrup is much sweeter than sucrose. Fructose is more appropriate than glucose for diabetic patients and enhances iron absorption in children [6]. The generally recognized as safe (GRAS) S. cerevisiae is a preferred protein-production host due to its well-understood genetics, collection of molecular biology tools that enable precise strain engineering and significant tolerance to industrial and chemical stresses [7]. First, invert sugar was produced using chemical method by the hydrolysis of sucrose with acid. Before identification of the invertase enzyme this method was highly used; however, acid hydrolysis of sucrose includes several disadvantages such as byproduct generation and low efficiency, limiting its industrial uses [8]. Invertase is a glycoprotein rich in mannose residues that belongs to the glycoside hydrolase (GH) family and consists of 370 enzymes [9]. Various isoforms with distinct characteristics of invertase are located in various parts of the cell and produced in intracellular and extracellular forms [10]. The major strain for the production of the invertase enzyme for the industries is S. cerevisiae [11]. In addition to its ability to catalyze and hydrolyze several sugars, invertase is capable of degrading numerous chemical compounds such as rhamnose and stachyose. As the first known protein in the role of biological catalysts, this enzyme has formed one of the most fundamental principles in enzymology. This characteristic has led to suggest invertase as a basis for the development of various models used in the study of enzyme reaction kinetics [12]. Previous studies' major focus was on conventional yeast strains and standard fermentation conditions, focusing primarily on basic production and biochemical characterization [3, 4]. Optimization of culture conditions, particularly nitrogen sources, has been verified as effective in enhancing enzyme yield [13]. The goal of this research was to enhance invertase activity. Invertase production and activity highly depend on the microbial strain, culture media and environmental conditions. However, systematic assessment of S. cerevisiae PTCC 5209 with optimized nitrogen sources is limited. This study demonstrated that combining this strain with two nitrogen sources enhanced the enzyme yield, while Amicon ultrafiltration efficiently concentrated the enzyme. The novelty of this study was linked to the combined approach of strain selection and nutritional optimization, including use of a combination of nitrogen sources, to maximize invertase production under controlled culture conditions.
Materials and Methods
2.1. Materials
Chemicals and mineral salts in this study included carbon sources of molasses (Brix 80, Jahan Alcohol, Iran) and sucrose (Merck, Germany); nitrogen sources of yeast extract (Leiber, Germany), meat peptone (Sigma-Aldrich, Germany), urea (pharmaceutical grade; Behansar, Iran) and diammonium phosphate (Merck, Germany); mineral salts of calcium chloride (Merck, Germany), magnesium sulfate (Merck, Germany), disodium hydrogen phosphate (Merck-DNA Biotech, Germany), dipotassium hydrogen phosphate (Merck, Germany), sodium potassium tartrate (Merck, Germany) and sodium acetate trihydrate (Merck, Germany); agar (Ibresco, Germany); sodium hydroxide (Merck, Germany); and glucose ( Merck, Germany).
2.2. Microorganism
The yeast strain of S. cerevisiae PTCC 5209 was provided by the Persian Type Culture Collection (PTCC, Iran). The strain was cultivated in yeast peptone dextrose adenine (YPDA) media (pH 5). For further experiments, glycerol stocks and slants were prepared.
2.3. Media
For enzyme production, the optimized culture media contained Na₂HPO₄ (2.5 g l-1), K₂HPO₄ (2.5 g l-1), meat peptone (10 g l-1), MgSO₄ (0.05 M) and CaCl₂ (0.01 M). The primary pH of the media was adjusted to 5.0 before sterilization.
2.4. Invertase assay
The culture media were centrifuged at 9,000 rpm for 20 min at 4 °C and the supernatant was collected as the crude enzyme source for the invertase assay. Invertase activity was investigated by measuring the quantity of reducing sugars released from sucrose using DNS method according to Miller [14]. The reaction mixture contained 0.4 ml of 1% (w/v) sucrose as substrate, 1.2 ml of 0.1 M acetate buffer (pH 5.0) and 0.4 ml of the crude enzyme supernatant. The mixture was incubated at room temperature (RM) for 30 min. After incubation, 0.25 ml of the reaction mixture was added to 1 ml of DNS reagent to terminate the reaction and the tubes were boiled for 10 min using water bath. After cooling to RM, the absorbance was measured at 540 nm using UV-vis spectrophotometer. One unit of invertase activity was reported as the quantity of enzyme needed to release 1 µmol of glucose per minute under the assay conditions.
2.5. Invertase activity calculation
Enzyme activity (mol min-1 ml-1) or (U ml-1) =
2.6. Carbon source optimization
Two carbon sources were assessed to investigate the optimal substrate for invertase production, including molasses with a Brix of 80 and sucrose. The culture media were supplemented with either 1% (v/v) molasses or 1% (w/v) sucrose and the pH was adjusted to 5.0. Each 250-ml flask containing 100 ml of the media was inoculated with S. cerevisiae and incubated at 30 °C for 24 h at 150 rpm using shaker incubator.
2.7. Sucrose concentration optimization
The culture media were prepared with various concentrations of sucrose ranging from 1 to 4% (w/v) to optimize invertase production [15]. With pH 5 in 250-ml flasks, culture media were inoculated with S. cerevisiae and incubated at 30 °C for 24 h at 150 rpm using shaker incubator.
2.8. Nitrogen source optimization
Four nitrogen sources were selected to investigate the best nitrogen source for invertase activity. These nitrogen sources were urea, yeast extract, meat peptone [16] and diammonium phosphate (DAP). The culture media were supplemented with 1% (w/v) of each nitrogen source and pH was adjusted to 5.0. Each 250-ml flask containing 100 ml of the media was inoculated with S. cerevisiae and incubated at 30 °C for 24 h at 150 rpm using shaker incubator.
2.9. Combination nitrogen source optimization
To enhance invertase production, various combinations of nitrogen sources were assessed, including 0.5% yeast extract and 0.5% meat peptone, 0.5% urea and 0.5% meat peptone, 0.5% urea and 0.5% yeast extract, and 0.5% yeast extract and 0.5% diammonium phosphate. Each combination was prepared in 100 ml of the culture media (pH adjusted to 5.0) using 250-ml flasks, inoculated with S. cerevisiae and incubated at 30 °C for 24 h at 150 rpm using shaker.
2.10. Optimization pH
Briefly, 100 ml of the production media were distributed into each 250-ml flask and pH was adjusted to 3, 4, 5, 6, 7 and 8 [17]. These were inoculated with S. cerevisiae and incubated at 30 °C for 24 h at 150 rpm using shaker incubator. Then, the supernatant was used for enzyme assay and investigation of invertase activity.
2.11. Acetate buffer pH optimization
To investigate that at what pH the enzyme was most active, acetate buffer was prepared at various pH levels between 4 and 7 and enzyme activity was assessed using enzyme assay with the acetate buffer at various pH levels.
2.12. Shaker incubator rpm optimization
To investigate the effect of the rpm of the shaker incubator on enzyme activity, the culture media containing microorganisms were incubated at 30 °C for 24 h at 150 and 160 rpm after inoculation, and enzyme activity was assessed, as described in the previous steps.
2.13. Shaker incubator temperature optimization
To investigate the Optimal shaker temperature to achieve higher enzyme activity, the culture media containing microorganisms were transferred into shakers at 25, 30 and 32 °C and 150 rpm after inoculation. After 24 h, enzyme assay was used as previously described.
2.14. Growth curve and enzyme activity
Yeast growth and invertase activity were monitored over 48 h. Cell growth was assessed spectrophotometrically at 600 nm every 2 h and the growth curve was plotted. Enzyme activity was investigated approximately every 4 h using standard invertase assay with each measurement carried out in duplicate (n = 2). Results were reported as mean ±SD (standard deviation).
2.15. Effects of temperature on enzyme activity
The crude enzyme from the supernatant was incubated at 30 to 90 °C for 30 min using water bath [18]. Enzyme activity was then assessed using standard invertase assay and absorbance of the samples was read at 540 nm.
2.16. Effects of substrate concentration and kinetic parameters (Michaelis-Menten equation)
The effect of substrate concentration on invertase activity was assessed using sucrose at final concentrations ranging from 0 to 300 mM under standard assay conditions. The reactions were carried out at constant temperatures of 30 and 50 °C. Kinetic parameters, including the Michaelis-Menten constant (Km) and the maximum reaction rate (Vmax), were calculated using non-linear regression analysis and Michaelis-Menten model.
2.17. The SMF fermentor
To assess enzyme production at a larger scale, fermentation was carried out using 3-l laboratory-scale bioreactor (working volume of 2.0 l; Zist Fan Sanat Iranian, Iran). The bioreactor was equipped with a Rushton-type impeller, an air sparger and automatic control systems for temperature, pH and dissolved oxygen (DO). Fermentation was carried out at 30 °C with pH 5.0. The culture was agitated at 150 rpm and continuously aerated with sterile air, while DO was set at approximately 5 mg l-1 throughout the process to ensure adequate oxygen transfer and homogeneous mixing. To minimize the risk of contamination, no sampling was carried out during the first 24 h after inoculation. Then, samples were collected at regular intervals to investigate yeast growth (OD₆₀₀) and invertase activity and growth and enzyme activity profiles were recorded. For each sample, OD₆₀₀ was measured in duplicate (technical replicates) to monitor cell growth and invertase activity was assessed in duplicate. Data were present as mean ±SD and error bars in figures represented SD.
2.18. Amicon (ultra centrifugal filter of 10 kDa)
Briefly, 10-kDa Amicon ultrafiltration was used to concentrate the crude invertase enzyme and simultaneously remove low-molecular-weight (LMW) salts and other solutes in the supernatant. The enzyme solution was processed according to the manufacturer’s instructions and the concentrated enzyme was collected for activity assays.
2.19. Statistical analysis
All experiments, except fermentation studies, were carried out in duplicate as independent biological replicates (n = 2). Enzyme activity for each replicate was calculated individually and results were present as mean ±SD. For fermentation samples, only one fermentor was used; each sample was assessed in duplicate (technical replicates) and OD₆₀₀ and enzyme activity were reported as mean ±SD. Michaelis-Menten plots were generated using GraphPad Prism 8 (GraphPad, USA) and the mean values of duplicate measurements. Standard deviations were not included in the fitting analysis since averaged values were used for each substrate concentration.
Results and Discussion
3.1. Carbon source optimization
After 24 h of yeast incubation in culture media containing 1% molasses or 1% sucrose as carbon sources, enzyme activity was assessed to investigate the most suitable substrate. Sucrose was selected as the optimal carbon source since molasses interfered with the DNS assay due to its strong reaction with the reagent, making accurate quantification of enzyme activity unreliable.
3.2. Sucrose concentration optimization
After selecting sucrose as the preferred carbon source for enzyme production, various concentrations of sucrose (1–4% w/v) were assessed to investigate the optimal level for maximum enzyme activity. The results showed that the highest enzyme activity was achieved at 1% sucrose.
3.3. Nitrogen source optimization
Culture media containing yeast extract, meat peptone, urea and diammonium phosphate (DAP) were assessed as nitrogen sources. After 24 h of incubation, the enzyme assay results showed that the media containing pharmaceutical-grade urea as the nitrogen source included the highest invertase activity.
3.4. Combination of nitrogen sources
To enhance enzyme production, various combinations of nitrogen sources were assessed. After 24 h of incubation, the results indicated that the media containing a combination of meat peptone and pharmaceutical-grade urea included the highest invertase activity.
3.5. Media pH optimization
Media of various pH levels between 3 and 8 were prepared. After 24 h of yeast inoculation and enzyme assay, the culture media with pH of 5 included the highest enzyme activity. At pH 7 and pH 8, enzyme activity could not be assessed due to the precipitation in the culture media.
3.6. The pH acetate buffer
The buffer used in the assay included acetate buffer. To achieve and ensure the appropriate pH for the invertase enzyme, buffers with various pH levels between 3 and 7 were prepared. Then, the enzyme assay was carried out. The invertase enzyme showed the highest activity at pH 5.
3.7. The rpm optimization
To assess the effects of agitation speed on enzyme activity, shaking rates of 150 and 160 rpm were assessed. The results showed that the culture agitated at 150 rpm included the highest invertase activity.
3.8. Shaker incubator temperature optimization
After inoculation, the culture flasks were incubated at 25, 30 and 35 °C for 24 h. Enzyme assay results showed that the highest invertase activity was achieved at 30 °C.
3.9. Growth curve and enzyme activity curve
The growth and enzyme activity curves were monitored over 48 h by measuring cell growth (OD₆₀₀) every 2 h and invertase activity approximately every 4 h, except during the early stage of inoculation, when enzyme secretion did not begin. The growth curve showed two distinct logarithmic phases, likely due to the presence of dual nitrogen sources in the media. The highest enzyme activity was observed at 18 and 48 h, while the maximum optical density (OD₆₀₀) occurred at 38 h. These results indicate that the peak enzyme secretion did not coincide with the time of maximum yeast growth (biomass accumulation).
3.10. Fermentor
During the first 24 h of fermentation, no sampling was carried out to minimize the risk of contamination. After this time, samples were collected at regular intervals to monitor cell growth and enzyme activity. The highest optical density (OD₆₀₀) was recorded at 48 h, while the maximum invertase activity occurred at 28 and 96 h. Similar to the shake-flask experiments, the peak of enzyme activity did not match with the maximum cell growth, indicating that invertase secretion was not directly correlated with the biomass accumulation.
3.11. Effects of temperature
The crude enzyme was incubated at 30, 40, 60, 70 and 90 °C for 30 min, followed by activity measurement using standard assay. The highest invertase activity was observed within the temperature range of 40–60 °C, with similar activity levels at 40 and 60 °C, indicating that the enzyme preserved its substantial stability and catalytic efficiency across this range.
3.12. Michaelis-Menten equation
The Michaelis–Menten parameters of invertase were investigated through non-linear regression at 30 and 50 °C, as summarized in Table 1. At 30 °C, the Km and Vmax values were 63.35 mM and 0.8557 µmol min-1, respectively. At 50 °C, Km increased to 124.2 mM and Vmax to 2.283 µmol min-1. The higher Km at 50 °C indicated decreased affinity of invertase for sucrose at increased temperatures, suggesting that structural changes or increased flexibility of the enzyme at higher temperatures might affect substrate binding. The increase in Vmax at 50 °C showed that the catalytic rate could increase at higher temperatures; however, the overall efficiency was moderated by the decreased substrate affinity.
3.13. Amicon ultra centrifugal filter
In this study, Amicon 10-kDa filter was used to concentrate the enzyme. Before centrifugation, the volume in the tube was 3.5 ml and after centrifugation, the rest of volume in the Amicon filter was 1.4 ml; hence, this was 2.5 times further concentrated.
The results of this study showed that the yeast reached its highest growth rate within 38 h, while the best enzyme activity was seen within 18 h, highlighting the fact that enzyme secretion was not strictly coupled to growth, a phenomenon reported for S. cerevisiae MK, where the maximum invertase production occurred at 48 h while biomass increased up to 96 h [19]. These observations highlighted the importance of optimizing harvest time to achieve maximal enzyme yield. Such differences highlighted the importance of selecting the optimal harvest time to maximize enzyme activity. The present results, including that the invertase enzyme pH optimization was 5, were similar to those of Al-Saady’s study [16] but differed from Shankar's study [18], where maximum activity was observed at pH 6 for invertase from S. cerevisiae MTCC 170, suggesting that strain-specific variations in invertase isoforms or differences in post-translational modifications and culture conditions such as media composition, temperature and aeration might further affect the pH profile. In 2024, Dokuzparmak investigated the effect of pulp on the activity of the invertase enzyme in S. cerevisiae and the results showed that the invertase enzyme activity increased by 2.5 times. In the current study, a combination of 1% sucrose, 0.5% urea and meat peptone at pH 5 and 30 °C and 150 rpm yielded the highest enzyme activity, aligning with Dokuzparmak’s findings under comparable conditions [20]. However, it is noteworthy that the optimization was carried out using one-factor-at-a-time (OFAT) approach, which did not account for potential interactions between the factors. For example, the optimal sucrose concentration investigated by one nitrogen source may shift, when a various nitrogen source is used. Future studies can use factorial design or response surface methodology (RSM) to investigate such interactions and achieve f
Dispelling the Myths Behind First-author Citation Counts
Full text linkWe conducted a full-scale evaluative citation analysis study of scholars in the XML research field to explore just how different from each other author rankings resulting from different citation counting methods actually are, and to demonstrate the capability of emerging data and tools on the Web in supporting more realistic citation counting methods. Our results contest some common arguments for the continued
use of first-author citation counts in the evaluation of scholars, such as high correlations between author rankings by first-author citation counts and other citation
counting methods, and high costs of using more realistic citation counting methods that are not well-supported by the ISI databases. It is argued that increasingly available digital full text research papers make it possible for citation analysis studies to go beyond what the ISI databases have directly supported and to employ more
sophisticated methods
koamabayili/VECTRON-author-checklist: VECTRON author checklist
No full textWe have done our best to complete the author checklist relating to the use of animals in the hut study. Note that the objective for the hut study was to evaluate the IRS treatment applications for residual efficacy against Anopheles mosquitoes, including the local An. coluzzii mosquito population. Cows were only used to attract mosquitoes into the huts and no tests were carried out directly on the cows. The author checklist is intended for use with studies where experiments are carried out on animals, which is why we have had such difficulty in completing this for the hut study, as many of the questions do not relate to how the cows were used
Author-wise bibliometric analysis based on entropy.
No full textAuthor-wise bibliometric analysis based on entropy.</p
Author Under Sail The Imagination of Jack London, 1893-1902
No full textIn Author Under Sail, Jay Williams offers the first complete literary biography of Jack London as a professional writer engaged in the labor of writing. It examines the authorial imagination in London's work, the use of imagination in both his fiction and nonfiction, and the ways he defined imagination in the creative process in his business dealings with his publishers, editors, and agents. In this first volume of a two-volume biography, Williams traverses the years 1893 to 1902, from London's "Story of a Typhoon" to The People of the Abyss. The Jack London who emerges in the pages of Author Under Sail is a writer whose partnership with publishers, most notably his productive alliance with George Brett of Macmillan, was one of the most formative in American literary history. London pioneered many author models during the heyday of realism and naturalism, blurring the boundaries of these popular genres by focusing on absorption and theatricality and the representation of the seen and unseen. London created an impassioned, sincere, and extremely personal realism unlike that of other American writers of the time. Author Under Sail is a literary tour de force that reveals the full range of London as writer, creative citizen, and entrepreneur at the same time it sheds light on the maverick side of machine-age literature.Intro -- Title Page -- Copyright Page -- Dedication -- Contents -- Acknowledgments -- Introduction -- 1. Spirit Truth -- 2. From Absorption to Theatricality and Back Again -- 3. "I Will Build a New Present" -- 4. Sons as Authors -- 5. Fathers as Publishers -- 6. The Daughter as Author -- 7. Lovers as Authors -- 8. At Sea with the Family -- 9. Yellow News, Yellow Stories -- 10. The Return Home -- Notes -- Bibliography -- Index -- About Jay WilliamsIn Author Under Sail, Jay Williams offers the first complete literary biography of Jack London as a professional writer engaged in the labor of writing. It examines the authorial imagination in London's work, the use of imagination in both his fiction and nonfiction, and the ways he defined imagination in the creative process in his business dealings with his publishers, editors, and agents. In this first volume of a two-volume biography, Williams traverses the years 1893 to 1902, from London's "Story of a Typhoon" to The People of the Abyss. The Jack London who emerges in the pages of Author Under Sail is a writer whose partnership with publishers, most notably his productive alliance with George Brett of Macmillan, was one of the most formative in American literary history. London pioneered many author models during the heyday of realism and naturalism, blurring the boundaries of these popular genres by focusing on absorption and theatricality and the representation of the seen and unseen. London created an impassioned, sincere, and extremely personal realism unlike that of other American writers of the time. Author Under Sail is a literary tour de force that reveals the full range of London as writer, creative citizen, and entrepreneur at the same time it sheds light on the maverick side of machine-age literature.Description based on publisher supplied metadata and other sources.Electronic reproduction. Ann Arbor, Michigan : ProQuest Ebook Central, YYYY. Available via World Wide Web. Access may be limited to ProQuest Ebook Central affiliated libraries
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