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Journal articles on the topic 'Amylases. Saccharomyces cerevisiae'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Viktor, Marko J., Shaunita H. Rose, Willem H. van Zyl, and Marinda Viljoen-Bloom. "Raw starch conversion by Saccharomyces cerevisiae expressing Aspergillus tubingensis amylases." Biotechnology for Biofuels 6, no. 1 (2013): 167. http://dx.doi.org/10.1186/1754-6834-6-167.

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2

Gronchi, Nicoletta, Lorenzo Favaro, Lorenzo Cagnin, Silvia Brojanigo, Valentino Pizzocchero, Marina Basaglia, and Sergio Casella. "Novel Yeast Strains for the Efficient Saccharification and Fermentation of Starchy By-Products to Bioethanol." Energies 12, no. 4 (February 22, 2019): 714. http://dx.doi.org/10.3390/en12040714.

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The use of solid starchy waste streams to produce value-added products, such as fuel ethanol, is a priority for the global bio-based economy. Despite technological advances, bioethanol production from starch is still not economically competitive. Large cost-savings can be achieved through process integration (consolidated bioprocessing, CBP) and new amylolytic microbes that are able to directly convert starchy biomass into fuel in a single bioreactor. Firstly, CBP technology requires efficient fermenting yeast strains to be engineered for amylase(s) production. This study addressed the selection of superior yeast strains with high fermentative performances to be used as recipient for future CBP engineering of fungal amylases. Twenty-one newly isolated wild-type Saccharomyces cerevisiae strains were screened at 30 °C in a simultaneous saccharification and fermentation (SSF) set up using starchy substrates at high loading (20% w/v) and the commercial amylases cocktail STARGEN™ 002. The industrial yeast Ethanol Red™ was used as benchmark. A cluster of strains produced ethanol levels (up to 118 g/L) significantly higher than those of Ethanol Red™ (about 109 g/L). In particular, S. cerevisiae L20, selected for a scale-up process into a 1-L bioreactor, confirmed the outstanding performance over the industrial benchmark, producing nearly 101 g/L ethanol instead of 94 g/L. As a result, this strain can be a promising CBP host for heterologous expression of fungal amylases towards the design of novel and efficient starch-to-ethanol routes.

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3

Jacobus, Ana Paula, Jeferson Gross, John H. Evans, Sandra Regina Ceccato-Antonini, and Andreas Karoly Gombert. "Saccharomyces cerevisiae strains used industrially for bioethanol production." Essays in Biochemistry 65, no. 2 (July 2021): 147–61. http://dx.doi.org/10.1042/ebc20200160.

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Abstract Fuel ethanol is produced by the yeast Saccharomyces cerevisiae mainly from corn starch in the United States and from sugarcane sucrose in Brazil, which together manufacture ∼85% of a global yearly production of 109.8 million m3 (in 2019). While in North America genetically engineered (GE) strains account for ∼80% of the ethanol produced, including strains that express amylases and are engineered to produce higher ethanol yields; in South America, mostly (>90%) non-GE strains are used in ethanol production, primarily as starters in non-aseptic fermentation systems with cell recycling. In spite of intensive research exploring lignocellulosic ethanol (or second generation ethanol), this option still accounts for <1% of global ethanol production. In this mini-review, we describe the main aspects of fuel ethanol production, emphasizing bioprocesses operating in North America and Brazil. We list and describe the main properties of several commercial yeast products (i.e., yeast strains) that are available worldwide to bioethanol producers, including GE strains with their respective genetic modifications. We also discuss recent studies that have started to shed light on the genes and traits that are important for the persistence and dominance of yeast strains in the non-aseptic process in Brazil. While Brazilian bioethanol yeast strains originated from a historical process of domestication for sugarcane fermentation, leading to a unique group with significant economic applications, in U.S.A., guided selection, breeding and genetic engineering approaches have driven the generation of new yeast products for the market.

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4

YÁÑEZ, Esther, A. Teresa CARMONA, Mercedes TIEMBLO, Antonio JIMÉNEZ, and María FERNÁNDEZ-LOBATO. "Expression of the Schwanniomyces occidentalis SWA2 amylase in Saccharomyces cerevisiae: role of N-glycosylation on activity, stability and secretion." Biochemical Journal 329, no. 1 (January 1, 1998): 65–71. http://dx.doi.org/10.1042/bj3290065.

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The role of N-linked glycosylation on the biological activity of Schwanniomyces occidentalis SWA2 α-amylase, as expressed in Saccharomyces cerevisiae, was analysed by site-directed mutagenesis of the two potential N-glycosylation sites, Asn-134 and Asn-229. These residues were replaced by Ala or Gly individually or in various combinations and the effects on the activity, secretion and thermal stability of the enzyme were studied. Any Asn-229 substitution caused a drastic decrease in activity levels of the extracellular enzyme. In contrast, substitutions of Asn-134 had little or no effect. The use of antibodies showed that α-amylase was secreted in all the mutants tested, although those containing substitutions at Asn-229 seemed to have a lower rate of synthesis and/or higher degradation than the wild-type strain. α-Amylases with substitution at Asn-229 had a 2 kDa lower molecular mass than the wild-type protein, as did the wild-type protein itself after treatment with endoglycosidase F. These findings indicate that Asn-229 is the single glycosylated residue in SWA2. Thermostability analysis of both purified wild-type (T50 = 50 °C, where T50 is the temperature resulting in 50% loss of activity) and mutant enzymes indicated that removal of carbohydrate from the 229 position results in a decrease of approx. 3 °C in the T50 of the enzyme. The Gly-229 mutation does not change the apparent affinity of the enzyme for starch (Km) but decreases to 1/22 its apparent catalytic efficiency (kcat/Km). These results therefore indicate that glycosylation at the 229 position has an important role in the extracellular activity levels, kinetics and stability of the Sw. occidentalis SWA2 α-amylase in both its wild-type and mutant forms.

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5

Yamada, Ryosuke, Syun-ichi Yamakawa, Tsutomu Tanaka, Chiaki Ogino, Hideki Fukuda, and Akihiko Kondo. "Direct and efficient ethanol production from high-yielding rice using a Saccharomyces cerevisiae strain that express amylases." Enzyme and Microbial Technology 48, no. 4-5 (April 2011): 393–96. http://dx.doi.org/10.1016/j.enzmictec.2011.01.002.

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6

Arifiyanti, Nanda Ayu, Dewi Nafisatul Aqliyah, and Mu'tasim Billah. "Bioetanol Dari Biji Nangka Dengan Proses Likuifikasi dan Fermentasi Menggunakan Saccharomyces Cerevisiae." ChemPro 1, no. 01 (March 31, 2020): 51–55. http://dx.doi.org/10.33005/chempro.v1i01.47.

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Potensi biji nangka (Arthocarphus heterophilus) belum dieksploitasi secara optimal. Biji nangka dapat diolah menjadi bahan baku pembuatan bioetanol. Penelitian ini menggunakan metode hidrolisis enzimatis dengan enzim α-amylase dan glukoamilase untuk memecah pati menjadi glucose dan metode fermentasi dapat mengubah glucose menjadi bioetanol menggunakan bakteri saccharomyces cerevisiae. Penelitian ini bertujuan untuk menentukan komposisi variasi penambahan enzim α-amylase dan glukoamilase yang relative baik, waktu fermentasi yang relative baik pada pembentukan bioethanol. Pembuatan bioethanol dilakukan dengan biji nangka 50gram, selanjutnya dikeringkan dengan oven suhu 150 0C selama 1jam, kemudian digiling, kemudian masuk ke proses hidrolisis dengan variabel komposisi penambahan enzim α-amylase dan glukoamilase (20; 30; 40; 50; 60ml) selanjutnya diuji menggunakan refraktometer brix. Selanjutnya, proses fermentasi dilakukan dengan menambahkan yeast Saccharomyces cereviseae dengan variasi lama fermentasi 24; 36; 48; 60; 72 jam. Hasil analisa menunjukkan kadar glukosa yang relatif baik diperoleh pada volume enzim alfa-amilase dan gluko-amilase sebanyak 60ml dengan kadar sebesar 14%. Pada proses fermentasi diperoleh kadar alkohol sebesar 40% dengan waktu fermentasi 60jam.

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7

Moon, Hee Chul, Sol Han, João Borges, Tamagno Pesqueira, Hyunwoo Choi, Sang Yeong Han, Hyeoncheol Cho, Ji Hun Park, João F. Mano, and Insung S. Choi. "Enzymatically degradable, starch-based layer-by-layer films: application to cytocompatible single-cell nanoencapsulation." Soft Matter 16, no. 26 (2020): 6063–71. http://dx.doi.org/10.1039/d0sm00876a.

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Starch-based layer-by-layer (LbL) nanofilms are formed and enzymatically degraded on individual Saccharomyces cerevisiae in a highly cytocompatible fashion. Their enzymatic degradation by α-amylase is also exploited for the controlled release of DNA.

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8

Terashima, M., S. Katoh, B. R. Thomas, and R. L. Rodriguez. "Characterization of rice ?-amylase isozymes expressed by Saccharomyces cerevisiae." Applied Microbiology and Biotechnology 43, no. 6 (November 1995): 1050–55. http://dx.doi.org/10.1007/bf00166924.

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9

Sakai, A., Y. Shimizu, and F. Hishinuma. "Isolation and characterization of mutants which show an oversecretion phenotype in Saccharomyces cerevisiae." Genetics 119, no. 3 (July 1, 1988): 499–506. http://dx.doi.org/10.1093/genetics/119.3.499.

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Abstract We have isolated mutants responsible for an oversecretion phenotype in Saccharomyces cerevisiae, using a promoter of SUC2 and the gene coding for alpha-amylase from mouse as a marker of secretion. These mutations defined two complementation groups, designated as ose1 (over secretion) and rgr1 (resistant to glucose repression). The ose1 mutant produced an oversecretion of amylase by 12- to 15-fold under derepressing conditions; however, the amylase mRNA was present at nearly the same amount as it was in the parent cells. No expression of the amylase gene was detected under repressing conditions. The rgr1 mutant oversecreted amylase by 11- to 13-fold under repressing conditions by 15- to 18-fold under derepressing conditions. The rgr1 mutant showed pleiotropic effects on the following cellular functions: (1) resistance to glucose repression, (2) temperature-sensitive lethality, (3) sporulation deficieny in homozygous diploid cells, and (4) abnormal cell morphology. The rgr1 mutation was not allelic with ssn6 and cyc9, and failed to suppress snf1.

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10

Valkonen, Mari, Merja Penttilä, and Markku Saloheimo. "Effects of Inactivation and Constitutive Expression of the Unfolded- Protein Response Pathway on Protein Production in the Yeast Saccharomyces cerevisiae." Applied and Environmental Microbiology 69, no. 4 (April 2003): 2065–72. http://dx.doi.org/10.1128/aem.69.4.2065-2072.2003.

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ABSTRACT One strategy to obtain better yields of secreted proteins has been overexpression of single endoplasmic reticulum-resident foldases or chaperones. We report here that manipulation of the unfolded-protein response (UPR) pathway regulator, HAC1, affects production of both native and foreign proteins in the yeast Saccharomyces cerevisiae. The effects of HAC1 deletion and overexpression on the production of a native protein, invertase, and two foreign proteins, Bacillus amyloliquefaciens α-amylase and Trichoderma reesei endoglucanase EGI, were studied. Disruption of HAC1 caused decreases in the secretion of both α-amylase (70 to 75% reduction) and EGI (40 to 50% reduction) compared to the secretion by the parental strain. Constitutive overexpression of HAC1 caused a 70% increase in α-amylase secretion but had no effect on EGI secretion. The invertase levels were twofold higher in the strain overexpressing HAC1. Also, the effect of the active form of T. reesei hac1 was tested in S. cerevisiae. hac1 expression caused a 2.4-fold increase in the secretion of α-amylase in S. cerevisiae and also slight increases in invertase and total protein production. Overexpression of both S. cerevisiae HAC1 and T. reesei hac1 caused an increase in the expression of the known UPR target gene KAR2 at early time points during cultivation.

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11

Matsui, Ikuo, Kazuhiko Ishikawa, Eriko Matsui, Sachio Miyairi, Sakuzo Fukui, and Koichi Honda. "Subsite Structure of Saccharomycopsis α-Amylase Secreted from Saccharomyces cerevisiae." Journal of Biochemistry 109, no. 4 (April 1991): 566–69. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a123420.

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12

Randez-Gil, F. "Expression of Aspergillus oryzae α-amylase gene in Saccharomyces cerevisiae." FEMS Microbiology Letters 112, no. 1 (August 15, 1993): 119–23. http://dx.doi.org/10.1016/0378-1097(93)90547-f.

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13

Rothstein, Steven J., Kristine N. Lahners, Colin M. Lazarus, David C. Baulcombe, and Anthony A. Gatenby. "Synthesis and secretion of wheat α-amylase in Saccharomyces cerevisiae." Gene 55, no. 2-3 (January 1987): 353–56. http://dx.doi.org/10.1016/0378-1119(87)90296-4.

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14

Kumagai, Monto H., Mena Shah, Masaaki Terashima, Zeljko Vrkljan, John R. Whitaker, and Raymond L. Rodriguez. "Expression and secretion of rice α-amylase by Saccharomyces cerevisiae." Gene 94, no. 2 (January 1990): 209–16. http://dx.doi.org/10.1016/0378-1119(90)90389-9.

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15

Liu, Zihe, Lifang Liu, Tobias Österlund, Jin Hou, Mingtao Huang, Linn Fagerberg, Dina Petranovic, Mathias Uhlén, and Jens Nielsen. "Improved Production of a Heterologous Amylase in Saccharomyces cerevisiae by Inverse Metabolic Engineering." Applied and Environmental Microbiology 80, no. 17 (June 27, 2014): 5542–50. http://dx.doi.org/10.1128/aem.00712-14.

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ABSTRACTThe increasing demand for industrial enzymes and biopharmaceutical proteins relies on robust production hosts with high protein yield and productivity. Being one of the best-studied model organisms and capable of performing posttranslational modifications, the yeastSaccharomyces cerevisiaeis widely used as a cell factory for recombinant protein production. However, many recombinant proteins are produced at only 1% (or less) of the theoretical capacity due to the complexity of the secretory pathway, which has not been fully exploited. In this study, we applied the concept of inverse metabolic engineering to identify novel targets for improving protein secretion. Screening that combined UV-random mutagenesis and selection for growth on starch was performed to find mutant strains producing heterologous amylase 5-fold above the level produced by the reference strain. Genomic mutations that could be associated with higher amylase secretion were identified through whole-genome sequencing. Several single-point mutations, including an S196I point mutation in theVTA1gene coding for a protein involved in vacuolar sorting, were evaluated by introducing these to the starting strain. By applying this modification alone, the amylase secretion could be improved by 35%. As a complement to the identification of genomic variants, transcriptome analysis was also performed in order to understand on a global level the transcriptional changes associated with the improved amylase production caused by UV mutagenesis.

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16

Nikolic, Svetlana, Marica Rakin, Maja Vukasinovic, Slavica Siler-Marinkovic, and Ljiljana Mojovic. "Bioethanol from corn meal hydrolyzates." Chemical Industry and Chemical Engineering Quarterly 11, no. 4 (2005): 189–94. http://dx.doi.org/10.2298/ciceq0504189n.

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The two-step enzymatic hydrolysis of corn meal by commercially available ?-amylase and amyloglycosidase and the subsequent or simultaneous ethanol fermentation of the hydrolyzates by Saccharomyces cerevisiae yeast were studied. The conditions of starch hydrolysis, such as substrate and enzyme concentration and the time required for enzymatic action, were optimized taking into account both the effects of hydrolysis and ethanol fermentation. The corn meal hydrolyzates obtained were good substrates for ethanol fermentation by Saccharomyces cerevisiae. A yield of ethanol of more than 80% of the theoretical one was achieved with a satisfactory product to substrate yield Yp/s (g/g) and good ethanol volumetric productivity P (g/lh). No shortage of fermentable sugars was observed during simultaneous hydrolysis and fermentation. Savings in time and energy could be realized by such a process.

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17

Roni, Kiagus A., Dorie Kartika, Hasyirullah Apriyadi, and Netty Herawati. "The Effect of Type and Concentration Yeast with Fermentation Time and Liquifaction Variations on the Bioethanol Concentration Resulted by Sorgum Seeds with Hydrolysis and Fermentation Processes." Journal of Computational and Theoretical Nanoscience 16, no. 12 (December 1, 2019): 5228–32. http://dx.doi.org/10.1166/jctn.2019.8591.

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Sorghum is one of the plants that can be used as raw material for making bioethanol. Sorghum has seeds with a starch composition of 73.8%, which is potential as a raw material for making bioethanol. Sorghum starch can be converted into bioethanol through the hydrolysis process (the process of converting carbohydrates into glucose) which consists of liquefaction and saccharification processes and is followed by a fermentation process. The hydrolysis method is carried out enzymatically. In this study alpha amylase and gluco amylase enzymes were used with various types of yeast including Saccharomyces cerevisiae, Rhizopus oryzae, Acetobacter xylinum, Mucor sp, and Aspergilus niger which varied with liquefaction temperatures including 80, 85, 90, 95, and 100 °C. Obtained the most optimal yeast is Saccharomyces cerevisiae with an optimal temperature of 95 °C resulting in a bioethanol concentration of 4.3%. After getting the optimal yeast and temperature, the fermentation step of the two variables is used in the next step. In the fermentation process, variations of yeast concentration and duration of fermentation were used, the optimum yeast concentration was at 2.5% with 48 hours of fermentation resulting in bioethanol concentration of 11%.

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18

Galdino, Alexsandro Sobreira, Roberto Nascimento Silva, Muriele Taborda Lottermann, Alice Cunha Morales Álvares, Lídia Maria Pepe de Moraes, Fernando Araripe Gonçalves Torres, Sonia Maria de Freitas, and Cirano José Ulhoa. "Biochemical and Structural Characterization of Amy1: An Alpha-Amylase from Cryptococcus flavus Expressed in Saccharomyces cerevisiae." Enzyme Research 2011 (March 30, 2011): 1–7. http://dx.doi.org/10.4061/2011/157294.

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An extracellular alpha-amylase (Amy1) whose gene from Cryptococcus flavus was previously expressed in Saccharomyces cerevisiae was purified to homogeneity (67 kDa) by ion-exchange and molecular exclusion chromatography. The enzyme was activated by NH4+ and inhibited by Cu+2 and Hg+2. Significant biochemical and structural discrepancies between wild-type and recombinant α-amylase with respect to Km values, enzyme specificity, and secondary structure content were found. Far-UV CD spectra analysis at pH 7.0 revealed the high thermal stability of both proteins and the difference in folding pattern of Amy1 compared with wild-type amylase from C. flavus, which reflected in decrease (10-fold) of enzymatic activity of recombinant protein. Despite the differences, the highest activity of Amy1 towards soluble starch, amylopectin, and amylase, in contrast with the lowest activity of Amy1w, points to this protein as being of paramount biotechnological importance with many applications ranging from food industry to the production of biofuels.

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19

Shigechi, Hisayori, Jun Koh, Yasuya Fujita, Takeshi Matsumoto, Yohei Bito, Mitsuyoshi Ueda, Eiichi Satoh, Hideki Fukuda, and Akihiko Kondo. "Direct Production of Ethanol from Raw Corn Starch via Fermentation by Use of a Novel Surface-Engineered Yeast Strain Codisplaying Glucoamylase and α-Amylase." Applied and Environmental Microbiology 70, no. 8 (August 2004): 5037–40. http://dx.doi.org/10.1128/aem.70.8.5037-5040.2004.

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ABSTRACT Direct and efficient production of ethanol by fermentation from raw corn starch was achieved by using the yeast Saccharomyces cerevisiae codisplaying Rhizopus oryzae glucoamylase and Streptococcus bovis α-amylase by using the C-terminal-half region of α-agglutinin and the flocculation functional domain of Flo1p as the respective anchor proteins. In 72-h fermentation, this strain produced 61.8 g of ethanol/liter, with 86.5% of theoretical yield from raw corn starch.

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20

Nonklang, Sanom, Babiker M. A. Abdel-Banat, Kamonchai Cha-aim, Nareerat Moonjai, Hisashi Hoshida, Savitree Limtong, Mamoru Yamada, and Rinji Akada. "High-Temperature Ethanol Fermentation and Transformation with Linear DNA in the Thermotolerant Yeast Kluyveromyces marxianus DMKU3-1042." Applied and Environmental Microbiology 74, no. 24 (October 17, 2008): 7514–21. http://dx.doi.org/10.1128/aem.01854-08.

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ABSTRACT We demonstrate herein the ability of Kluyveromyces marxianus to be an efficient ethanol producer and host for expressing heterologous proteins as an alternative to Saccharomyces cerevisiae. Growth and ethanol production by strains of K. marxianus and S. cerevisiae were compared under the same conditions. K. marxianus DMKU3-1042 was found to be the most suitable strain for high-temperature growth and ethanol production at 45°C. This strain, but not S. cerevisiae, utilized cellobiose, xylose, xylitol, arabinose, glycerol, and lactose. To develop a K. marxianus DMKU3-1042 derivative strain suitable for genetic engineering, a uracil auxotroph was isolated and transformed with a linear DNA of the S. cerevisiae ScURA3 gene. Surprisingly, Ura+ transformants were easily obtained. By Southern blot hybridization, the linear ScURA3 DNA was found to have inserted randomly into the K. marxianus genome. Sequencing of one Lys− transformant confirmed the disruption of the KmLYS1 gene by the ScURA3 insertion. A PCR-amplified linear DNA lacking K. marxianus sequences but containing an Aspergillus α-amylase gene under the control of the ScTDH3 promoter together with an ScURA3 marker was subsequently used to transform K. marxianus DMKU3-1042 in order to obtain transformants expressing Aspergillus α-amylase. Our results demonstrate that K. marxianus DMKU3-1042 can be an alternative cost-effective bioethanol producer and a host for transformation with linear DNA by use of S. cerevisiae-based molecular genetic tools.

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21

Kayath, Christian Aimé, Armel Ibala Zamba, Saturnin Nicaise Mokémiabeka, Meddy Opa-Iloy, Paola Sandra Elenga Wilson, Moïse Doria Kaya-Ongoto, Rodd Jurah Mouellet Maboulou, and Etienne Nguimbi. "Synergic Involvements of Microorganisms in the Biomedical Increase of Polyphenols and Flavonoids during the Fermentation of Ginger Juice." International Journal of Microbiology 2020 (August 1, 2020): 1–12. http://dx.doi.org/10.1155/2020/8417693.

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Steered fermentation by microorganisms gives great added value in the nutritional quality of local food. Ginger rhizome naturally contains a myriad of bioactive compounds including polyphenol and flavonoids. The aim of this work was to ferment the ginger juice, to evaluate the biochemical parameters of ginger wine, and to understand the involvement of microorganisms in the bioincrease of polyphenol compounds. Titratable acidity and pH values were determined and showed that pH is around 1.6 at the end of the fermentation when the acidity is around 6.431 g/L. Using colorimetric assay, the total polyphenolic and flavonoid compounds were evaluated throughout the fermentation. The variation of the polyphenol and flavonoid concentrations of the unsweetened sample was around 10.18 to 14.64 mg Eq AG/g and 1.394 to 2.224 mg Eq Cat/g Ms, but those from the sweet sample were around 10.82 to 18.34 mg Eq AG/g Ms and 1.311 to 2.290 mg Eq Cat/g. Using one-step PCR, multiplex techniques with specific primers, with yeast-like phenotype 27.27% (6), have been assigned among 22 isolates to Saccharomyces cerevisiae. By using PCR multiplex techniques, Bacillus licheniformis, Bacillus pumilus, Bacillus safensis, and Saccharomyces cerevisiae have been identified. Together with Saccharomyces cerevisiae, we showed that Bacillus sp. are able to secrete enzymatic landscape with some activities up to 50% including cellulase, amylase, pectinase, and protease.

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22

Liu, Zihe, Tobias Österlund, Jin Hou, Dina Petranovic, and Jens Nielsen. "Anaerobic α-Amylase Production and Secretion with Fumarate as the Final Electron Acceptor in Saccharomyces cerevisiae." Applied and Environmental Microbiology 79, no. 9 (February 22, 2013): 2962–67. http://dx.doi.org/10.1128/aem.03207-12.

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ABSTRACTIn this study, we focus on production of heterologous α-amylase in the yeastSaccharomyces cerevisiaeunder anaerobic conditions. We compare the metabolic fluxes and transcriptional regulation under aerobic and anaerobic conditions, with the objective of identifying the final electron acceptor for protein folding under anaerobic conditions. We find that yeast produces more amylase under anaerobic conditions than under aerobic conditions, and we propose a model for electron transfer under anaerobic conditions. According to our model, during protein folding the electrons from the endoplasmic reticulum are transferred to fumarate as the final electron acceptor. This model is supported by findings that the addition of fumarate under anaerobic (but not aerobic) conditions improves cell growth, specifically in the α-amylase-producing strain, in which it is not used as a carbon source. Our results provide a model for the molecular mechanism of anaerobic protein secretion using fumarate as the final electron acceptor, which may allow for further engineering of yeast for improved protein secretion under anaerobic growth conditions.

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23

Nonato, Roberto V., and Kazuo Shishido. "α-factor-directed synthesis of Bacillus stearothermophilus α-amylase in saccharomyces cerevisiae." Biochemical and Biophysical Research Communications 152, no. 1 (April 1988): 76–82. http://dx.doi.org/10.1016/s0006-291x(88)80682-x.

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24

Kovaleva, I. E., L. A. Novikova, and Y. N. Luzikov. "Synthesis and secretion of bacterial α-amylase by the yeast Saccharomyces cerevisiae." FEBS Letters 251, no. 1-2 (July 17, 1989): 183–86. http://dx.doi.org/10.1016/0014-5793(89)81451-6.

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25

Wang, Bi-Dar, and Tsong-Teh Kuo. "Induction of a Mitosis Delay and Cell Lysis by High-Level Secretion of Mouse α-Amylase from Saccharomyces cerevisiae." Applied and Environmental Microbiology 67, no. 8 (August 1, 2001): 3693–701. http://dx.doi.org/10.1128/aem.67.8.3693-3701.2001.

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ABSTRACT Some foreign proteins are produced in yeast in a cell cycle-dependent manner, but the cause of the cell cycle dependency is unknown. In this study, we found that Saccharomyces cerevisiae cells secreting high levels of mouse α-amylase have elongated buds and are delayed in cell cycle completion in mitosis. The delayed cell mitosis suggests that critical events during exit from mitosis might be disturbed. We found that the activities of PP2A (protein phosphatase 2A) and MPF (maturation-promoting factor) were reduced in α-amylase-oversecreting cells and that these cells showed a reduced level of assembly checkpoint protein Cdc55, compared to the accumulation in wild-type cells. MPF inactivation is due to inhibitory phosphorylation on Cdc28, as a cdc28mutant which lacks an inhibitory phosphorylation site on Cdc28 prevents MPF inactivation and prevents the defective bud morphology induced by overproduction of α-amylase. Our data also suggest that high levels of α-amylase may downregulate PPH22,leading to cell lysis. In conclusion, overproduction of heterologous α-amylase in S. cerevisiaeresults in a negative regulation of PP2A, which causes mitotic delay and leads to cell lysis.

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26

Fatmawati, Akbarningrum, Tuani Lidiawati, Stephen Hadinata, and Mikhael Adiarto. "Solid-State Fermentation of Banana Peels Potential Study for Feed Additive." MATEC Web of Conferences 215 (2018): 01027. http://dx.doi.org/10.1051/matecconf/201821501027.

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Agricultural solid wastes present abundantly on earth as crops harvesting as well as processing are countinuesly run. Banana peels are one of agricultural solid wastes produced anywhere the banana processing presents. The peels present abundantly in tropical countries such as Indonesia. The carbohydrate content of banana peels make it useful for the production of many chemicals, including feed. Meanwhile the large need in feed in farming including fish farming could prevent farmer to obtain substantial profit. This research studied the possibility of banana peel as one of abundant Indonesian agricultural solid waste to be utilized as fish feed which is known requiring certain level of protein content. This was done by fermenting the peels in fixed bed reaction mode using surface aeration and non-aeration. The fermentation was conducted using yeast Saccharomyces cerevisiae Y1536 and Rhizopus Oryzae FNCC 6157. The reaction time was varied for 1, 3, and 5 days. The important parameters studied were protein contents, and amylase activity of the fermented banana peels. Despite aeration indicated more operational cost, it showed significant impact on the fermentation of banana peels. The best condition for fermentation using Saccharomyces cerevisiae Y1536 were 5 day fermentation with surface aeration which result in the increase of protein content up to 4.05%, the decrease of fiber content up to 1.08%, and amylase activity of 9.99 DP. Whilst the fermentation using Rhizopus Oryzae FNCC 6157 obtained its best result at 1 day fermentation with aeration, which are protein content increase up to 4.04% and fiber content decrease up to 0.69%. However, the fermentation using this mold showed its best amylase activity result of 12.75 DP at 5 day surface aerated fermentation.

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Kusmiyati, K., and Lukhi Mulia Shitophyta. "Produksi Bioetanol dari Bahan Baku Singkong, Jagung dan Iles-iles :Pengaruh Suhu Fermentasi dan Berat Yeast Saccharomyces cerevisiae." Reaktor 15, no. 2 (August 1, 2014): 97. http://dx.doi.org/10.14710/reaktor.15.2.97-103.

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Kebutuhan bahan bakar di masa sekarang semakin bertambah besar sehingga berdampak pada menipisnya sumber bahan bakar dan meningkatnya polusi udara di lingkungan. Penggunaan bahan bakar alternatif dari sumber non fosil merupakan pilihan terbaik sebagai pengganti bahan bakar fosil. Bioetanol merupakan salah satu energi alternatif yang tepat digunakan baik di masa sekarang ataupun di masa yang akan datang. Bahan baku etanol yang digunakan pada penelitian ini adalah singkong, dan iles-iles.Variabel penelitian yang diamati temperatur fermentasi (30°C; 40°C; 50°C) dan komposisi Saccharomyces cerevisiae (2,5 g; 5 g; 10 g; 15 g) Proses pembuatan bioetanol terdiri dari hidrolisis enzim yaitun likuifikasi menggunakan a-amylase1,6% v/w (t = 1 jam; T = 95-100°C; pH 6) dan sakarifikasi menggunakan b-amylase 3,2% v/w (t = 4 jam; T = 60°C; pH 5) serta proses fermentasi menggunakan Saccharomyces cerevisiae ( t = 120 jam; pH 4,5; yeast 5 g). Kadar etanol tertinggi dihasilkan pada temperatur fermentasi 30°C untuk semua bahan baku dengan kadar etanol masing-masing 83,43 g/L untuk singkong,80,77 g/L untuk jagung,dan 79,94 g/L untuk iles-iles.

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YAMASHITA, Ichiro, Tetsuya ITOH, and Sakuzo FUKUI. "Cloning and expression of the Saccharomycopsis fibuligera .ALPHA.-amylase gene in Saccharomyces cerevisiae." Agricultural and Biological Chemistry 49, no. 10 (1985): 3089–91. http://dx.doi.org/10.1271/bbb1961.49.3089.

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MATSUI, Ikuo, Eriko MATSUI, Kazuhiko ISHIKAWA, Sachio MIYAIRI, and Koichi HONDA. "The enzymatic and molecular characteristics of Saccharomycopsis .ALPHA.-amylase secreted from Saccharomyces cerevisiae." Agricultural and Biological Chemistry 54, no. 8 (1990): 2009–15. http://dx.doi.org/10.1271/bbb1961.54.2009.

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Wang, Tsung Tsan, Long Liu Lin, and Wen Hwei Hsu. "Cloning and Expression of a Schwanniomyces occidentalis α-Amylase Gene in Saccharomyces cerevisiae." Applied and Environmental Microbiology 55, no. 12 (1989): 3167–72. http://dx.doi.org/10.1128/aem.55.12.3167-3172.1989.

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Makarow, M. "Endocytosis in Saccharomyces cerevisiae: internalization of alpha-amylase and fluorescent dextran into cells." EMBO Journal 4, no. 7 (July 1985): 1861–66. http://dx.doi.org/10.1002/j.1460-2075.1985.tb03861.x.

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32

Ma, Rufei, Lu Sui, Jingsheng Zhang, Jinrong Hu, and Ping Liu. "Polyphasic Characterization of Yeasts and Lactic Acid Bacteria Metabolic Contribution in Semi-Solid Fermentation of Chinese Baijiu (Traditional Fermented Alcoholic Drink): Towards the Design of a Tailored Starter Culture." Microorganisms 7, no. 5 (May 25, 2019): 147. http://dx.doi.org/10.3390/microorganisms7050147.

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Chinese Baijiu is principally produced through a spontaneous fermentation process, which involves complex microorganism communities. Among them, yeasts and lactic acid bacteria (LAB) are important communities. The study examined the isolated strains from fermented grains of Baijiu regarding their activity of α-amylase and glucoamylase, ethanol tolerance, glucose utilization, as well as metabolite production in the process of laboratory-scale sorghum-based fermentation. Selected strains (Saccharomycopsis fibuligera 12, Saccharomyces cerevisiae 3, and Pediococcus acidilactici 4) were blended in different combinations. The influence of selected strains on the metabolic variation in different semi-solid fermentations was investigated by gas chromatography–mass spectrometry (GC–MS) accompanied by multivariate statistical analysis. According to the principal component analysis (PCA), the metabolites produced varied in different mixtures of pure cultures. S. fibuligera produced various enzymes, particularly α-amylase and glucoamylase, and exhibited a better performance compared with other species regarding the ability to convert starch to soluble sugars and positively affect the production process of volatile compounds. S. cerevisiae had a high fermentation capacity, thereby contributing to substrates utilization. Lactic acid bacteria had a good ability to produce lactic acid. This study attaches importance to the special functions of S. fibuligera, S. cerevisiae, and P. acidilactici in Chinese Baijiu making, and investigates their metabolic characteristics in the process of lab-scale semi-solid fermentation.

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Huang, Mingtao, Guokun Wang, Jiufu Qin, Dina Petranovic, and Jens Nielsen. "Engineering the protein secretory pathway of Saccharomyces cerevisiae enables improved protein production." Proceedings of the National Academy of Sciences 115, no. 47 (November 5, 2018): E11025—E11032. http://dx.doi.org/10.1073/pnas.1809921115.

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Baker’s yeast Saccharomyces cerevisiae is one of the most important and widely used cell factories for recombinant protein production. Many strategies have been applied to engineer this yeast for improving its protein production capacity, but productivity is still relatively low, and with increasing market demand, it is important to identify new gene targets, especially targets that have synergistic effects with previously identified targets. Despite improved protein production, previous studies rarely focused on processes associated with intracellular protein retention. Here we identified genetic modifications involved in the secretory and trafficking pathways, the histone deacetylase complex, and carbohydrate metabolic processes as targets for improving protein secretion in yeast. Especially modifications on the endosome-to-Golgi trafficking was found to effectively reduce protein retention besides increasing protein secretion. Through combinatorial genetic manipulations of several of the newly identified gene targets, we enhanced the protein production capacity of yeast by more than fivefold, and the best engineered strains could produce 2.5 g/L of a fungal α-amylase with less than 10% of the recombinant protein retained within the cells, using fed-batch cultivation.

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Yamada, Ryosuke, Tsutomu Tanaka, Chiaki Ogino, Hideki Fukuda, and Akihiko Kondo. "Efficient and practical ethanol production from high yield rice by amylase expressing Saccharomyces cerevisiae." Journal of Bioscience and Bioengineering 108 (November 2009): S50. http://dx.doi.org/10.1016/j.jbiosc.2009.08.144.

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Yamakawa, Syun-ichi, Ryosuke Yamada, Tsutomu Tanaka, Chiaki Ogino, and Akihiko Kondo. "Repeated fermentation from raw starch using Saccharomyces cerevisiae displaying both glucoamylase and α-amylase." Enzyme and Microbial Technology 50, no. 6-7 (May 2012): 343–47. http://dx.doi.org/10.1016/j.enzmictec.2012.03.005.

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Liao, Bo, Gordon A. Hill, and William J. Roesler. "Amylolytic activity and fermentative ability of Saccharomyces cerevisiae strains that express barley α-amylase." Biochemical Engineering Journal 53, no. 1 (December 2010): 63–70. http://dx.doi.org/10.1016/j.bej.2010.09.009.

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Zhilinskaia, Nadezhda, Rui Wang, Olga Ivanchenko, Petr Balanov, and Irina Smotraeva. "Biotechnological recycling of byproducts in the rice soft beverage industry: a preliminary research." E3S Web of Conferences 247 (2021): 01006. http://dx.doi.org/10.1051/e3sconf/202124701006.

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The use of industrial waste as the secondary raw materials is relevant all over the world. The rice sediment is a byproduct of the rice soft beverage industry. The rice mash was obtained by the rice sediment fermentation with α-amylase and ethanol yeast Saccharomyces cerevisiae. The rice wort fermentation efficiency was estimated by rice mash ethanol concentration, the visible mass concentration of mash dry substances, mash acidity, total yeast number and yeast budding, yeast cell area. The most intensive fermentation was in the sample with α-amylase. On the 7th day of fermentation, the alcohol concentration in this sample was 5.28volume (%), which is 5 times more than in the sample without α-amylase. Digital morphometric characteristics of yeast correlated with actual fermentation parameters, reflecting yeast adaptive reactions at various ethanol technological stages. The rice mash can be used in the rectification process to obtain new products - ethanol distillate or bioethanol. New methods and expanding technologies for biotechnological rice sediment recycling are required in this field of research.

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Steyn, Andries J. C., and Isak S. Pretorius. "Co-expression of a Saccharomyces diastaticus glucoamylase-encoding gene and a Bacillus amyloliquefaciens α-amylase-encoding gene in Saccharomyces cerevisiae." Gene 100 (April 1991): 85–93. http://dx.doi.org/10.1016/0378-1119(91)90353-d.

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Yanase, Michiyo, Hiroki Takata, Takeshi Takaha, Takashi Kuriki, Steven M. Smith, and Shigetaka Okada. "Cyclization Reaction Catalyzed by Glycogen Debranching Enzyme (EC 2.4.1.25/EC 3.2.1.33) and Its Potential for Cycloamylose Production." Applied and Environmental Microbiology 68, no. 9 (September 2002): 4233–39. http://dx.doi.org/10.1128/aem.68.9.4233-4239.2002.

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ABSTRACT Glycogen debranching enzyme (GDE) has 4-α-glucanotransferase and amylo-1,6-glucosidase activities in the single polypeptide chain. We analyzed the detailed action profile of GDE from Saccharomyces cerevisiae on amylose and tested whether GDE catalyzes cyclization of amylose. GDE treatment resulted in a rapid reduction of absorbance of iodine-amylose complex and the accumulation of a product that was resistant to an exo-amylase (glucoamylase [GA]) but was degraded by an endo-type α-amylase to glucose and maltose. These results indicated that GDE catalyzed cyclization of amylose to produce cyclic α-1,4 glucan (cycloamylose). The formation of cycloamylose was confirmed by high-performance anion-exchange chromatography, and the size was shown to range from a degree of polymerization of 11 to a degree of polymerization around 50. The minimum size and the size distribution of cycloamylose were different from those of cycloamylose produced by other 4-α-glucanotransferases. GDE also efficiently produced cycloamylose even from the branched glucan substrate, starch, demonstrating its potential for industrial production of cycloamylose.

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Sohn, Young-Sun, Cheon Seok Park, Sun-Bok Lee, and Dewey D. Y. Ryu. "Disruption of PMR1, Encoding a Ca2+-ATPase Homolog in Yarrowia lipolytica, Affects Secretion and Processing of Homologous and Heterologous Proteins." Journal of Bacteriology 180, no. 24 (December 15, 1998): 6736–42. http://dx.doi.org/10.1128/jb.180.24.6736-6742.1998.

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ABSTRACT The Yarrowia lipolytica PMR1 gene (YlPMR1) is a Saccharomyces cerevisiae PMR1 homolog which encodes a putative secretory pathway Ca2+-ATPase. In this study, we investigated the effects of a YlPMR1 disruption on the processing and secretion of native and foreign proteins in Y. lipolytica and found variable responses by theYlPMR1-disrupted mutant depending on the protein. The secretion of 32-kDa mature alkaline extracellular protease (AEP) was dramatically decreased, and incompletely processed precursors were observed in the YlPMR1-disrupted mutant. A 36- and a 52-kDa premature AEP were secreted, and an intracellular 52-kDa premature AEP was also detected. The acid extracellular protease activity of theYlPMR1-disrupted mutant was increased by 60% compared to that of the wild-type strain. The inhibitory effect of mutations in secretory pathway Ca2+-ATPase genes on the secretion of rice α-amylase was also observed in the Y. lipolytica andS. cerevisiae PMR1-disrupted mutants. Unlike rice α-amylase, the secretion of Trichoderma reeseiendoglucanase I (EGI) was not influenced by the YlPMR1disruption. However, the secreted EGI from theYlPMR1-disrupted mutant had different characteristics than that of the control. While wild-type cells secreted the hyperglycosylated form of EGI, hyperglycosylation was completely absent in the YlPMR1-disrupted mutant. Our results indicate that the effects of the YlPMR1 disruption as manifested by the phenotypic response depend on the characteristics of the reporter protein in the recombinant yeast strain evaluated.

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Martínez, José L., Eugenio Meza, Dina Petranovic, and Jens Nielsen. "The impact of respiration and oxidative stress response on recombinant α-amylase production by Saccharomyces cerevisiae." Metabolic Engineering Communications 3 (December 2016): 205–10. http://dx.doi.org/10.1016/j.meteno.2016.06.003.

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42

Hara, Kiyotaka Y., Songhee Kim, Kentaro Kiriyama, Hideyo Yoshida, Shogo Arai, Jun Ishii, Chiaki Ogino, Hideki Fukuda, and Akihiko Kondo. "An energy-saving glutathione production method from low-temperature cooked rice using amylase-expressing Saccharomyces cerevisiae." Biotechnology Journal 7, no. 5 (February 29, 2012): 686–89. http://dx.doi.org/10.1002/biot.201100432.

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43

Abarca, Dolores, María Fernández-Lobato, Manuel Gonzalo Claros, and Antonio Jiménez. "Isolation and expression in Saccharomyces cerevisiae of a gene encoding an α-amylase from Schwanniomyces castellii." FEBS Letters 255, no. 2 (September 25, 1989): 455–59. http://dx.doi.org/10.1016/0014-5793(89)81144-5.

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44

Hoshida, Hisashi, Tsuneyasu Fujita, Kamonchai Cha-aim, and Rinji Akada. "N-glycosylation deficiency enhanced heterologous production of a Bacillus licheniformis thermostable α-amylase in Saccharomyces cerevisiae." Applied Microbiology and Biotechnology 97, no. 12 (January 11, 2013): 5473–82. http://dx.doi.org/10.1007/s00253-012-4582-2.

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45

Lheman, Jennifer, Anthony Sutiono, Yanti Yanti, Raymond Rubianto Tjandrawinata, and Bibiana Widiyati Lay. "FUNCTIONAL BIGNAY CIDERS INHIBIT KEY ENZYMES LINKED TO OBESITY AND DIABETES FOR METABOLIC SYNDROME PROTECTION." Jurnal Teknologi 83, no. 2 (February 2, 2021): 67–75. http://dx.doi.org/10.11113/jurnalteknologi.v83.14898.

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Metabolic syndrome has become one of the major health issues worldwide. Cider beverages have several functional properties for health, such as antioxidant, antimicrobial, anti-inflammatory, and antidiabetic effects. In this study, we formulated cider beverages from bignay fruits (Antidesma bunius), identified their compounds, and evaluated their functional effects for metabolic syndrome protection. Ciders were produced from the aqueous extract of bignay fruit powder, fermented using Saccharomyces cerevisiae and Acetobacter xylinum for 3, 7, and 14 days. Compound identification in bignay ciders was done using gas chromatography-mass spectrometry (GC/MS). Antioxidant activity was done by the 1,1-diphenyl-2-picrylhydrazyl assay, while enzymatic inhibitory assays were tested against lipase, α-glucosidase, α-amylase, and angiotensin converting enzyme (ACE). GC/MS profiling showed that most bignay ciders contained major organic acids and amino acids. All ciders exerted high antioxidant activity (>60%). Bignay ciders fermented from A. xylinum demonstrated significant inhibition (>90%) against lipase and α-glucosidase activities. However, ciders had no functional effect on a-amylase and angiotensin-converting enzyme inhibition. These data suggest that bignay ciders may have potential as functional beverages with antioxidant, antiobesity, and antidiabetic effects for management of metabolic syndrome.

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Knox, Alison M., James C. du Preez, and Stephanus G. Kilian. "Starch fermentation characteristics of Saccharomyces cerevisiae strains transformed with amylase genes from Lipomyces kononenkoae and Saccharomycopsis fibuligera." Enzyme and Microbial Technology 34, no. 5 (April 2004): 453–60. http://dx.doi.org/10.1016/j.enzmictec.2003.12.010.

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47

Ruohonen, Laura, Peter Hackman, Päivi Lehtovaara, Jonathan K. C. Knowles, and Sirkka Keränen. "Efficient secretion of Bacillus amyloliquefaciens α-amylase cells by its own signal peptide from Saccharomyces cerevisiae host." Gene 59, no. 2-3 (January 1987): 161–70. http://dx.doi.org/10.1016/0378-1119(87)90324-6.

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48

Steyn, Andries J. C., and Isak S. Pretorius. "Characterization of a novel ?-amylase from Lipomyces kononenkoae and expression of its gene (LKA1) in Saccharomyces cerevisiae." Current Genetics 28, no. 6 (1995): 526–33. http://dx.doi.org/10.1007/bf00518165.

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49

Yesmin, M. N., M. A. K. Azad, M. Kamruzzaman, and M. N. Uddin. "Bioethanol Production from Corn, Pumpkin and Carrot of Bangladesh as Renewable Source using Yeast Saccharomyces cerevisiae." Acta Chemica Malaysia 4, no. 2 (December 1, 2020): 45–54. http://dx.doi.org/10.2478/acmy-2020-0008.

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AbstractBangladesh produces a large amount of corn, pumpkin and carrots every year. To meet its huge energy demand and to lessen dependence on traditional fossil fuel these products are cost effective, renewable and abundant source for bioethanol production. The research was aimed to evaluate Bangladeshi corn, rotten carrot and pumpkin for bioethanol production. About 100 g of substrates was mixed with 300 ml distilled water and blended and sterilized. All the experiment was conducted with a temperature of 35oC, pH 6.0 and 20% sugar concentration. For fermentation, 200 ml yeast (Saccharomyces cerevisiae CCD) was added to make the total volume 500 ml. Addition of small amount of 1750 unit α-amylase enzyme to the substrate solution was found to enhance the fermentation process quicker. After 6- days of incubation, corn produced 63.00 ml of ethanol with 13.33 % (v/v) purity. Bioethanol production capacity of two different local varieties of pumpkin (red and black color) was assessed. Red pumpkin (Cucurbita maxima L.) produces 53 ml of ethanol with purity 6 %v/v and black color pumpkin produces 40 ml of yield with a low purity 4 %v/v. Carrot (Daucus carota L.) produces 73.67 ml of ethanol with 12.66 % (v/v) purity.

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Osemwengie, S. O., E. I. Osagie, and B. Onwukwe. "Optimization of bioethanol production from cassava peels." Journal of Applied Sciences and Environmental Management 24, no. 12 (February 16, 2021): 2077–83. http://dx.doi.org/10.4314/jasem.v24i12.11.

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The bioethanol production from waste is acquiring attraction as a strategy for increasing energy security. This study aims to optimize the production of ethanol from cassava peel using Box Bhenken experimental design. The total carbohydrate content of about 90% in cassava peel was subjected to enzymatic hydrolysis using Alpha-amylase followed by Simultaneous Saccharification and Fermentation (SSF) by Saccharomyces cerevisiae for bioethanol production. The production of bioethanol from cassava peels was investigated for 1-4 hours (hydrolysis time), 0.5–1.5mg/L (enzyme loading), and 1-5 days (incubation time). A statistical model was developed and validated to predict the yield of bioethanol after fermentation, and the Response Surface Methodology (RSM) was used to optimize the conditions. The results revealed that the maximum ethanol yield of 1.911% was obtained at the optimum hydrolysis time, enzyme loading, and incubation time (i.e. 2.5 hours, 1 mg/L, and 3 days respectively).

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