scholarly journals Direct Production of Ethanol from Raw Corn Starch via Fermentation by Use of a Novel Surface-Engineered Yeast Strain Codisplaying Glucoamylase and α-Amylase

2004 ◽  
Vol 70 (8) ◽  
pp. 5037-5040 ◽  
Author(s):  
Hisayori Shigechi ◽  
Jun Koh ◽  
Yasuya Fujita ◽  
Takeshi Matsumoto ◽  
Yohei Bito ◽  
...  

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.

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Liang Sun ◽  
Jae Won Lee ◽  
Sangdo Yook ◽  
Stephan Lane ◽  
Ziqiao Sun ◽  
...  

AbstractPlant cell wall hydrolysates contain not only sugars but also substantial amounts of acetate, a fermentation inhibitor that hinders bioconversion of lignocellulose. Despite the toxic and non-consumable nature of acetate during glucose metabolism, we demonstrate that acetate can be rapidly co-consumed with xylose by engineered Saccharomyces cerevisiae. The co-consumption leads to a metabolic re-configuration that boosts the synthesis of acetyl-CoA derived bioproducts, including triacetic acid lactone (TAL) and vitamin A, in engineered strains. Notably, by co-feeding xylose and acetate, an enginered strain produces 23.91 g/L TAL with a productivity of 0.29 g/L/h in bioreactor fermentation. This strain also completely converts a hemicellulose hydrolysate of switchgrass into 3.55 g/L TAL. These findings establish a versatile strategy that not only transforms an inhibitor into a valuable substrate but also expands the capacity of acetyl-CoA supply in S. cerevisiae for efficient bioconversion of cellulosic biomass.


Genetics ◽  
2003 ◽  
Vol 163 (1) ◽  
pp. 447-452 ◽  
Author(s):  
Jeffrey S Thompson ◽  
Marilyn L Snow ◽  
Summer Giles ◽  
Leslie E McPherson ◽  
Michael Grunstein

Abstract Fourteen novel single-amino-acid substitution mutations in histone H3 that disrupt telomeric silencing in Saccharomyces cerevisiae were identified, 10 of which are clustered within the α1 helix and L1 loop of the essential histone fold. Several of these mutations cause derepression of silent mating locus HML, and an additional subset cause partial loss of basal repression at the GAL1 promoter. Our results identify a new domain within the essential core of histone H3 that is required for heterochromatin-mediated silencing.


1990 ◽  
Vol 10 (9) ◽  
pp. 4744-4756
Author(s):  
J Schultz ◽  
L Marshall-Carlson ◽  
M Carlson

The SSN6 protein functions as a negative regulator of a variety of genes in Saccharomyces cerevisiae and is required for normal growth, mating, and sporulation. It is a member of a family defined by a repeated amino acid sequence, the TPR (tetratricopeptide repeat) motif. Here, we have used specific antibody to identify and characterize the SSN6 protein. Both SSN6 and a bifunctional SSN6-beta-galactosidase fusion protein were localized in the nucleus by immunofluorescence staining. The N-terminal one-third of the protein containing the TPR units was identified as the region that is important for SSN6 function. Analysis of four nonsense alleles, isolated as intragenic suppressors of an ssn6::URA3 insertion, revealed that polypeptides truncated after TPR unit 7 provide SSN6 function. Deletion analysis suggested that TPR units are required but that 4 of the 10 TPR units are sufficient. In addition, deletion studies indicated that three very long, homogeneous tracts of polyglutamine and poly(glutamine-alanine) are dispensable. Previous genetic evidence suggested the SSN6 protein as a possible target of the SNF1 protein kinase. Here, we show that the C terminus of SSN6 is phosphorylated in vivo and that the SNF1 kinase is not responsible for most of the phosphorylation. Finally, SSN6 has a modest effect on the maintenance of minichromosomes.


2018 ◽  
Vol 215 ◽  
pp. 01027
Author(s):  
Akbarningrum Fatmawati ◽  
Tuani Lidiawati ◽  
Stephen Hadinata ◽  
Mikhael Adiarto

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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