Conversion of dextrinized cassava starch into ethanol using cultures of Aspergillus awamori and Saccharomyces cerevisiae

1984 ◽  
Vol 6 (2) ◽  
pp. 60-64 ◽  
Author(s):  
Ernesto J. del Rosario ◽  
Roberto L. Wong
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cassava Starch ◽  
Aspergillus Awamori

Evaluation of the waste from cassava starch production as a substrate for ethanol fermentation by Saccharomyces cerevisiae

2010 ◽  
Vol 61 (3) ◽  
pp. 431-436 ◽  
Author(s):  
Ancharida Akaracharanya ◽  
Jutarat Kesornsit ◽  
Natchanun Leepipatpiboon ◽  
Teerapatr Srinorakutara ◽  
Vichien Kitpreechavanich ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Ethanol Fermentation ◽  
Cassava Starch ◽  
Starch Production

scholarly journals Antagonistic lactic acid bacteria in association with Saccharomyces cerevisiae as starter cultures for standardization of sour cassava starch production

2019 ◽  
Vol 56 (9) ◽  
pp. 3969-3979
Author(s):  
Fernanda Corrêa Leal Penido ◽  
Carmen de Oliveira Goulart ◽  
Yara Cristina Fidelis Galvão ◽  
Carolina Vasconcelos Teixeira ◽  
Roseane Batitucci Passos de Oliveira ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Lactic Acid ◽  
Lactic Acid Bacteria ◽  
Cassava Starch ◽  
Starter Cultures ◽  
Starch Production

scholarly journals Substitution of asparagine residues in Aspergillus awamori glucoamylase by site-directed mutagenesis to eliminate N-glycosylation and inactivation by deamidation

1994 ◽  
Vol 301 (1) ◽  
pp. 275-281 ◽  
Author(s):  
H M Chen ◽  
C Ford ◽  
P J Reilly
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Membrane ◽  
Specific Activity ◽  
Site Directed Mutagenesis ◽  
Aspergillus Awamori ◽  
Directed Mutagenesis ◽  
Wild Type ◽  
Wild Type Enzyme ◽  
Recognition Sites ◽  
Membrane Components

Aspergillus awamori glucoamylase is a secreted glycoprotein containing N-linked carbohydrate recognition sites at Asn-171, Asn-182 and Asn-395. Site-directed mutagenesis was performed at Asn-182 and Asn-395 to determine whether these residues were N-glycosylated by Saccharomyces cerevisiae, to investigate the function of any glycans linked to them, and to determine the effect of their deamidation on glucoamylase thermostability. Asn-171 and Asn-395, but not Asn-182, were N-glycosylated. Deletion of the glycan N-linked to Asn-395 did not affect specific activity, but greatly decreased enzyme secretion and thermostability. The mutant lacking the N-glycan linked to Asn-395 was synthesized very slowly, and was more associated with cell membrane components and susceptible to proteinase degradation than were wild-type or other mutant glucoamylases. Its secreted form was 30-fold less thermostable than wild-type enzyme at pH 4.5. Replacement of Asn-182 by Gln to eliminate deamidation at this site did not change glucoamylase specific activity or thermostability, while replacement by Asp decreased specific activity about 25%, but increased thermostability moderately at pH 4.5 below 70 degrees C. Both mutations of Asn-182 increased glucoamylase production.

Sign in / Sign up

Export Citation Format

Share Document