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Title: Production of alpha-amylase by yeast

Abstract

The enzyme alpha-amylase confers to an organism the enzymatic activity for the degradation of polyglucosides with alpha-1,4 glycosidic bonds such as starch and glycogen which are among the major storage compounds in plants and animals. Most alpha-amylases are single polypeptides of molecular weights around 50,000 dalton. They are generally found in the digestive tract of animals and in germinating seeds. Among the products released upon enzymatic degradation of polyglucosides maltose, a sugar that can be utilized as carbon source by yeast, is a major constituent. A cDNA segment complementary to mouse salivary amylase messenger RNA has been inserted into the yeast expression vector pMA56 behind the promoter of the gene encoding alcohol dehydrogenase I of yeast. Yeast transformants harboring plasmids with the normal orientation of the promoter and the mouse amylase cDNA gene produce amylase and release the enzyme in free form into the culture medium. Approximately 90% of the amylase activity is found in the medium. Yeast strains carrying MAL allele and transformed with a plasmid which directed the synthesis of mouse alpha-amylase were tested on plates containing starch and in batch fermentations using different high molecular weight sugars and oligosaccharides as carbon source. The results of these experimentsmore » will be discussed. (Refs. 21).« less

Authors:
Publication Date:
Research Org.:
Univ. Aarhus, Aarhus, Denmark. Dept. Physiology, Carlsberg Lab., Valby, Denmark
OSTI Identifier:
5564623
Resource Type:
Journal Article
Journal Name:
CRC Crit. Rev. Biotechnol.; (United States)
Additional Journal Information:
Journal Volume: 5:3
Country of Publication:
United States
Language:
English
Subject:
09 BIOMASS FUELS; 59 BASIC BIOLOGICAL SCIENCES; AMYLASE; DNA-CLONING; YEASTS; GENETIC ENGINEERING; DNA; GENETICS; MICE; PLASMIDS; PRODUCTION; SALIVARY GLANDS; ANIMALS; BIOLOGY; BODY; CELL CONSTITUENTS; CLONING; ENZYMES; FUNGI; GLANDS; GLYCOSYL HYDROLASES; HYDROLASES; MAMMALS; MICROORGANISMS; NUCLEIC ACIDS; O-GLYCOSYL HYDROLASES; ORGANIC COMPOUNDS; ORGANS; PLANTS; RODENTS; VERTEBRATES; 140504* - Solar Energy Conversion- Biomass Production & Conversion- (-1989); 550200 - Biochemistry

Citation Formats

Thomse, K K. Production of alpha-amylase by yeast. United States: N. p., 1987. Web. doi:10.3109/07388558709086979.
Thomse, K K. Production of alpha-amylase by yeast. United States. https://doi.org/10.3109/07388558709086979
Thomse, K K. 1987. "Production of alpha-amylase by yeast". United States. https://doi.org/10.3109/07388558709086979.
@article{osti_5564623,
title = {Production of alpha-amylase by yeast},
author = {Thomse, K K},
abstractNote = {The enzyme alpha-amylase confers to an organism the enzymatic activity for the degradation of polyglucosides with alpha-1,4 glycosidic bonds such as starch and glycogen which are among the major storage compounds in plants and animals. Most alpha-amylases are single polypeptides of molecular weights around 50,000 dalton. They are generally found in the digestive tract of animals and in germinating seeds. Among the products released upon enzymatic degradation of polyglucosides maltose, a sugar that can be utilized as carbon source by yeast, is a major constituent. A cDNA segment complementary to mouse salivary amylase messenger RNA has been inserted into the yeast expression vector pMA56 behind the promoter of the gene encoding alcohol dehydrogenase I of yeast. Yeast transformants harboring plasmids with the normal orientation of the promoter and the mouse amylase cDNA gene produce amylase and release the enzyme in free form into the culture medium. Approximately 90% of the amylase activity is found in the medium. Yeast strains carrying MAL allele and transformed with a plasmid which directed the synthesis of mouse alpha-amylase were tested on plates containing starch and in batch fermentations using different high molecular weight sugars and oligosaccharides as carbon source. The results of these experiments will be discussed. (Refs. 21).},
doi = {10.3109/07388558709086979},
url = {https://www.osti.gov/biblio/5564623}, journal = {CRC Crit. Rev. Biotechnol.; (United States)},
number = ,
volume = 5:3,
place = {United States},
year = {Thu Jan 01 00:00:00 EST 1987},
month = {Thu Jan 01 00:00:00 EST 1987}
}