Enhanced leavening ability of baker's yeast by overexpression of SNR84 with PGM2 deletion

J Ind Microbiol Biotechnol. 2015 Jun;42(6):939-48. doi: 10.1007/s10295-015-1618-5. Epub 2015 Apr 16.

Abstract

Dough-leavening ability is one of the main aspects considered when selecting a baker's yeast strain for baking industry. Generally, modification of maltose metabolic pathway and known regulatory networks of maltose metabolism were used to increase maltose metabolism to improve leavening ability in lean dough. In this study, we focus on the effects of PGM2 (encoding for the phosphoglucomutase) and SNR84 (encoding for the H/ACA snoRNA) that are not directly related to both the maltose metabolic pathway and known regulatory networks of maltose metabolism on the leavening ability of baker's yeast in lean dough. The results show that the modifications on PGM2 and/or SNR84 are effective ways in improving leavening ability of baker's yeast in lean dough. Deletion of PGM2 decreased cellular glucose-1-phosphate and overexpression of SNR84 increased the maltose permease activity. These changes resulted in 11, 19 and 21% increases of the leavening ability for PGM2 deletion, SNR84 overexpression and SNR84 overexpression combining deleted PGM2, respectively.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bread / microbiology*
  • Carbohydrate Metabolism / genetics*
  • Food Industry / methods
  • Gene Deletion
  • Gene Expression Regulation, Fungal
  • Genes, Fungal / genetics
  • Glucosephosphates / metabolism
  • Maltose / metabolism*
  • Monosaccharide Transport Proteins / metabolism
  • Phosphoglucomutase / deficiency*
  • Phosphoglucomutase / genetics
  • Phosphoglucomutase / metabolism
  • RNA, Small Nucleolar / genetics*
  • Saccharomyces cerevisiae / enzymology
  • Saccharomyces cerevisiae / genetics*
  • Saccharomyces cerevisiae / metabolism*

Substances

  • Glucosephosphates
  • Monosaccharide Transport Proteins
  • RNA, Small Nucleolar
  • Maltose
  • maltose permease
  • glucose-1-phosphate
  • Phosphoglucomutase