Reduction of endogenous nucleic acid in a single-cell protein.

AUTOR(ES)

Yang, H H

RESUMO

The reduction of nucleic acid by an endogenous polynucleotide phosphorylase and ribonuclease in cells of Brevibacterium JM98A (ATCC 29895) was studied. A simple process was developed for the activation of the endogenous RNA-degrading enzyme(s). RNA degradation was activated by the presence of Pi with 14.2 mumol of ribonucleoside 5'-monophosphate per g of cell mass accumulating extracellularly. The optimum pH for degradation of RNA was 10.5 and the optimum temperature was 55 to 60 degrees C. Enzymatic activity was inhibited by the presence of Ca2+, Zn2+, or Mg2+. Although some of the RNA-degrading enzymatic activity was associated with the ribosomal fraction, most was soluble. Both polynucleotide phosphorylase and ribonuclease activities were identified.

Documentos Relacionados

• Single-Cell Protein Production in Alkaline Mesquite Wood Extracts
• Amino acid profiles and presumptive nutritional assessment of single-cell protein from certain lactobacilli.
• Single-Cell Protein Profiling of Wastewater Enterobacterial Communities Predicts Disinfection Efficiency
• Single-Cell Protein Production by the Acid-Tolerant Fungus Scytalidium acidophilum from Acid Hydrolysates of Waste Paper †
• Lack of allergic reactions in workers exposed to Pruteen (bacterial single-cell protein).