Aspergillus niger에서 단백질분해효소 결함 돌연변이주의 제조 및 특성규명

  • 정헌세 (충남대학교 미생물학과) ;
  • 채순기 (배재대학교 생화학과) ;
  • 박희문 (충남대학교 미생물학과) ;
  • 맹필재 (충남대학교 미생물학과) ;
  • 김정윤 (충남대학교 미생물학과)
  • Published : 1997.08.01

Abstract

Several protease-deficient mutants of Aspergillus niger have been isolated by halo-screening on skim milk plate after UV irradiation of conidiospores. The extracellular proteolytic activities of the mutant strains grown in an optimized medium varied from 3% to 85% of that of the parental strain. Especially, two mutant strains named as ANPD-129 and ANPD-153, which had 3% and 49% of acid protease activity of the parental strain, respectively, were further characterized both physiologically and genetically. The growth rates of the mutants, ANPD-129 and ANPD-153, were similar to that of the parental strain, unlike other protease-deficient mutants. The diploid formed between the two mutants restored protease activity to a similar level of that of the parental strain. This result revealed that ANPD-129 and ANPD-153 had mutations at different loci. Using master strains with marked chromosomes these loci were assigned to linkage groups. The mutation locus (prt129) in ANPD-129 was assigned to linkage group VI and the locus (prt153) in ANPD-153 to linkage group III.

Keywords

References

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