แจ้งเอกสารไม่ครบถ้วน, ไม่ตรงกับชื่อเรื่อง หรือมีข้อผิดพลาดเกี่ยวกับเอกสาร ติดต่อที่นี่ ==>
หากไม่มีอีเมลผู้รับให้กรอก thailis-noc@uni.net.th
หากไม่มีอีเมลผู้รับให้กรอก thailis-noc@uni.net.th
Kanchana Weeradechapon. Nucleotide sequence analysis and strain improvement for high expression of penicillin G acylase gene from Bacillus megaterium UN-1. Master's Degree(Microbiology). Mahidol University. Mahidol University Library and Knowledge Center. : Mahidol University, 1993.
Nucleotide sequence analysis and strain improvement for high expression of penicillin G acylase gene from Bacillus megaterium UN-1
การหาลำดับ nucleotide และการปรับปรุงสายพันธุ์ของ Bacillus megaterium UN-1 ที่สร้างเอนไซม์ penicillin G acylase
Name: Kanchana Weeradechapon
MeSH:
Bacillus megaterium
MeSH:
Base sequence
MeSH:
Penicillin G
Abstract:
Penicillin G acylase (PAC) catalyzes the hydrolysis of benzylpenicillin to 6-aminoper,icillanic acid (6-APA), a key intermediate, in the synthesis of semisynthetic peniciliins. The penicillin G acylase gene (pac) gene was isolated from Bacillus megaterium UN-1, a high penicillin G acylase producer mutant of Bacillus megaterium ATCC 14945. Complete nucleotide sequence of pac gene was determined and found that the gene contained an open reading frame encoding for 802 amino acids with MW of about 92,000 Da. This polypeptide consisted of a 26 amino acid signal peptide. The putative -35 and -10 sequences were TTGAAT and TATAAG, respectively. Comparison of pac nucleotide sequence to that from Arthrobacter viscosus revealed 97% homology. Results from SDS-PAGE suggested that the penicillin G acylase of Bacillus megaterium UN-1 comprised of two subunits MW of about 23,000 Da and 57,000 Da. Therefore, this enzyme seem to be synthesized first as a single polypeptide and later being processed during maturation to two subunits as reported in the other pac gene of various microorganisms. In order to increase the yield of enzyme production, four plasmids containing pac gene were constructed and transformed to Bacillus megaterium UN-CAT1, a penicillin G acylase negative mutant of Bacillus megaterium UN-1, and Bacillus subtilis MI113. The expression of the plasmids containing pac gene in Bacillus megaterium UN-CAT1, the mutant host, was higher than that in Bacillus subtilis MI113. The penicillin G acylase activity in Bacillus megaterium UN-CAT1 and Bacillus subtilis MI113, both carrying pBA402, a plasmid containing pac gene with its self-promoter ) were approximate 26 times and 13 times higher than that in Bacillus megaterium UN-1, a donor penicillin G acylase producer which contained no plasmid. Hence, Bacillus megaterium UN-CAT1 carrying pBA402, is a good potential strain to be used for penicillin G acylase production.
Mahidol University. Mahidol University Library and Knowledge Center
Address:
NAKHONPATHOM
Email:
liwww@mahidol.ac.th
Name: Watanalai Panbangred
Role:
Thesis Advisors
Name: Vithaya Meevootisom
Role:
Thesis Advisors
Name: Chuenchit Boonchird
Role:
Thesis Advisors
Created:
1993
Modified:
2561-02-19
Issued:
2018-02-17
วิทยานิพนธ์/Thesis
application/pdf
eng
DegreeName: Master of Science
Level: Master's Degree
Descipline: Microbiology
Grantor: Mahidol University
©copyrights Mahidol University
RightsAccess:
ใช้เวลา
0.236336 วินาที
Kanchana Weeradechapon
| Title | Contributor | Type |
|---|---|---|
| Nucleotide sequence analysis and strain improvement for high expression of penicillin G acylase gene from Bacillus megaterium UN-1
มหาวิทยาลัยมหิดล Kanchana Weeradechapon | Watanalai Panbangred Vithaya Meevootisom Chuenchit Boonchird | วิทยานิพนธ์/Thesis |
Watanalai Panbangred
Vithaya Meevootisom
Chuenchit Boonchird