The Production and Characterization of Penicillin G Acylase from Bacillus Thuringiensis BGSC BD1 Wild Type

Rizky Aulia Prasasti Dewi; Erma Widyasti; Deden Rosid Waltam; Edi Wahjono; Nuur Faridatun Hasanah; Siswa Setyahadi; Nurul Apsari Aji; Dewi Nandyawati; Eko Santoso; Dini Achnafani; Ayi Mufti; Molina Indah Pradiv; Kharis Yohan Abidin

doi:10.1063/5.0201503

The Production and Characterization of Penicillin G Acylase from Bacillus Thuringiensis BGSC BD1 Wild Type

Rizky Aulia Prasasti Dewi, Erma Widyasti, Deden Rosid Waltam, Edi Wahjono, Dianursanti, Nuur Faridatun Hasanah, Siswa Setyahadi, Nurul Apsari Aji, Dewi Nandyawati, Eko Santoso, Dini Achnafani, Ayi Mufti, Molina Indah Pradiv, Kharis Yohan Abidin

Department of Chemical Engineering

Research output: Contribution to journal › Conference article › peer-review

Abstract

Penicillin G Acylase (PGA) is the responsible enzyme for hydrolysis of ß-lactams antibiotics. It became important since the majority process to produce these antibiotics turn into enzymatic. One which is amoxicillin. In this study, a wild type of Bacillus thuringiensis BGSC BD1 among three other isolates from Bioindustrial Lab, LAPTIAB, BRIN Culture Collection are selected as the best producer of the enzyme. The PGA production in LB media for five trials resulting the stable PGA activity of about 3 U/ml with harvesting time at 20 hours of fermentation. The characterization of the enzyme showed optimum activity in a pH range of 7 to 8 with maximum temperature up to 60 °C. The SDS-PAGE result showed two bands with molecular weights around 26 and41 kDa that represent the a and ß units of PGA.

Original language	English
Article number	040001
Journal	AIP Conference Proceedings
Volume	3080
Issue number	1
DOIs	https://doi.org/10.1063/5.0201503
Publication status	Published - 7 Mar 2024
Event	15th Asian Congress on Biotechnology in conjunction with the 7th International Symposium on Biomedical Engineering, ACB-ISBE 2022 - Bali, Indonesia Duration: 2 Oct 2022 → 6 Oct 2022

Keywords

Amoxicillin
Bacillus thuringiensis
Characterization
Penicillin G Acylase (PGA)
Wild Type

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10.1063/5.0201503

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Dewi, R. A. P., Widyasti, E., Waltam, D. R., Wahjono, E., Dianursanti, Hasanah, N. F., Setyahadi, S., Aji, N. A., Nandyawati, D., Santoso, E., Achnafani, D., Mufti, A., Pradiv, M. I., & Abidin, K. Y. (2024). The Production and Characterization of Penicillin G Acylase from Bacillus Thuringiensis BGSC BD1 Wild Type. AIP Conference Proceedings, 3080(1), Article 040001. https://doi.org/10.1063/5.0201503

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title = "The Production and Characterization of Penicillin G Acylase from Bacillus Thuringiensis BGSC BD1 Wild Type",

abstract = "Penicillin G Acylase (PGA) is the responsible enzyme for hydrolysis of {\ss}-lactams antibiotics. It became important since the majority process to produce these antibiotics turn into enzymatic. One which is amoxicillin. In this study, a wild type of Bacillus thuringiensis BGSC BD1 among three other isolates from Bioindustrial Lab, LAPTIAB, BRIN Culture Collection are selected as the best producer of the enzyme. The PGA production in LB media for five trials resulting the stable PGA activity of about 3 U/ml with harvesting time at 20 hours of fermentation. The characterization of the enzyme showed optimum activity in a pH range of 7 to 8 with maximum temperature up to 60 °C. The SDS-PAGE result showed two bands with molecular weights around 26 and41 kDa that represent the a and {\ss} units of PGA.",

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author = "Dewi, {Rizky Aulia Prasasti} and Erma Widyasti and Waltam, {Deden Rosid} and Edi Wahjono and Dianursanti and Hasanah, {Nuur Faridatun} and Siswa Setyahadi and Aji, {Nurul Apsari} and Dewi Nandyawati and Eko Santoso and Dini Achnafani and Ayi Mufti and Pradiv, {Molina Indah} and Abidin, {Kharis Yohan}",

note = "Publisher Copyright: {\textcopyright} 2024 American Institute of Physics Inc.. All rights reserved.; 15th Asian Congress on Biotechnology in conjunction with the 7th International Symposium on Biomedical Engineering, ACB-ISBE 2022 ; Conference date: 02-10-2022 Through 06-10-2022",

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Dewi, RAP, Widyasti, E, Waltam, DR, Wahjono, E, Dianursanti, Hasanah, NF, Setyahadi, S, Aji, NA, Nandyawati, D, Santoso, E, Achnafani, D, Mufti, A, Pradiv, MI & Abidin, KY 2024, 'The Production and Characterization of Penicillin G Acylase from Bacillus Thuringiensis BGSC BD1 Wild Type', AIP Conference Proceedings, vol. 3080, no. 1, 040001. https://doi.org/10.1063/5.0201503

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T1 - The Production and Characterization of Penicillin G Acylase from Bacillus Thuringiensis BGSC BD1 Wild Type

AU - Dewi, Rizky Aulia Prasasti

AU - Widyasti, Erma

AU - Waltam, Deden Rosid

AU - Wahjono, Edi

AU - Dianursanti,

AU - Hasanah, Nuur Faridatun

AU - Setyahadi, Siswa

AU - Aji, Nurul Apsari

AU - Nandyawati, Dewi

AU - Santoso, Eko

AU - Achnafani, Dini

AU - Mufti, Ayi

AU - Pradiv, Molina Indah

AU - Abidin, Kharis Yohan

PY - 2024/3/7

Y1 - 2024/3/7

N2 - Penicillin G Acylase (PGA) is the responsible enzyme for hydrolysis of ß-lactams antibiotics. It became important since the majority process to produce these antibiotics turn into enzymatic. One which is amoxicillin. In this study, a wild type of Bacillus thuringiensis BGSC BD1 among three other isolates from Bioindustrial Lab, LAPTIAB, BRIN Culture Collection are selected as the best producer of the enzyme. The PGA production in LB media for five trials resulting the stable PGA activity of about 3 U/ml with harvesting time at 20 hours of fermentation. The characterization of the enzyme showed optimum activity in a pH range of 7 to 8 with maximum temperature up to 60 °C. The SDS-PAGE result showed two bands with molecular weights around 26 and41 kDa that represent the a and ß units of PGA.

AB - Penicillin G Acylase (PGA) is the responsible enzyme for hydrolysis of ß-lactams antibiotics. It became important since the majority process to produce these antibiotics turn into enzymatic. One which is amoxicillin. In this study, a wild type of Bacillus thuringiensis BGSC BD1 among three other isolates from Bioindustrial Lab, LAPTIAB, BRIN Culture Collection are selected as the best producer of the enzyme. The PGA production in LB media for five trials resulting the stable PGA activity of about 3 U/ml with harvesting time at 20 hours of fermentation. The characterization of the enzyme showed optimum activity in a pH range of 7 to 8 with maximum temperature up to 60 °C. The SDS-PAGE result showed two bands with molecular weights around 26 and41 kDa that represent the a and ß units of PGA.

KW - Amoxicillin

KW - Bacillus thuringiensis

KW - Characterization

KW - Penicillin G Acylase (PGA)

KW - Wild Type

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U2 - 10.1063/5.0201503

DO - 10.1063/5.0201503

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AN - SCOPUS:85188470580

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VL - 3080

JO - AIP Conference Proceedings

JF - AIP Conference Proceedings

IS - 1

M1 - 040001

T2 - 15th Asian Congress on Biotechnology in conjunction with the 7th International Symposium on Biomedical Engineering, ACB-ISBE 2022

Y2 - 2 October 2022 through 6 October 2022

ER -

The Production and Characterization of Penicillin G Acylase from Bacillus Thuringiensis BGSC BD1 Wild Type

Abstract

Keywords

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