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Heterologous expression of the plant cysteine protease bromelain and its inhibitor in Pichia pastoris.
Biotechnol Prog. 2017 01; 33(1):54-65.BP

Abstract

Expression of proteases in heterologous hosts remains an ambitious challenge due to severe problems associated with digestion of host proteins. On the other hand, proteases are broadly used in industrial applications and resemble promising drug candidates. Bromelain is an herbal drug that is medicinally used for treatment of oedematous swellings and inflammatory conditions and consists in large part of proteolytic enzymes. Even though various experiments underline the requirement of active cysteine proteases for biological activity, so far no investigation succeeded to clearly clarify the pharmacological mode of action of bromelain. The potential role of proteases themselves and other molecules of this multi-component extract currently remain largely unknown or ill defined. Here, we set out to express several bromelain cysteine proteases as well as a bromelain inhibitor molecule in order to gain defined molecular entities for subsequent studies. After cloning the genes from its natural source Ananas comosus (pineapple plant) into Pichia pastoris and subsequent fermentation and purification, we obtained active protease and inhibitor molecules which were subsequently biochemically characterized. Employing purified bromelain fractions paves the way for further elucidation of pharmacological activities of this natural product. © 2016 American Institute of Chemical Engineers Biotechnol. Prog., 33:54-65, 2017.

Authors+Show Affiliations

Ursapharm Arzneimittel GmbH, Industriestraβe 35, Saarbrücken, 66129, Germany.Ursapharm Arzneimittel GmbH, Industriestraβe 35, Saarbrücken, 66129, Germany.PharmBioTec GmbH, Science Park 1, Saarbrücken, 66123, Germany.Helmholtz Institute for Pharmaceutical Research Saarland, Department of Microbial Natural Products, Helmholtz Centre for Infection Research and Pharmaceutical Biotechnology at Saarland University, Saarbrücken, 66041, Germany.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

27860461

Citation

Luniak, Nora, et al. "Heterologous Expression of the Plant Cysteine Protease Bromelain and Its Inhibitor in Pichia Pastoris." Biotechnology Progress, vol. 33, no. 1, 2017, pp. 54-65.
Luniak N, Meiser P, Burkart S, et al. Heterologous expression of the plant cysteine protease bromelain and its inhibitor in Pichia pastoris. Biotechnol Prog. 2017;33(1):54-65.
Luniak, N., Meiser, P., Burkart, S., & Müller, R. (2017). Heterologous expression of the plant cysteine protease bromelain and its inhibitor in Pichia pastoris. Biotechnology Progress, 33(1), 54-65. https://doi.org/10.1002/btpr.2405
Luniak N, et al. Heterologous Expression of the Plant Cysteine Protease Bromelain and Its Inhibitor in Pichia Pastoris. Biotechnol Prog. 2017;33(1):54-65. PubMed PMID: 27860461.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Heterologous expression of the plant cysteine protease bromelain and its inhibitor in Pichia pastoris. AU - Luniak,Nora, AU - Meiser,Peter, AU - Burkart,Sonja, AU - Müller,Rolf, Y1 - 2016/11/29/ PY - 2016/09/07/received PY - 2016/11/08/revised PY - 2016/11/20/pubmed PY - 2017/12/13/medline PY - 2016/11/19/entrez KW - Pichia pastoris KW - bromelain KW - bromelain inhibitor KW - cysteine protease KW - heterologous expression SP - 54 EP - 65 JF - Biotechnology progress JO - Biotechnol. Prog. VL - 33 IS - 1 N2 - Expression of proteases in heterologous hosts remains an ambitious challenge due to severe problems associated with digestion of host proteins. On the other hand, proteases are broadly used in industrial applications and resemble promising drug candidates. Bromelain is an herbal drug that is medicinally used for treatment of oedematous swellings and inflammatory conditions and consists in large part of proteolytic enzymes. Even though various experiments underline the requirement of active cysteine proteases for biological activity, so far no investigation succeeded to clearly clarify the pharmacological mode of action of bromelain. The potential role of proteases themselves and other molecules of this multi-component extract currently remain largely unknown or ill defined. Here, we set out to express several bromelain cysteine proteases as well as a bromelain inhibitor molecule in order to gain defined molecular entities for subsequent studies. After cloning the genes from its natural source Ananas comosus (pineapple plant) into Pichia pastoris and subsequent fermentation and purification, we obtained active protease and inhibitor molecules which were subsequently biochemically characterized. Employing purified bromelain fractions paves the way for further elucidation of pharmacological activities of this natural product. © 2016 American Institute of Chemical Engineers Biotechnol. Prog., 33:54-65, 2017. SN - 1520-6033 UR - https://www.unboundmedicine.com/medline/citation/27860461/Heterologous_expression_of_the_plant_cysteine_protease_bromelain_and_its_inhibitor_in_Pichia_pastoris_ L2 - https://doi.org/10.1002/btpr.2405 DB - PRIME DP - Unbound Medicine ER -