Journal of Microbiology

Journal Articles

Comparative Secretory Efficiency of Two Chitosanase Signal Peptides from Bacillus subtilis in Escherichia coli: Tae-Yang Eom, Yehui Gang, Youngdeuk Lee, Yoon-Hyeok Kang, Eunyoung Jo, Svini Dileepa Marasinghe, Heung Sik Park, Gun-Hoo Park, Chulhong Oh; J. Microbiol. 2024;62(12):1155-1164. Published online November 25, 2024; DOI: https://doi.org/10.1007/s12275-024-00186-1

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Abstract: The production of recombinant proteins in Escherichia coli is often challenged by cytoplasmic expression due to proteolytic degradation and inclusion body formation. Extracellular expression can overcome these problems by simplifying downstream processing and improving protein yields. This study aims to compare the efficiency of two Bacillus subtilis chitosanase signal peptides in mediating extracellular secretion in E. coli. We identified a naturally occurring mutant signal peptide (mCsn2-SP) from B. subtilis CH2 chitosanase (CH2CSN), which is characterized by a deletion of six amino acids in the N-region relative to the signal peptide (Csn1-SP) from B. subtilis CH1 chitosanase (CH1CSN). The CH1CSN and CH2CSN genes were cloned into the pET-11a vector and protein secretion was evaluated in E. coli BL21(DE3) host cells. Expression was induced with 0.1 mM and 1 mM isopropyl β-D-1-thiogalactopyranoside (IPTG) at 30 °C for one and three days. CH2CSN showed higher secretion levels compared to CH1CSN under all experimental conditions, especially with 0.1 mM IPTG induction for 3 days, which resulted in a 2.37-fold increase in secretion. Furthermore, it was demonstrated that mCsn2-SP is capable of secreting human Cu,Zn-superoxide dismutase (hSOD) in E. coli BL21(DE3) and successfully translocating it to the periplasmic region. This study represents the inaugural investigation into the utilisation of a naturally modified signal peptide, thereby corroborating the assertion that signal peptide deletion variants can influence protein secretion efficiency. Furthermore, the findings substantiate the proposition that such variants can serve as a viable alternative for the secretion of heterologous proteins in E. coli.

Mycobacterium tuberculosis PE_PGRS45 (Rv2615c) Promotes Recombinant Mycobacteria Intracellular Survival via Regulation of Innate Immunity, and Inhibition of Cell Apoptosis: Tao Xu , Chutong Wang , Minying Li , Jing Wei , Zixuan He , Zhongqing Qian , Xiaojing Wang , Hongtao Wang; J. Microbiol. 2024;62(1):49-62. Published online February 9, 2024; DOI: https://doi.org/10.1007/s12275-023-00101-0

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Tuberculosis (TB), a bacterial infectious disease caused by Mycobacterium tuberculosis (M. tuberculosis), is a significant global public health problem. Mycobacterium tuberculosis expresses a unique family of PE_PGRS proteins that have been implicated in pathogenesis. Despite numerous studies, the functions of most PE_PGRS proteins in the pathogenesis of mycobacterium infections remain unclear. PE_PGRS45 (Rv2615c) is only found in pathogenic mycobacteria. In this study, we successfully constructed a recombinant Mycobacterium smegmatis (M. smegmatis) strain which heterologously expresses the PE_PGRS45 protein. We found that overexpression of this cell wall-associated protein enhanced bacterial viability under stress in vitro and cell survival in macrophages. MS_PE_PGRS45 decreased the secretion of pro-inflammatory cytokines such as IL-1β, IL-6, IL-12p40, and TNF-α. We also found that MS_PE_PGRS45 increased the expression of the anti-inflammatory cytokine IL-10 and altered macrophage-mediated immune responses. Furthermore, PE_PGRS45 enhanced the survival rate of M. smegmatis in macrophages by inhibiting cell apoptosis. Collectively, our findings show that PE_PGRS45 is a virulent factor actively involved in the interaction with the host macrophage.

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Evolution of the PE_PGRS Proteins of Mycobacteria: Are All Equal or Are Some More Equal than Others?
Bei Chen, Belmin Bajramović, Bastienne Vriesendorp, Herman Pieter Spaink
Biology.2025; 14(3): 247. CrossRef
Recent advances in research on Mycobacterium tuberculosis virulence factors and their role in pathogenesis
Ming-Rui Sun, Jia-Yin Xing, Xiao-Tian Li, Ren Fang, Yang Zhang, Zhao-Li Li, Ning-Ning Song
Journal of Microbiology, Immunology and Infection.2025;[Epub] CrossRef
Rv2741 Promotes Mycobacterium Survival by Modulating Macrophage Function via the IL-1α-MAPK Axis
Xintong He, Yonglin He, Xichuan Deng, Nan Lu, Anlong Li, Sijia Gao, Shiyan He, Yuran Wang, Nanzhe Fu, Zijie Wang, Yuxin Nie, Lei Xu
ACS Infectious Diseases.2025; 11(3): 676. CrossRef

Nano-encapsulation of naringinase produced by Trichoderma longibrachiatum ATCC18648 on thermally stable biopolymers for citrus juice debittering: Manal M. Housseiny , Heba I. Aboelmagd; J. Microbiol. 2019;57(6):521-531. Published online May 27, 2019; DOI: https://doi.org/10.1007/s12275-019-8528-6

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Abstract

Characteristics of naringinase nano-encapsulated forms on different carrier materials (chitosan and alginate polymers) were investigated in this study. Screening of twelve fungal isolates for naringinase production indicated that Trichoderma longibrachiatum was the most promising. Grapefruit rind was used as a substrate containing naringin for naringinase production. TEM micrographs showed that chitosan nano-capsules were applied for the production of morphologically homogeneous enzymatic nano-particles with high enzyme encapsulation efficiency, small asymmetric sizes (from 15.09 to 27.07 nm with the mean of 21.8 nm) and rough surfaces compared to nano-encapsulated naringinase in alginate which showed nano-particle size (from 33.37 to 51.01 nm with the mean of 43.03 nm). It was revealed that the highest naringinase activity was found in case of chitosan nano-capsule naringinase compared to alginate nano-capsule one. Thermogram analysis (TGA) showed that the free enzyme loses about 92% of its weight at approximately 110°C, while the nanoencapsulated ones show more stability at higher temperatures. Conclusively, the nano-capsulation process improves the kinetics and operational stability so could be useful as a debittering agent for various thermal processing applications in citrus juices industries which makes the fruit juice more acceptable and cost-effective to the consumer.

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Recent advancements in encapsulation of chitosan-based enzymes and their applications in food industry
Hongcai Zhang, Miaomiao Feng, Yapeng Fang, Yan Wu, Yuan Liu, Yanyun Zhao, Jianxiong Xu
Critical Reviews in Food Science and Nutrition.2023; 63(32): 11044. CrossRef
Alginate-based materials for enzyme encapsulation
Yilun Weng, Guangze Yang, Yang Li, Letao Xu, Xiaojing Chen, Hao Song, Chun-Xia Zhao
Advances in Colloid and Interface Science.2023; 318: 102957. CrossRef
Design and development of laboratory scale batch type device for debittering of bitter citrus juice
Arun Kumar Gupta, Muzamil Ahmad Rather, Poonam Mishra
Journal of Food Process Engineering.2023;[Epub] CrossRef
Current and emerging applications in detection and removal of bitter compounds in citrus fruit juice: A critical review
Arun Kumar Gupta, Subhamoy Dhua, Pratiksha, Vijay Kumar, Bindu Naik, Lembe Samukelo Magwaza, Khayelihle Ncama, Umezuruike Linus Opara, David Julian McClements, Poonam Mishra
Food Bioscience.2023; 55: 102995. CrossRef
Isolation and Molecular Characterization of the Naringinase Producing Micro-organisms for the Bio-transformation of Flavonoid
Ananda Sindhe, K. Lingappa
Journal of Pure and Applied Microbiology.2023; 17(1): 456. CrossRef
Preparation of Aspergillus niger 426 naringinases for debittering citrus juice utilization of agro-industrial residues
Fernanda de Oliveira, Tereza Cristina Luque Castellane, Marcelo Rodrigues de Melo, João Batista Buzato
International Microbiology.2022; 25(1): 123. CrossRef
Trends in the development of innovative nanobiocatalysts and their application in biocatalytic transformations
Elena Gkantzou, Alexandra V. Chatzikonstantinou, Renia Fotiadou, Archontoula Giannakopoulou, Michaela Patila, Haralambos Stamatis
Biotechnology Advances.2021; 51: 107738. CrossRef
Recent developments in enzyme immobilization technology for high-throughput processing in food industries
Asghar Taheri-Kafrani, Sara Kharazmi, Mahmoud Nasrollahzadeh, Asieh Soozanipour, Fatemeh Ejeian, Parisa Etedali, Hajar-Alsadat Mansouri-Tehrani, Amir Razmjou, Samaneh Mahmoudi-Gom Yek, Rajender S. Varma
Critical Reviews in Food Science and Nutrition.2021; 61(19): 3160. CrossRef
Polymers as Encapsulating Agents and Delivery Vehicles of Enzymes
Adejanildo da S. Pereira, Camila P. L. Souza, Lidiane Moraes, Gizele C. Fontes-Sant’Ana, Priscilla F. F. Amaral
Polymers.2021; 13(23): 4061. CrossRef

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