Enhancement of alkaline protease production in recombinant Bacillus licheniformis by response surface methodology

Zhang, Ying; Hu, Junfeng; Zhang, Qing; Cai, Dongbo; Chen, Shouwen; Wang, Yonghong

doi:10.1186/s40643-023-00641-8

Cited by 9 publications

(6 citation statements)

References 34 publications

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“…The relevant data of the quadratic regression analysis were acquired. [48,49]. The p < 0.05 of TA-04 mutant strain in Table 1 indicates that the model is significant.…”

Section: Experimental Findings Based On the Box-behnken Designmentioning

confidence: 91%

Comprehensive Analysis of Catalytic Characteristics and Molecular Mechanisms in Mutant Trametes versicolor Strains with Enhanced Laccase Activities

Zhang,

Yan,

et al. 2023

Fermentation

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The commercial potential of Trametes versicolor laccases in the degradation of various persistent contaminants is significant. Despite numerous attempts through rational metabolic engineering to enhance the properties of laccases, the outcomes have proven unsatisfactory for practical implementation. The present study successfully generated two novel mutants, namely, TA-04 and TA-15, derived from Trametes versicolor ATCC20869, utilizing atmospheric and room temperature plasma (ARTP). The laccase activities of TA-04 and TA-15 showed a significant increase to 136.507 ± 4.827 U/mg DCW and 153.804 ± 6.884 U/mg DCW, respectively, which were 1.201 and 1.354 times than that of the original strain. The laccase activities of the mutant strains TA-04 and TA-15 surpassed that of the original strain by 10.372% and 18.914%, respectively, at a higher pH level of five. Sequencing analysis of TA-04 and TA-15 revealed that several alternative amino acids within their active regions may enhance their catalytic characteristics under a higher temperature and pH condition. This study employed ARTP mutagenesis to propose two highly efficient microbial mutants derived from Trametes versicolor ATCC20869, exhibiting enhanced laccase activities. These mutants hold promising potential for the degradation of diverse environmental pollutants.

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“…The relevant data of the quadratic regression analysis were acquired. [48,49]. The p < 0.05 of TA-04 mutant strain in Table 1 indicates that the model is significant.…”

Section: Experimental Findings Based On the Box-behnken Designmentioning

confidence: 91%

Comprehensive Analysis of Catalytic Characteristics and Molecular Mechanisms in Mutant Trametes versicolor Strains with Enhanced Laccase Activities

Zhang,

Yan,

et al. 2023

Fermentation

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“…Isolation of salt-tolerant microorganisms from these environments requires many steps such as sample collection, isolation of strains, morphological characteristics and molecular sequence identification of strains (Abanoz et al 2017 ). To obtain excellent STP-producing strains, additional steps such as optimizing enzyme production conditions and evaluating the enzyme production capacity of the microorganism based on the enzyme activity index have been implemented (Wahab and Ahmed 2018 ; Zhang et al 2023 ). While microorganisms obtained through conventional screening methods exhibit high salt tolerance and stable enzyme production capacity, limitations such as low screening efficiency and time consumption may restrict their widespread application.…”

Section: Study On Microorganisms Producing Stpsmentioning

confidence: 99%

Microbial-derived salt-tolerant proteases and their applications in high-salt traditional soybean fermented foods: a review

Yao,

Liu,

Liu

et al. 2023

Bioresour. Bioprocess.

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Different microorganisms can produce different proteases, which can adapt to different industrial requirements such as pH, temperature, and pressure. Salt-tolerant proteases (STPs) from microorganisms exhibit higher salt tolerance, wider adaptability, and more efficient catalytic ability under extreme conditions compared to conventional proteases. These unique enzymes hold great promise for applications in various industries including food, medicine, environmental protection, agriculture, detergents, dyes, and others. Scientific studies on microbial-derived STPs have been widely reported, but there has been little systematic review of microbial-derived STPs and their application in high-salt conventional soybean fermentable foods. This review presents the STP-producing microbial species and their selection methods, and summarizes and analyzes the salt tolerance mechanisms of the microorganisms. It also outlines various techniques for the isolation and purification of STPs from microorganisms and discusses the salt tolerance mechanisms of STPs. Furthermore, this review demonstrates the contribution of modern biotechnology in the screening of novel microbial-derived STPs and their improvement in salt tolerance. It highlights the potential applications and commercial value of salt-tolerant microorganisms and STPs in high-salt traditional soy fermented foods. The review ends with concluding remarks on the challenges and future directions for microbial-derived STPs. This review provides valuable insights into the separation, purification, performance enhancement, and application of microbial-derived STPs in traditional fermented foods. Graphical Abstract

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“…Exploring microbial diversity has immense potential for discovering novel enzymes with substantial commercial applications (Y. Zhang et al, 2023).…”

Section: Introductionmentioning

confidence: 99%

Study on The Low-Temperature Active Alkaline Serine Protease Production Capacity and Detergent Application Potential of Novel Exiguobacterium indicum 1.2.3

KATI

2023

Preprint

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Microorganisms have long captivated researchers for their potential to produce enzymes with diverse industrial applications. Efficient production of proteases from new strains is crucial as these enzymes play a vital role in breaking down protein bonds, enabling their use in industrial applications. Therefore, a novel Exiguobacterium indicum 1.2.3 was isolated (Istanbul, Turkiye) and characterized in this study. This strain produced alkaline serine protease, which works in lower temperatures (20-40°C) with casein as a specific substrate. The protease was completely stable for 3 hours at 30 °C. The enzyme was also highly stable in the pH range 811. The optimum activity was obtained at pH 10. The crude enzyme activity was enhanced by various metal ions and retained 147%, 125%, 124%, and 117% of its activity within 1 mM Ca2+, Mn2+, Cu2+, and Mg2+, respectively. The crude enzyme was inactive with PMSF, indicating a serine residue on the active side. The enzyme exhibited a great proteolytic effect in the presence of surfactants and oxidizing agents. The addition of Tween 80, Triton X-100, and sodium perborate improved enzymatic activity up to 135%, 109%, and 105%, respectively. According to the washing results, the crude enzyme effectively removed the blood on different types of standard pre-stained textiles at 30 °C. In conclusion, Exiguobacterium indicum 1.2.3 is a promising candidate for protease production, with its diverse applications spanning various industrial sectors, particularly detergents.

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Enhancement of alkaline protease production in recombinant Bacillus licheniformis by response surface methodology

Cited by 9 publications

References 34 publications

Comprehensive Analysis of Catalytic Characteristics and Molecular Mechanisms in Mutant Trametes versicolor Strains with Enhanced Laccase Activities

Comprehensive Analysis of Catalytic Characteristics and Molecular Mechanisms in Mutant Trametes versicolor Strains with Enhanced Laccase Activities

Microbial-derived salt-tolerant proteases and their applications in high-salt traditional soybean fermented foods: a review

Study on The Low-Temperature Active Alkaline Serine Protease Production Capacity and Detergent Application Potential of Novel Exiguobacterium indicum 1.2.3

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