Expression in Lactococcus lactis of a β-1,3-1,4-glucanase gene from Bacillus sp. SJ-10 isolated from fermented fish

Tak, Jin Yeong; Jang, Won Je; Lee, Jong Min; Suraiya, Sharmin; Kong, In‐Soo

doi:10.1016/j.pep.2019.05.006

Cited by 6 publications

(4 citation statements)

References 23 publications

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“…X4 and Bacillus sp. SJ-10 cultures (Baek et al 2017 ; Tak et al 2019 ), and for both wild type and mutant β-1,3–1,4-glucanase purified from Bacillus subtilis MA139 (Pei et al 2015 ). Also, it was higher than that reported for recombinant β-1,3–1,4-glucanase purified from Saccharophagus degradans (30 °C) (Lafond et al 2016 ), and Bacillus velezensis ZJ20 (35 °C) (Xu et al 2016 ).…”

Section: Discussionmentioning

confidence: 99%

Purification, characterization, immobilization and applications of an enzybiotic β-1,3–1,4-glucanase produced from halotolerant marine Halomonas meridiana ES021

Gadallah

El-Borai

El-Aassar

et al. 2023

World J Microbiol Biotechnol

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Extracellular β-1,3–1,4-glucanase-producing strain Halomonas meridiana ES021 was isolated from Gabal El-Zeit off shore, Red Sea, Egypt. The Extracellular enzyme was partially purified by precipitation with 75% acetone followed by anion exchange chromatography on DEAE-cellulose, where a single protein band was determined with molecular mass of approximately 72 kDa. The Km value was 0.62 mg β-1,3–1,4-glucan/mL and Vmax value was 7936 U/mg protein. The maximum activity for the purified enzyme was observed at 40 °C, pH 5.0, and after 10 min of the reaction. β-1,3–1,4-glucanase showed strong antibacterial effect against Bacillus subtilis, Streptococcus agalactiae and Vibrio damsela. It also showed antifungal effect against Penicillium sp. followed by Aspergillus niger. No toxicity was observed when tested on Artemia salina. Semi-purified β-1,3–1,4-glucanase was noticed to be effective in clarification of different juices at different pH values and different time intervals. The maximum clarification yields were 51.61% and 66.67% on mango juice at 40 °C and pH 5.3 for 2 and 4 h, respectively. To our knowledge, this is the first report of β-1,3–1,4-glucanase enzyme from halotolerant Halomonas species. Graphic Abstract

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Section: Discussionmentioning

confidence: 99%

Purification, characterization, immobilization and applications of an enzybiotic β-1,3–1,4-glucanase produced from halotolerant marine Halomonas meridiana ES021

Gadallah

El-Borai

El-Aassar

et al. 2023

World J Microbiol Biotechnol

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“…S. simulans PMR35 from Budu was reported to secrete lipase in a high‐salt environment (Kanjan & Sakpetch, 2020). A bacterial endoglucanase, β−1,3‐1,4‐glucanase, was obtained from jeotgal , a Korean traditional fermented fish, and this enzyme can be used to hydrolyze linear β‐glucans containing β−1,3 and β−1,4 linkages (Tak et al., 2019).…”

Section: Microbiome Of Traditional Fermented Fish Productsmentioning

confidence: 99%

Transforming the fermented fish landscape: Microbiota enable novel, safe, flavorful, and healthy products for modern consumers

Wang

Chen

et al. 2023

Comp Rev Food Sci Food Safe

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Regular consumption of fish promotes sustainable health while reducing negative environmental impacts. Fermentation has long been used for preserving perishable foods, including fish. Fermented fish products are popular consumer foods of historical and cultural significance owing to their abundant essential nutrients and distinct flavor. This review discusses the recent scientific progress on fermented fish, especially the involved flavor formation processes, microbial metabolic activities, and interconnected biochemical pathways (e.g., enzymatic/non‐enzymatic reactions associated with lipids, proteins, and their interactions). The multiple roles of fermentation in preservation of fish, development of desirable flavors, and production of health‐promoting nutrients and bioactive substances are also discussed. Finally, prospects for further studies on fermented fish are proposed, including the need of monitoring microorganisms, along with the precise control of a fermentation process to transform the traditional fermented fish to novel, flavorful, healthy, and affordable products for modern consumers. Microbial‐enabled innovative fermented fish products that consider both flavor and health benefits are expected to become a significant segment in global food markets. The integration of multi‐omics technologies, biotechnology‐based approaches (including synthetic biology and metabolic engineering) and sensory and consumer sciences, is crucial for technological innovations related to fermented fish. The findings of this review will provide guidance on future development of new or improved fermented fish products through regulating microbial metabolic processes and enzymatic activities.

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“…The overexpression and purification of recombinant proteins via genetic engineering have enabled the widespread application of these proteins [ 14 ]. Heterologous expression systems have been adopted to increase β-glucosidase activity.…”

Section: Introductionmentioning

confidence: 99%

“…Heterologous expression systems have been adopted to increase β-glucosidase activity. Different β-glucosidase genes have been heterologously expressed in microbial systems such as Lactobacillus lactis [ 14 ], Escherichia coli [ 15 ], and Pichia pastoris [ 16 ]. In particular, L. lactis , which is generally regarded as a safe (GRAS) microorganism and has probiotic properties, is used to express heterologous genes [ 17 , 18 ].…”

Section: Introductionmentioning

confidence: 99%

Expression of β-Glucosidases from the Yak Rumen in Lactic Acid Bacteria: A Genetic Engineering Approach

Yang

Sunkang

et al. 2023

Microorganisms

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β-glucosidase derived from microorganisms has wide industrial applications. In order to generate genetically engineered bacteria with high-efficiency β-glucosidase, in this study two subunits (bglA and bglB) of β-glucosidase obtained from the yak rumen were expressed as independent proteins and fused proteins in lactic acid bacteria (Lactobacillus lactis NZ9000). The engineered strains L. lactis NZ9000/pMG36e-usp45-bglA, L. lactis NZ9000/pMG36e-usp45-bglB, and L. lactis NZ9000/pMG36e-usp45-bglA-usp45-bglB were successfully constructed. These bacteria showed the secretory expression of BglA, BglB, and Bgl, respectively. The molecular weights of BglA, BglB, and Bgl were about 55 kDa, 55 kDa, and 75 kDa, respectively. The enzyme activity of Bgl was significantly higher (p < 0.05) than that of BglA and BglB for substrates such as regenerated amorphous cellulose (RAC), sodium carboxymethyl cellulose (CMC-Na), desiccated cotton, microcrystalline cellulose, filter paper, and 1% salicin. Moreover, 1% salicin appeared to be the most suitable substrate for these three recombinant proteins. The optimum reaction temperatures and pH values for these three recombinant enzymes were 50 °C and 7.0, respectively. In subsequent studies using 1% salicin as the substrate, the enzymatic activities of BglA, BglB, and Bgl were found to be 2.09 U/mL, 2.36 U/mL, and 9.4 U/mL, respectively. The enzyme kinetic parameters (Vmax, Km, Kcat, and Kcat/Km) of the three recombinant strains were analyzed using 1% salicin as the substrate at 50 °C and pH 7.0, respectively. Under conditions of increased K+ and Fe2+ concentrations, the Bgl enzyme activity was significantly higher (p < 0.05) than the BglA and BglB enzyme activity. However, under conditions of increased Zn2+, Hg2+, and Tween20 concentrations, the Bgl enzyme activity was significantly lower (p < 0.05) than the BglA and BglB enzyme activity. Overall, the engineered lactic acid bacteria strains generated in this study could efficiently hydrolyze cellulose, laying the foundation for the industrial application of β-glucosidase.

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Expression in Lactococcus lactis of a β-1,3-1,4-glucanase gene from Bacillus sp. SJ-10 isolated from fermented fish

Cited by 6 publications

References 23 publications

Purification, characterization, immobilization and applications of an enzybiotic β-1,3–1,4-glucanase produced from halotolerant marine Halomonas meridiana ES021

Purification, characterization, immobilization and applications of an enzybiotic β-1,3–1,4-glucanase produced from halotolerant marine Halomonas meridiana ES021

Transforming the fermented fish landscape: Microbiota enable novel, safe, flavorful, and healthy products for modern consumers

Expression of β-Glucosidases from the Yak Rumen in Lactic Acid Bacteria: A Genetic Engineering Approach

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