Journal of Microbiology

Journal Articles

The role of Jacalin-related lectin gene AOL_s00083g511 in the development and pathogenicity of the nematophagous fungus Arthrobotrys oligospora: Xinyuan Dong , Jiali Si , Guanghui Zhang , Zhen Shen , Li Zhang , Kangliang Sheng , Jingmin Wang , Xiaowei Kong , Xiangdong Zha , Yongzhong Wang; J. Microbiol. 2021;59(8):736-745. Published online July 5, 2021; DOI: https://doi.org/10.1007/s12275-021-1029-4

61 View
0 Download
4 Web of Science
3 Crossref

Arthrobotrys oligospora is a model species of nematophagous fungi and has great potential for the biological control of nematode diseases. Lectin is a protein that binds to carbohydrates and their complexes with high specificity, which mediates recognition events in various physiological and pathological processes. This study aimed to investigate the role of the Jacalin-related lectin (JRL) gene, AOL_s00083g511, in A. oligospora development. Through a homology recombination approach, we obtained the AOL_s00083g511 knockout mutant strain (Δg511). Next, the biological characteristics of the Δg511 mutant strain, including growth rate, conidia germination rate, adaptation to environmental stresses, and nematocidal activity, were compared with those of the wild-type (WT) strain. The results showed that the JRL gene AOL_ s00083g511 did not affect fungal growth, conidia germination, 3D-trap formation, and the ability of A. oligospora to prey on nematodes significantly. We speculate that this phenomenon may be caused by a loss of the key β1–β2 loops in the AOL_ s00083g511-encoded JRL domain and an intrinsic genetic compensation of AOL_s00083g511 in this fungus. The growth rates of both strains on high salt or surfactant media were similar; however, in the strong oxidation medium, the growth rate of the Δg511 mutant was significantly lower than that of the WT strain, indicating that AOL_s00083g511 might play a role in oxidative stress resistance. These findings provide a basis for further analysis of the related functions of the JRL gene in A. oligospora and their potential roles in the biological control of nematodes in the future.

Citations

Citations to this article as recorded by

Function discovery of a non-ribosomal peptide synthetase-like encoding gene in the nematode-trapping fungus Arthrobotrys oligospora
Tiantian Gu, Hengqian Lu, Huiwen Liu, Guanghui Zhang, Yongzhong Wang
Frontiers in Microbiology.2023;[Epub] CrossRef
The fucose-specific lectin gene AOL_s00054g276 affects trap formation and nematocidal activity of the nematophagous fungus Arthrobotrys oligospora
Jiali Si, Xinyuan Dong, Guanghui Zhang, Hengqian Lu, Kaijing Tang, Li Zhang, Xiaowei Kong, Kangliang Sheng, Jingmin Wang, Xiangdong Zha, Yongzhong Wang
FEMS Microbiology Letters.2022;[Epub] CrossRef
Phospholipase C (AoPLC2) regulates mycelial development, trap morphogenesis, and pathogenicity of the nematode-trapping fungus Arthrobotrys oligospora
Meihua Xie, Ni Ma, Na Bai, Meichen Zhu, Ke-Qin Zhang, Jinkui Yang
Journal of Applied Microbiology.2022; 132(3): 2144. CrossRef

Molecular characterization of Hsf1 as a master regulator of heat shock response in the thermotolerant methylotrophic yeast Ogataea parapolymorpha: Jin Ho Choo , Su-Bin Lee , Hye Yun Moon , Kun Hwa Lee , Su Jin Yoo , Keun Pil Kim , Hyun Ah Kang; J. Microbiol. 2021;59(2):151-163. Published online February 1, 2021; DOI: https://doi.org/10.1007/s12275-021-0646-2

51 View
0 Download
3 Web of Science
3 Crossref

Abstract

Ogataea parapolymorpha (Hansenula polymorpha DL-1) is a thermotolerant methylotrophic yeast with biotechnological applications. Here, O. parapolymorpha genes whose expression is induced in response to heat shock were identified by transcriptome analysis and shown to possess heat shock elements (HSEs) in their promoters. The function of O. parapolymorpha HSF1 encoding a putative heat shock transcription factor 1 (OpHsf1) was characterized in the context of heat stress response. Despite exhibiting low sequence identity (26%) to its Saccharomyces cerevisiae homolog, OpHsf1 harbors conserved domains including a DNA binding domain (DBD), domains involved in trimerization (TRI), transcriptional activation (AR1, AR2), transcriptional repression (CE2), and a C-terminal modulator (CTM) domain. OpHSF1 could complement the temperature sensitive (Ts) phenotype of a S. cerevisiae hsf1 mutant. An O. parapolymorpha strain with an H221R mutation in the DBD domain of OpHsf1 exhibited significantly retarded growth and a Ts phenotype. Intriguingly, the expression of heat-shock-protein‒coding genes harboring HSEs was significantly decreased in the H221R mutant strain, even under non-stress conditions, indicating the importance of the DBD for the basal growth of O. parapolymorpha. Notably, even though the deletion of C-terminal domains (ΔCE2, ΔAR2, ΔCTM) of OpHsf1 destroyed complementation of the growth defect of the S. cerevisiae hsf1 strain, the C-terminal domains were shown to be dispensable in O. parapolymorpha. Overexpression of OpHsf1 in S. cerevisiae increased resistance to transient heat shock, supporting the idea that OpHsf1 could be useful in the development of heatshock‒ resistant yeast host strains.

Citations

Citations to this article as recorded by

A comprehensive review and comparison of L-tryptophan biosynthesis in Saccharomyces cerevisiae and Escherichia coli
Xinru Ren, Yue Wei, Honglu Zhao, Juanjuan Shao, Fanli Zeng, Zhen Wang, Li Li
Frontiers in Bioengineering and Biotechnology.2023;[Epub] CrossRef
Heat shock in Cronobacter sakazakii induces direct protection and cross-protection against simulated gastric fluid stress
Hongmei Niu, MingzheYang, Yonghua Qi, Yangtai Liu, Xiang Wang, Qingli Dong
Food Microbiology.2022; 103: 103948. CrossRef
A review of yeast: High cell-density culture, molecular mechanisms of stress response and tolerance during fermentation
Dongxu Shen, Xiaoli He, Peifang Weng, Yanan Liu, Zufang Wu
FEMS Yeast Research.2022;[Epub] CrossRef

Development of a strategy for the screening of α-glucosidase-producing microorganisms: Bo Zhou+ , Nan Huang+ , Wei Zeng+ , Hao Zhang , Guiguang Chen , Zhiqun Liang; J. Microbiol. 2020;58(2):163-172. Published online January 29, 2020; DOI: https://doi.org/10.1007/s12275-020-9267-4

50 View
0 Download
4 Web of Science
4 Crossref

Abstract

α-Glucosidase is a crucial enzyme for the production of isomaltooligosaccharide. In this study, a novel method comprising eosin Y (EY) and α-D-methylglucoside (AMG) in glass plates was tested for the primary screening of α-glucosidaseproducing strains. First, α-glucosidase-producing Aspergillus niger strains were selected on plates containing EY and AMG based on transparent zone formation resulting from the solubilization of EY by the hydrolyzed product. Conventional
methods
that use trypan blue (TB) and p-nitrophenyl-α-Dglucopyranoside (pPNP) as indicators were then compared with the new strategy. The results showed that EY-containing plates provide the advantages of low price and higher specificity for the screening of α-glucosidase-producing strains. We then evaluated the correlation between the hydrolytic activity of α-glucosidase and diffusion distance, and found that good linearity could be established within a 6–75 U/ml enzyme concentration range. Finally, the hydrolytic and transglycosylation activities of α-glucosidase obtained from the target isolates were determined by EY plate assay and 3,5- dinitrosalicylic acid-Saccharomyces cerevisiae assay, respectively. The results showed that the diameter of the transparent zone varied among isolates was positively correlated with α-glucosidase hydrolytic activity, while good linearity could also be established between α-glucosidase transglycosylation activity and non-fermentable reducing sugars content. With this strategy, 7 Aspergillus niger mutants with high yield of α-glucosidase from 200 obvious single colonies on the primary screen plate were obtained.

Citations

Citations to this article as recorded by

Purification, characterization of a novel α-glucosidase from Debaryomyces hansenii strain MCC 0202 and chromatographic separation for high purity isomalto-oligosaccharides production
Saravanan Rengarajan, Rameshthangam Palanivel
Process Biochemistry.2024; 136: 109. CrossRef
Development of a PMA‐LAMP visual detection assay for viable Cronobacter sakazakii
Qiming Chen, Yang Yu, Xiaodi Chen, Fangming Tu, Peng Wang, Junyi Huang, Zhanmin Liu
International Journal of Dairy Technology.2024; 77(2): 427. CrossRef
Identification of chitin synthase activator in Aspergillus niger and its application in citric acid fermentation
Chunxu Jiang, Han Wang, Menghan Liu, Li Wang, Ruwen Yang, Peng Wang, Zongmei Lu, Yong Zhou, Zhiming Zheng, Genhai Zhao
Applied Microbiology and Biotechnology.2022; 106(21): 6993. CrossRef
Cloning and characterization of a recombinant α-glucosidase from Ensifer adhaerens NBRC 100388 and evaluation of its glucosyl transfer activity
Tatsuya Suzuki, Miyu Fukaya, Kazuki Takahashi, Michiki Takeuchi, Ryotaro Hara, Jun Ogawa, Makoto Ueda
Biocatalysis and Agricultural Biotechnology.2020; 30: 101837. CrossRef

Overexpression and characterization of a novel cold-adapted and salt-tolerant GH1 β-glucosidase from the marine bacterium Alteromonas sp. L82: Jingjing Sun , Wei Wang , Congyu Yao , Fangqun Dai , Xiangjie Zhu , Junzhong Liu , Jianhua Hao; J. Microbiol. 2018;56(9):656-664. Published online August 23, 2018; DOI: https://doi.org/10.1007/s12275-018-8018-2

44 View
0 Download
35 Crossref

Abstract

A novel gene (bgl) encoding a cold-adapted β-glucosidase was cloned from the marine bacterium Alteromonas sp. L82. Based on sequence analysis and its putative catalytic conserved region, Bgl belonged to the glycoside hydrolase family 1. Bgl was overexpressed in E. coli and purified by Ni2+ affinity chromatography. The purified recombinant β- glucosidase showed maximum activity at temperatures between 25°C to 45°C and over the pH range 6 to 8. The enzyme lost activity quickly after incubation at 40°C. Therefore, recombinant β-glucosidase appears to be a cold-adapted enzyme. The addition of reducing agent doubled its activity and 2 M NaCl did not influence its activity. Recombinant β-glucosidase was also tolerant of 700 mM glucose and some organic solvents. Bgl had a Km of 0.55 mM, a Vmax of 83.6 U/mg, a kcat of 74.3 s-1 and kcat/Km of 135.1 at 40°C, pH 7 with 4-nitrophenyl-β-D-glucopyranoside as a substrate. These properties indicate Bgl may be an interesting candidate for biotechnological and industrial applications.

Citations

Citations to this article as recorded by

Streptomyces beigongshangae sp. nov., isolated from baijiu fermented grains, could transform ginsenosides of Panax notoginseng
Bo Liu, Haoyue Gu, Rui Shi, Xiahong He, Zhanbin Sun, Qing Ren, Hanxu Pan
International Journal of Systematic and Evolutionary Microbiology .2024;[Epub] CrossRef
A novel GH1 β-glucosidase from an Arctic bacterium: Characterization and secretory expression in Bacillus subtilis
Jingjing Sun, Wei Wang, Jianhua Hao
Process Biochemistry.2024; 140: 108. CrossRef
Screening, cloning, immobilization and application prospects of a novel β-glucosidase from the soil metagenome
Qian Yao, Jin Xu, Nan Tang, Weiji Chen, Quliang Gu, He Li
Environmental Research.2024; 244: 117676. CrossRef
Characterization of a novel cold-adapted GH1 β-glucosidase from Psychrobacillus glaciei and its application in the hydrolysis of soybean isoflavone glycosides
Jinjian He, Jiajing Duan, Pinglian Yu, Yuying Li, Mansheng Wang, Xiu Zhang, Zishu Chen, Pengjun Shi
Current Research in Food Science.2024; 8: 100777. CrossRef
Biochemical and in silico structural properties of a thermo-acid stable β-glucosidase from Beauveria bassiana
Buka Magwaza, Ayodeji Amobonye, Prashant Bhagwat, Santhosh Pillai
Heliyon.2024; 10(7): e28667. CrossRef
Moderately thermostable GH1 β-glucosidases from hyperacidophilic archaeon Cuniculiplasma divulgatum S5
Anna N Khusnutdinova, Hai Tran, Saloni Devlekar, Marco A Distaso, Ilya V Kublanov, Tatiana Skarina, Peter Stogios, Alexei Savchenko, Manuel Ferrer, Olga V Golyshina, Alexander F Yakunin, Peter N Golyshin
FEMS Microbiology Ecology.2024;[Epub] CrossRef
Structural determinants of cold activity and glucose tolerance of a family 1 glycoside hydrolase (GH1) from Antarctic Marinomonas sp. ef1
Louise Jane Gourlay, Marco Mangiagalli, Elisabetta Moroni, Marina Lotti, Marco Nardini
The FEBS Journal.2024; 291(13): 2897. CrossRef
Partial characterization of β-glucosidase, β-xylosidase, and α-l-arabinofuranosidase from Jiangella alba DSM 45237 and their potential in lignocellulose-based biorefining
Zeynep Gül Aytaş, Münir Tunçer, Çağrı Seda Kul, Sümeyye Cilmeli, Nurayan Aydın, Tuğrul Doruk, Ali Osman Adıgüzel
Sustainable Chemistry and Pharmacy.2023; 31: 100900. CrossRef
Heterologous expression and characterization of salt-tolerant β-glucosidase from xerophilic Aspergillus chevalieri for hydrolysis of marine biomass
Hironori Senba, Daisuke Saito, Yukihiro Kimura, Shinichi Tanaka, Mikiharu Doi, Shinji Takenaka
Archives of Microbiology.2023;[Epub] CrossRef
Expression of β-Glucosidases from the Yak Rumen in Lactic Acid Bacteria: A Genetic Engineering Approach
Chuan Wang, Yuze Yang, Chunjuan Ma, Yongjie Sunkang, Shaoqing Tang, Zhao Zhang, Xuerui Wan, Yaqin Wei
Microorganisms.2023; 11(6): 1387. CrossRef
Structural and functional insights of a cold-adaptive β-glucosidase with very high glucose tolerance from Microbacterium sp. CIAB417
Anjali Purohit, Lata Pawar, Sudesh Kumar Yadav
Enzyme and Microbial Technology.2023; 169: 110284. CrossRef
Advances in cold-adapted enzymes derived from microorganisms
Yehui Liu, Na Zhang, Jie Ma, Yuqi Zhou, Qiang Wei, Chunjie Tian, Yi Fang, Rongzhen Zhong, Guang Chen, Sitong Zhang
Frontiers in Microbiology.2023;[Epub] CrossRef
Improving the catalytic activity of β-glucosidase from Coniophora puteana via semi-rational design for efficient biomass cellulose degradation
Hai-Yan Zhou, Qi Chen, Yi-Feng Zhang, Dou-Dou Chen, Xiao-Nan Yi, De-Shui Chen, Xin-Ping Cheng, Mian Li, Hong-Yan Wang, Kai-Qian Chen, Zhi-Qiang Liu, Yu-Guo Zheng
Enzyme and Microbial Technology.2023; 164: 110188. CrossRef
Study on the Biochemical Characterization and Selectivity of Three β-Glucosidases From Bifidobacterium adolescentis ATCC15703
Yanbo Hu, Liyuan Zhai, Huili Hong, Zenghui Shi, Jun Zhao, Duo Liu
Frontiers in Microbiology.2022;[Epub] CrossRef
Biochemical characterization of a novel glucose-tolerant GH3 β-glucosidase (Bgl1973) from Leifsonia sp. ZF2019
Yi He, Chenxi Wang, Ronghu Jiao, Qinxue Ni, Yan Wang, Qianxin Gao, Youzuo Zhang, Guangzhi Xu
Applied Microbiology and Biotechnology.2022; 106(13-16): 5063. CrossRef
Spatial variability of bacterial community compositions in the Mariana Trench
Wei Wang, Jingjing Sun, Jianhua Hao
Canadian Journal of Microbiology.2022; 68(10): 633. CrossRef
Life from a Snowflake: Diversity and Adaptation of Cold-Loving Bacteria among Ice Crystals
Carmen Rizzo, Angelina Lo Giudice
Crystals.2022; 12(3): 312. CrossRef
Cold-Active β-Galactosidases: Insight into Cold Adaptation Mechanisms and Biotechnological Exploitation
Marco Mangiagalli, Marina Lotti
Marine Drugs.2021; 19(1): 43. CrossRef
Two Key Amino Acids Variant of α-l-arabinofuranosidase from Bacillus subtilis Str. 168 with Altered Activity for Selective Conversion Ginsenoside Rc to Rd
Ru Zhang, Shi Quan Tan, Bian Ling Zhang, Zi Yu Guo, Liang Yu Tian, Pei Weng, Zhi Yong Luo
Molecules.2021; 26(6): 1733. CrossRef
Cloning, expression, biochemical characterization, and molecular docking studies of a novel glucose tolerant β-glucosidase from Saccharomonospora sp. NB11
Numan Saleh Zada, Ali Osman Belduz, Halil Ibrahim Güler, Anum Khan, Miray Sahinkaya, Arife Kaçıran, Hilal Ay, Malik Badshah, Aamer Ali Shah, Samiullah Khan
Enzyme and Microbial Technology.2021; 148: 109799. CrossRef
A novel β-glucosidase from a hot-spring metagenome shows elevated thermal stability and tolerance to glucose and ethanol
Girija Kaushal, Amit K. Rai, Sudhir P. Singh
Enzyme and Microbial Technology.2021; 145: 109764. CrossRef
Homology analysis of 35 β-glucosidases in Oenococcus oeni and biochemical characterization of a novel β-glucosidase BGL0224
Jie Zhang, Ning Zhao, Junnan Xu, Yiman Qi, Xinyuan Wei, Mingtao Fan
Food Chemistry.2021; 334: 127593. CrossRef
A glucose tolerant β-glucosidase from Thermomicrobium roseum that can hydrolyze biomass in seawater
Sushant K. Sinha, Maithili Datta, Supratim Datta
Green Chemistry.2021; 23(18): 7299. CrossRef
An overview on marine cellulolytic enzymes and their potential applications
Noora Barzkar, Muhammad Sohail
Applied Microbiology and Biotechnology.2020; 104(16): 6873. CrossRef
A Novel Glucose-Tolerant GH1 β-Glucosidase and Improvement of Its Glucose Tolerance Using Site-Directed Mutation
Jingjing Sun, Wei Wang, Yu Ying, Jianhua Hao
Applied Biochemistry and Biotechnology.2020; 192(3): 999. CrossRef
Magnetically recyclable catalytic nanoparticles grafted with Bacillus subtilis β-glucosidase for efficient cellobiose hydrolysis
Shivangi Chamoli, Ekta Yadav, Hemansi, Jitendra Kumar Saini, Ashok Kumar Verma, Naveen Kumar Navani, Piyush Kumar
International Journal of Biological Macromolecules.2020; 164: 1729. CrossRef
Engineering of β-Glucosidase Bgl15 with Simultaneously Enhanced Glucose Tolerance and Thermostability To Improve Its Performance in High-Solid Cellulose Hydrolysis
Lichuang Cao, Ran Chen, Xin Huang, Shuifeng Li, Sufang Zhang, Xiangpeng Yang, Zongmin Qin, Wei Kong, Wei Xie, Yuhuan Liu
Journal of Agricultural and Food Chemistry.2020; 68(19): 5391. CrossRef
A d-glucose- and d-xylose-tolerant GH1 β-glucosidase from Cellulosimicrobium funkei HY-13, a fibrolytic gut bacterium of Eisenia fetida
Do Young Kim, Jonghoon Kim, Sun Hwa Lee, Chungwook Chung, Dong-Ha Shin, Bon-Hwan Ku, Kwang-Hee Son, Ho-Yong Park
Process Biochemistry.2020; 94: 282. CrossRef
A rationally identified marine GH1 β‐glucosidase has distinguishing functional features for simultaneous saccharification and fermentation
Amanda S. de Sousa, Ricardo R. de Melo, Renan Y. Miyamoto, Mariana A. B. Morais, Liliane P. Andrade, Natália Milan, Mayara C. de Avila, Cláudia M. de Souza, Regina C. Adão, Josiane A. Scarpassa, Plínio S. Vieira, Leandro V. dos Santos, Carlos H. I. Ramos,
Biofuels, Bioproducts and Biorefining.2020; 14(6): 1163. CrossRef
Deep Hypersaline Anoxic Basins as Untapped Reservoir of Polyextremophilic Prokaryotes of Biotechnological Interest
Stefano Varrella, Michael Tangherlini, Cinzia Corinaldesi
Marine Drugs.2020; 18(2): 91. CrossRef
Aroma enhancement of instant green tea infusion using β-glucosidase and β-xylosidase
Ting Zhang, Ke Fang, Hui Ni, Ting Li, Li Jun Li, Qing Biao Li, Feng Chen
Food Chemistry.2020; 315: 126287. CrossRef
RNase G controls tpiA mRNA abundance in response to oxygen availability in Escherichia coli
Jaejin Lee, Dong-Ho Lee, Che Ok Jeon, Kangseok Lee
Journal of Microbiology.2019; 57(10): 910. CrossRef
Comparison between irradiating and autoclaving citrus wastes as substrate for solid‐state fermentation by Aspergillus aculeatus
H. Ni, T. Zhang, X. Guo, Y. Hu, A. Xiao, Z. Jiang, L. Li, Q. Li
Letters in Applied Microbiology.2019;[Epub] CrossRef
The coordinated action of RNase III and RNase G controls enolase expression in response to oxygen availability in Escherichia coli
Minho Lee, Minju Joo, Minji Sim, Se-Hoon Sim, Hyun-Lee Kim, Jaejin Lee, Minkyung Ryu, Ji-Hyun Yeom, Yoonsoo Hahn, Nam-Chul Ha, Jang-Cheon Cho, Kangseok Lee
Scientific Reports.2019;[Epub] CrossRef
Identification and molecular characterization of a psychrophilic GH1 β-glucosidase from the subtropical soil microorganism Exiguobacterium sp. GXG2
Bangqiao Yin, Hengsen Gu, Xueyan Mo, Yue Xu, Bing Yan, Quanwen Li, Qian Ou, Bo Wu, Chen Guo, Chengjian Jiang
AMB Express.2019;[Epub] CrossRef

Diversity and enzyme activity of Penicillium species associated with macroalgae in Jeju Island: Myung Soo Park , Seobihn Lee , Seung-Yoon Oh , Ga Youn Cho , Young Woon Lim; J. Microbiol. 2016;54(10):646-654. Published online September 30, 2016; DOI: https://doi.org/10.1007/s12275-016-6324-0

50 View
0 Download
16 Crossref

Abstract

A total of 28 strains of 19 Penicillium species were isolated in a survey of extracellular enzyme-producing fungi from macroalgae along the coast of Jeju Island of Korea. Penicillium species were identified based on morphological and β-tubulin sequence analyses. In addition, the halo-tolerance and enzyme activity of all strains were evaluated. The diversity of Penicillium strains isolated from brown algae was higher than the diversity of strains isolated from green and red algae. The commonly isolated species were Penicillium antarcticum, P. bialowiezense, P. brevicompactum, P. crustosum, P. oxalicum, P. rubens, P. sumatrense, and P. terrigenum. While many strains showed endoglucanase, β-glucosidase, and protease activity, no alginase activity was detected. There was a positive correlation between halo-tolerance and endoglucanase activity within Penicillium species. Among 19 Penicillium species, three species–P. kongii, P. olsonii, and P. viticola– have not been previously recorded in Korea.

Citations

Citations to this article as recorded by

Plastic-inhabiting fungi in marine environments and PCL degradation activity
Sung Hyun Kim, Jun Won Lee, Ji Seon Kim, Wonjun Lee, Myung Soo Park, Young Woon Lim
Antonie van Leeuwenhoek.2022; 115(12): 1379. CrossRef
Marine fungal abilities to enzymatically degrade algal polysaccharides, proteins and lipids: a review
Yoran Le Strat, Nicolas Ruiz, Joël Fleurence, Yves-François Pouchus, Paul Déléris, Justine Dumay
Journal of Applied Phycology.2022; 34(3): 1131. CrossRef
Characterization of two 1,3-β-glucan-modifying enzymes from Penicillium sumatraense reveals new insights into 1,3-β-glucan metabolism of fungal saprotrophs
Valentina Scafati, Francesca Troilo, Sara Ponziani, Moira Giovannoni, Anna Scortica, Daniela Pontiggia, Francesco Angelucci, Adele Di Matteo, Benedetta Mattei, Manuel Benedetti
Biotechnology for Biofuels and Bioproducts.2022;[Epub] CrossRef
Four Unrecorded Aspergillus Species from the Rhizosphere Soil in South Korea
Jun Won Lee, Sung Hyun Kim, Young-Hyun You, Young Woon Lim, Myung Soo Park
Mycobiology.2021; 49(4): 346. CrossRef
Advances in research on calf rennet substitutes and their effects on cheese quality
Xiaofeng Liu, Yuanfeng Wu, Rongfa Guan, Guochao Jia, YuChen Ma, Yao Zhang
Food Research International.2021; 149: 110704. CrossRef
Mutation, Chemoprofiling, Dereplication, and Isolation of Natural Products from Penicillium oxalicum
Vidushi Abrol, Manoj Kushwaha, Divya Arora, Sharada Mallubhotla, Sundeep Jaglan
ACS Omega.2021; 6(25): 16266. CrossRef
Evaluating the xerophilic potential of moulds on selected egg tempera paints on glass and wooden supports using fluorescent microscopy
Janez Kosel, Maša Kavčič, Lea Legan, Klara Retko, Polonca Ropret
Journal of Cultural Heritage.2021; 52: 44. CrossRef
Dietary effects on gut microbiota of the mesquite lizard Sceloporus grammicus (Wiegmann, 1828) across different altitudes
Nina Montoya-Ciriaco, Selene Gómez-Acata, Ligia Catalina Muñoz-Arenas, Luc Dendooven, Arturo Estrada-Torres, Aníbal H. Díaz de la Vega-Pérez, Yendi E. Navarro-Noya
Microbiome.2020;[Epub] CrossRef
Penicillium from Rhizosphere Soil in Terrestrial and Coastal Environments in South Korea
Myung Soo Park, Jun Won Lee, Sung Hyun Kim, Ji-Hyun Park, Young-Hyun You, Young Woon Lim
Mycobiology.2020; 48(6): 431. CrossRef
Three Unrecorded Species Belonging toPenicilliumSectionSclerotiorafrom Marine Environments in Korea
Myung Soo Park, Dawoon Chung, Kyunghwa Baek, Young Woon Lim
Mycobiology.2019; 47(2): 165. CrossRef
Fungal Diversity and Enzyme Activity Associated with the Macroalgae, Agarum clathratum
Seobihn Lee, Myung Soo Park, Hanbyul Lee, Jae-Jin Kim, John A. Eimes, Young Woon Lim
Mycobiology.2019; 47(1): 50. CrossRef
Biodiversity of Penicillium species from marine environments in Portugal and description of Penicillium lusitanum sp. nov., a novel species isolated from sea water
Micael F. M. Gonçalves, Liliana Santos, Bruno M. V. Silva, Alberto C. Abreu, Tânia F. L. Vicente, Ana C. Esteves, Artur Alves
International Journal of Systematic and Evolutionary Microbiology.2019; 69(10): 3014. CrossRef
Taxonomic revision of the biotechnologically important species Penicillium oxalicum with the description of two new species from acidic and saline soils
Alena Kubátová, Martina Hujslová, Jens C. Frisvad, Milada Chudíčková, Miroslav Kolařík
Mycological Progress.2019; 18(1-2): 215. CrossRef
The diversity and ecological roles of Penicillium in intertidal zones
Myung Soo Park, Seung-Yoon Oh, Jonathan J. Fong, Jos Houbraken, Young Woon Lim
Scientific Reports.2019;[Epub] CrossRef
Fungal Root Microbiome from Healthy and Brittle Leaf Diseased Date Palm Trees (Phoenix dactylifera L.) Reveals a Hidden Untapped Arsenal of Antibacterial and Broad Spectrum Antifungal Secondary Metabolites
Fedia B. Mefteh, Amal Daoud, Ali Chenari Bouket, Faizah N. Alenezi, Lenka Luptakova, Mostafa E. Rateb, Adel Kadri, Neji Gharsallah, Lassaad Belbahri
Frontiers in Microbiology.2017;[Epub] CrossRef
Species List of Aspergillus, Penicillium and Talaromyces in Korea, Based on ‘One Fungus One Name’ System

The Korean Journal of Mycology.2016;[Epub] CrossRef

Research Support, Non-U.S. Gov'ts

Characterization of Recombinant β-Glucosidase from Arthrobacter chlorophenolicus and Biotransformation of Ginsenosides Rb1, Rb2, Rc, and Rd: Myung Keun Park , Chang-Hao Cui , Sung Chul Park , Seul-Ki Park , Jin-Kwang Kim , Mi-Sun Jung , Suk-Chae Jung , Mi-Sun Jung , Suk-Chae Jung , Sun-Chang Kim , Wan-Taek Im; J. Microbiol. 2014;52(5):399-406. Published online May 9, 2014; DOI: https://doi.org/10.1007/s12275-014-3601-7

47 View
0 Download
10 Crossref

Abstract

The focus of this study was the cloning, expression, and characterization of recombinant ginsenoside hydrolyzing β-glucosidase from Arthrobacter chlorophenolicus with an ultimate objective to more efficiently bio-transform ginse-nosides. The gene bglAch, consisting of 1,260 bp (419 amino acid residues) was cloned and the recombinant enzyme, over-expressed in Escherichia coli BL21 (DE3), was characterized. The GST-fused BglAch was purified using GST·Bind agarose resin and characterized. Under optimal conditions (pH 6.0 and 37°C) BglAch hydrolyzed the outer glucose and arabino-pyranose moieties of ginsenosides Rb1 and Rb2 at the C20 position of the aglycone into ginsenoside Rd. This was fol-lowed by hydrolysis into F2 of the outer glucose moiety of ginsenoside Rd at the C3 position of the aglycone. Additio-nally, BglAch more slowly transformed Rc to F2 via C-Mc1 (compared to hydrolysis of Rb1 or Rb2). These results in-dicate that the recombinant BglAch could be useful for the production of ginsenoside F2 for use in the pharmaceutical and cosmetic industries.

Citations

Citations to this article as recorded by

Production and pharmaceutical research of minor saponins in Panax notoginseng (Sanqi): Current status and future prospects
Hui Zhang, Jianxiu Li, Mengxue Diao, Jianbin Li, Nengzhong Xie
Phytochemistry.2024; 223: 114099. CrossRef
Microbial production and applications of β-glucosidase-A review
Wenqi Yang, Yaowu Su, Rubing Wang, Huanyu Zhang, Hongyan Jing, Jie Meng, Guoqi Zhang, Luqi Huang, Lanping Guo, Juan Wang, Wenyuan Gao
International Journal of Biological Macromolecules.2024; 256: 127915. CrossRef
Progress in the Conversion of Ginsenoside Rb1 into Minor Ginsenosides Using β-Glucosidases
Hongrong Zhu, Rui Zhang, Zunxi Huang, Junpei Zhou
Foods.2023; 12(2): 397. CrossRef
Enzymatic biotransformation of ginsenoside Rb1 by recombinant β-glucosidase of bacterial isolates from Indonesia
Almando Geraldi, Ni'matuzahroh, Fatimah, Chang-Hao Cui, Thi Thuy Nguyen, Sun Chang Kim
Biocatalysis and Agricultural Biotechnology.2020; 23: 101449. CrossRef
Characterization of a Novel Ginsenoside MT1 Produced by an Enzymatic Transrhamnosylation of Protopanaxatriol-Type Ginsenosides Re
Byeong-Min Jeon, Jong-In Baek, Min-Sung Kim, Sun-Chang Kim, Chang-hao Cui
Biomolecules.2020; 10(4): 525. CrossRef
In silico Approach to Elucidate Factors Associated with GH1 β-Glucosidase Thermostability
Amer Ahmed, Ayesha Sumreen, Aasia Bibi, Faiz ul Hassan Nasim, Kashfa Batool
Journal of Pure and Applied Microbiology.2019; 13(4): 1953. CrossRef
A literature update elucidating production of Panax ginsenosides with a special focus on strategies enriching the anti-neoplastic minor ginsenosides in ginseng preparations
Tanya Biswas, A. K. Mathur, Archana Mathur
Applied Microbiology and Biotechnology.2017; 101(10): 4009. CrossRef
Classification of glycosidases that hydrolyze the specific positions and types of sugar moieties in ginsenosides
Kyung-Chul Shin, Deok-Kun Oh
Critical Reviews in Biotechnology.2016; 36(6): 1036. CrossRef
Insight into a novel β-1,4-glucosidase from Streptomyces griseorubens JSD-1
H.-W. Feng, Y.-E. Zhi, Y.-J. Sun, L.-R. Xu, L.-M. Wang, X.-J. Zhan, P. Zhou
Applied Biochemistry and Microbiology.2016; 52(4): 371. CrossRef
Overexpression and characterization of a glycoside hydrolase family 1 enzyme from Cellulosimicrobium cellulans sp. 21 and its application for minor ginsenosides production
Ye Yuan, Yanbo Hu, Chenxing Hu, Jiayi Leng, Honglei Chen, Xuesong Zhao, Juan Gao, Yifa Zhou
Journal of Molecular Catalysis B: Enzymatic.2015; 120: 60. CrossRef

Identification of the Genes Involved in 1-Deoxynojirimycin Synthesis in Bacillus subtilis MORI 3K-85: Kyung-Don Kang , Yong Seok Cho , Ji Hye Song , Young Shik Park , Jae Yeon Lee , Kyo Yeol Hwang , Sang Ki Rhee , Ji Hyung Chung , Ohsuk Kwon , Su-Il Seong; J. Microbiol. 2011;49(3):431-440. Published online June 30, 2011; DOI: https://doi.org/10.1007/s12275-011-1238-3

48 View
0 Download
34 Scopus

Abstract: 1-Deoxynojirimycin (DNJ), a D-glucose analogue with a nitrogen atom substituting for the ring oxygen, is a strong inhibitor of intestinal α-glucosidase. DNJ has several promising biological activities, including its antidiabetic, antitumor, and antiviral activities. Nevertheless, only limited amounts of DNJ are available because it can only be extracted from some higher plants, including the mulberry tree, or purified from the culture broth of several types of soil bacteria, such as Streptomyces sp. and Bacillus sp. In our previous study, a DNJ-producing bacterium, Bacillus subtilis MORI, was isolated from the traditional Korean fermented food Chungkookjang. In the present study, we report the identification of the DNJ biosynthetic genes in B. subtilis MORI 3K-85 strain, a DNJ-overproducing derivate of the B. subtilis MORI strain generated by γ-irradiation. The genomic DNA library of B. subtilis MORI 3K-85 was constructed in Escherichia coli, and clones showing α-glucosidase inhibition activity were selected. After DNA sequencing and a series of subcloning, we were able to identify a putative operon which consists of gabT1, yktc1, and gutB1 genes predicted to encode putative transaminase, phosphatase, and oxidoreductase, respectively. When a recombinant plasmid containing this operon sequence was transformed into an E. coli strain, the resulting transformant was able to produce DNJ into the culture medium. Our results indicate that the gabT1, yktc1, and gutB1 genes are involved in the DNJ biosynthetic pathway in B. subtilis MORI, suggesting the possibility of employing these genes to establish a large-scale microbial DNJ overproduction system through genetic engineering and process optimization.

Identification and Functional Analysis of a Gene Encoding β-Glucosidase from the Brown-Rot Basidiomycete Fomitopsis palustris: Hwang-Woo Ji , Chang-Jun Cha; J. Microbiol. 2010;48(6):808-813. Published online January 9, 2011; DOI: https://doi.org/10.1007/s12275-010-0482-2

40 View
0 Download
7 Scopus

Abstract: The brown-rot basidiomycete Fomitopsis palustris is known to degrade crystalline cellulose (Avicel) and produce three major cellulases, exoglucanases, endoglucanases, and β-glucosidases. A novel β-glucosidase designated as Cel3A was identified from F. palustris grown at the expense of Avicel. The deduced amino acid sequence of Cel3A showed high homology with those of other fungal β-glucosidases that belong to glycosyl hydrolase (GH) family 3. The sequence analysis also indicated that Cel3A contains the N- and C-terminal domains of GH family 3 and Asp-209 was conserved as a catalytic nucleophile. The cloned gene was successfully expressed in the yeast Pichia pastoris and the recombinant protein exhibited β-glucosidase activity with cellobiose and some degree of thermostability. Considering the size and sequence of the protein, the β-glucosidase identified in this study is different from the protein purified directly from F. palustris in the previous study. Our results suggest that the fungus possesses at least two β-glucosidase genes.

Purification and Characterization of the α-Glucosidase Produced by Thermophilic Fungus Thermoascus aurantiacus CBMAI 756: Ana Flávia Azevedo Carvalho , Maurício Boscolo , Roberto da Silva , Henrique Ferreira , Eleni Gomes; J. Microbiol. 2010;48(4):452-459. Published online August 20, 2010; DOI: https://doi.org/10.1007/s12275-010-9319-2

38 View
0 Download
9 Scopus

Abstract: Αn α-glucosidase enzyme produced by the fungus Thermoascus aurantiacus CBMAI 756 was purified by ultra filtration, ammonium sulphate precipitation, and chromatography using Q Sepharose, Sephacryl S-200, and Superose 12 columns. The apparent molecular mass of the enzyme was 83 kDa as determined in gel electrophoresis. Maximum activity was observed at pH 4.5 at 70°C. Enzyme showed stability stable in the pH range of 3.0-9.0 and lost 40% of its initial activity at the temperatures of 40, 50, and 60°C. In the presence of ions Na+, Ba2+, Co2+, Ni2+, Mg2+, Mn2+, Al3+, Zn2+, Ca2+ this enzyme maintained 90-105% of its maximum activity and was inhibited by Cr3+, Ag+, and Hg2+. The enzyme showed a transglycosylation property, by the release of oligosaccharides after 3 h of incubation with maltose, and specificity for short maltooligosaccharides and α-PNPG. The Km measured for the α-glucosidase was 0.07 μM, with a Vmax of 318.0 μmol/min/mg.

Purification and Biochemical Properties of a Glucose-Stimulated β-D-Glucosidase Produced by Humicola grisea var. thermoidea Grown on Sugarcane Bagasse: Cesar Vanderlei Nascimento , Flávio Henrique Moreira Souza , Douglas Chodi Masui , Francisco Assis Leone , Rosane Marina Peralta , João Atílio Jorge , Rosa Prazeres Melo Furriel; J. Microbiol. 2010;48(1):53-62. Published online March 11, 2010; DOI: https://doi.org/10.1007/s12275-009-0159-x

38 View
0 Download
57 Scopus

Abstract: The effect of several carbon sources on the production of mycelial-bound β-glucosidase by Humicola grisea var. thermoidea in submerged fermentation was investigated. Maximum production occurred when cellulose was present in the culture medium, but higher specific activities were achieved with cellobiose or sugarcane bagasse. Xylose or glucose (1%) in the reaction medium stimulated β-glucosidase activity by about 2-fold in crude extracts from mycelia grown in sugarcane bagasse. The enzyme was purified by ammonium sulfate precipitation, followed by Sephadex G-200 and DEAE-cellulose chromatography, showing a single band in PAGE and SDS-PAGE. The β-glucosidase had a carbohydrate content of 43% and showed apparent molecular masses of 57 and 60 kDa, as estimated by SDS-PAGE and gel filtration, respectively. The optimal pH and temperature were 6.0 and 50°C, respectively. The purified enzyme was thermostable up to 60 min in water at 55°C and showed half-lives of 7 and 14 min when incubated in the absence or presence of 50 mM glucose, respectively, at 60°C. The enzyme hydrolyzed p-nitrophenyl-β-D-glucopyranoside, p-nitrophenyl-β-galactopyranoside, p-nitrophenyl-β-D-fucopyranoside, p-nitrophenyl-β-D-xylopyranoside, o-nitrophenyl-β-Dgalactopyranoside, lactose, and cellobiose. The best synthetic and natural substrates were p-nitrophenyl-β-Dfucopyranoside and cellobiose, respectively. Purified enzyme activity was stimulated up to 2-fold by glucose or xylose at concentrations from 25 to 200 mM. The addition of purified or crude β-glucosidase to a reaction medium containing Trichoderma reesei cellulases increased the saccharification of sugarcane bagasse by about 50%. These findings suggest that H. grisea var. thermoidea β-glucosidase has a potential for biotechnological applications in the bioconversion of lignocellulosic materials.

Characterization of a Novel β-Glucosidase-Like Activity from a Soil Metagenome: Chengjian Jiang , Gefei Ma , Shuangxi Li , Tingting Hu , Zhiqun Che , Peihong Shen , Bing Yan , Bo Wu; J. Microbiol. 2009;47(5):542-548. Published online October 24, 2009; DOI: https://doi.org/10.1007/s12275-009-0024-y

39 View
0 Download
38 Scopus

Abstract: We report the cloning of a novel β-glucosidase-like gene by function-based screening of a metagenomic library from uncultured soil microorganisms. The gene was named bgl1C and has an open reading frame of 1,443 base pairs. It encodes a 481 amino acid polypeptide with a predicted molecular mass of about 57.8 kDa. The deduced amino acid sequence did not show any homology with known β-glucosidases. The putative β-glucosidase gene was subcloned into the pETBlue-2 vector and overexpressed in E. coli Tuner (DE3) pLacІ; the recombinant protein was purified to homogeneity. Functional characterization with a high performance liquid chromatography method demonstrated that the recombinant Bgl1C protein hydrolyzed D-glucosyl-β-(1-4)-D-glucose to glucose. The maximum activity for Bgl1C protein occurred at pH 8.0 and 42°C using p-nitrophenyl-β-D-glucoside as the substrate. A CaCl2 concentration of 1 mM was required for optimal activity. The putative β-glucosidase had an apparent Km value of 0.19 mM, a Vmax value of 4.75 U/mg and a kcat value of 316.7/min under the optimal reaction conditions. The biochemical characterization of Bgl1C has enlarged our understanding of the novel enzymes that can be isolated from the soil metagenome.

A Specific Short Dextrin-Hydrolyzing Extracellular Glucosidase from the Thermophilic Fungus Thermoascus aurantiacus 179-5: Ana Flavia Azevedo Carvalho , Aline Zorzetto Gonclves , Roberto da Silva , Eleni Gomes; J. Microbiol. 2006;44(3):276-283.; DOI: https://doi.org/2385 [pii]

40 View
0 Download

Abstract: The thermophilic fungus Thermoascus aurantiacus 179-5 produced large quantities of a glucosidase which preferentially hydrolyzed maltose over starch. Enzyme production was high in submerged fermentation, with a maximal activity of 30 U/ml after 336 h of fermentation. In solid-state fermentation, the activity of the enzyme was 22 U/ml at 144 h in medium containing wheat bran and 5.8 U/ml at 48 h when cassava pulp was used as the culture medium. The enzyme was specific for maltose, very slowly hydrolyzed starch, dextrins (2-7G) and the synthetic substrate (α-PNPG), and did not hydrolyze sucrose. These properties suggest that the enzyme is a type II α-glucosidase. The optimum temperature of the enzyme was 70?. In addition, the enzyme was highly thermostable (100% stability for 10 h at 60? and a half-life of 15 min at 80?), and stable within a wide pH range.

Degradation of Crystalline Cellulose by the Brown-rot Basidiomycete Fomitopsis palustris: Jeong-Jun Yoon , Young-Kyoon Kim; J. Microbiol. 2005;43(6):487-492.; DOI: https://doi.org/2301 [pii]

39 View
0 Download

Abstract: This study demonstrated that the brown rot basidiomycete Fomitopsis palustris was able to degrade crystalline cellulose (Avicel). This fungus could also produce the three major cellulases (exoglucanases, endoglucanases, and -glucosidase) when the cells were grown on 2.0% Avicel. Avicel degraded by F. palustris showed a decrease in relative crystallinity from 83% to 78.5% after 14 days of incubation. The characterization study indicated that optimum pH was 4.5 and optimum temperature was 70oC for exoglucanase (cellobiohydrolase) activity. Hydrolysis of Avicel by the crude enzyme from F. palustris yielded 1.6 mg/ml of glucose after 43 h, which corresponded to a cellulose conversion degree of 3.2%. Therefore, this study revealed for the first time that the brown rot basidiomycete F. palustris produces cellulases capable of yielding soluble sugars from crystalline cellulose.

Journal Articles

Molecular Detection of [alpha]-Glucosidase Inhibitor-producing Actinomycetes: Chang-Gu Hyun , Seung-Young Kim , Jin-Haeng Hur , Myung-Ji Seo , Joo-Won Suh , Soon-Ok Kim; J. Microbiol. 2005;43(3):313-318.; DOI: https://doi.org/2207 [pii]

47 View
0 Download

Abstract: In this study, we demonstrate the use of a PCR-based method for the detection of the specific genes involved in natural-product biosynthesis. This method was applied, using specifically designed PCR primers, to the amplification of a gene segment encoding for sedo-heptulose 7-phosphate cyclase, which appears to be involved in the biosynthetic pathways of C_7N aminoacyclitol or its keto analogue-containing metabolites, in a variety of actinomycetes species. The sequences of DNA fragments (about 540 bp) obtained from three out of 39 actinomycete strains exhibited a high degree of homology with the sedo-heptulose 7-phosphate cyclase gene, which has been implicated in acarbose biosynthesis. The selective cultivation conditions of this experiment induced the expression of these loci, indicating that the range of C_7N aminoacyclitol or its keto analogue-group natural products might be far greater than was previously imagined. Considering that a total of approximately 20 C_7N aminoacyclitol metabolites, or its keto analogue-containing metabolites, have been described to date, it appears likely that some of the unknown loci described herein might constitute new classes of C_7N aminoacyclitol, or of its keto analogue-containing metabolites. As these metabolites, some of which contain valienamine, are among the most potent antidiabetic agents thus far discovered, the molecular detection of specific metabolite-producing actinomycetes may prove a crucial step in current attempts to expand the scope and diversity of natural-product discovery.

Isolation and Characterization of a-Glucosidase Inhibitor from the Fungus Ganoderma lucidum: Shin-Duk Kim , Hong Joon Nho; J. Microbiol. 2004;42(3):223-227.; DOI: https://doi.org/2085 [pii]

38 View
0 Download

Abstract: An [alpha]-glucosidase inhibitor, SKG-3, was isolated from the fruiting bodies of Ganoderma lucidum and its physico-chemical properties were characterized. It was a highly specific and effective reversible inhibitor of [alpha]-glucosidase. It showed very potent inhibitory activity against [alpha]-glucosidase with an IC_50 value of 4.6 mg/ml, but no activity for any other glycosidases tested. Enzyme activity could be recovered upon dialysis, thus providing evidence for the reversibility of the inhibition. A Lineweaver-Burk plot indicated that the SKG-3 inhibition of [alpha]-glucosidase was competitive.

First
Prev
Page of 2
Next
Last

Search