- Detailed Modes of Action and Biochemical Characterization of endo-Arabinanase from Bacillus licheniformis DSM13
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Jung-Mi Park , Myoung-Uoon Jang , Jung-Hyun Kang , Min-Jeong Kim , So-Won Lee , Yeong Bok Song , Chul-Soo Shin , Nam Soo Han , Tae-Jip Kim
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J. Microbiol. 2012;50(6):1041-1046. Published online December 30, 2012
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DOI: https://doi.org/10.1007/s12275-012-2489-3
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An endo-arabinanase (BLABNase) gene from Bacillus licheniformis DSM13 was cloned and expressed in Escherichia coli, and the biochemical properties of its encoded enzyme were characterized. The BLABNase gene consists of a single
open reading frame of 987 nucleotides that encodes 328 amino acids with a predicted molecular mass of about 36 kDa. BLABNase exhibited the highest activity against debranched α-(1,5)-arabinan in 50 mM sodium acetate buffer (pH 6.0) at 55°C. Enzymatic characterization revealed that BLABNase hydrolyzes debranched or linear arabinans with a much higher activity than branched arabinan from sugar
beet. Enzymatic hydrolysis pattern analyses demonstrated BLABNase to be a typical endo-(1,5)-α-L-arabinanase (EC 3.2.1.99) that randomly cleaves the internal α-(1,5)-linked L-arabinofuranosyl residues of a branchless arabinan backbone to release arabinotriose mainly, although a small amount of arabino-oligosaccharide intermediates is also liberated. Our results indicated that BLABNase acts preferentially along with the oligosaccharides longer than arabinopentaose,
thus enabling the enzymatic production of various arabinooligosaccharides.
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Citations
Citations to this article as recorded by  - Functional Characterization of Endo- and Exo-Hydrolase Genes in Arabinan Degradation Gene Cluster of Bifidobacterium longum subsp. suis
Yewon Kang, Chang-Yun Choi, Jihun Kang, Ye-Rin Ju, Hye Bin Kim, Nam Soo Han, Tae-Jip Kim
International Journal of Molecular Sciences.2024; 25(6): 3175. CrossRef - Thermophilic Hemicellulases Secreted by Microbial Consortia Selected from an Anaerobic Digester
Luca Bombardi, Marco Orlando, Martina Aulitto, Salvatore Fusco
International Journal of Molecular Sciences.2024; 25(18): 9887. CrossRef - GH43 endo-arabinanase from Bacillus licheniformis: Structure, activity and unexpected synergistic effect on cellulose enzymatic hydrolysis
Erick Giancarlo S. Farro, Ana Elisa T. Leite, Isabela A. Silva, Jefferson G. Filgueiras, Eduardo R. de Azevedo, Igor Polikarpov, Alessandro S. Nascimento
International Journal of Biological Macromolecules.2018; 117: 7. CrossRef - Novel approaches for biotechnological production and application of L-arabinose
Csaba Fehér
Journal of Carbohydrate Chemistry.2018; 37(5): 251. CrossRef - Exploiting sp2‐Hybridisation in the Development of Potent 1,5‐α‐l‐Arabinanase Inhibitors
Travis Coyle, Aleksandra W. Debowski, Annabelle Varrot, Keith A. Stubbs
ChemBioChem.2017; 18(11): 974. CrossRef - An Acid-Adapted Endo-α-1,5-l-arabinanase for Pectin Releasing
Chong Lang, Rujian Yang, Ying Yang, Bei Gao, Li Zhao, Wei Wei, Hualei Wang, Shingo Matsukawa, Jingli Xie, Dongzhi Wei
Applied Biochemistry and Biotechnology.2016; 180(5): 900. CrossRef - In vitro digestion and fermentation properties of linear sugar-beet arabinan and its oligosaccharides
Jin Seok Moon, So Yeon Shin, Hye Sun Choi, Wooha Joo, Seung Kee Cho, Ling Li, Jung-Hyun Kang, Tae-Jip Kim, Nam Soo Han
Carbohydrate Polymers.2015; 131: 50. CrossRef - Increased biomass saccharification by supplementation of a commercial enzyme cocktail with endo-arabinanase from Bacillus licheniformis
Carla Botelho Machado, Ana Paula Citadini, Rosana Goldbeck, Evandro Antônio de Lima, Fernanda Lopes Figueiredo, Tony Márcio da Silva, Zaira Bruna Hoffmam, Amanda Silva de Sousa, Fábio Márcio Squina, Maria de Lourdes Teixeira de Moraes Poliz, Roberto Rulle
Biotechnology Letters.2015; 37(7): 1455. CrossRef - Biochemical Characterization of a Novel Endo-1,5-α-l-arabinanase fromRhizomucor miehei
Zhou Chen, Yu Liu, Qiaojuan Yan, Shaoqing Yang, Zhengqiang Jiang
Journal of Agricultural and Food Chemistry.2015; 63(4): 1226. CrossRef
- Monascus Red Pigment Overproduction by Coculture with Recombinant Saccharomyces cerevisiae Secreting Glucoamylase
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Ho-Soo Lim , Seung-Ku Yoo , Chul-Soo Shin , Young-Min Hyun
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J. Microbiol. 2000;38(1):48-51.
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Abstract
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In liquid cultures using sucrose media, the coculture of Monascus with recombinant Saccharomyces cerevisiae expressing the glucoamylase gene from Aspergillus niger enhanced red pigment production by approx. 19%, compared with the coculture of wild type S. cerevisiae. Coculture with recombinant S. cerevisiae was more effective than with wild type S. cerevisiae for Monascus red pigment production. Cocultures of Monascus with commercial amylases of Aspergillus also induced high production of pigment and morphological changes in a solid culture using sucrose media.
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