Metal-dependent thermal stability of recombinant endo-mannanase (ManB-1601) belonging to family GH 26 from Bacillus sp. CFR1601

Enzyme and Microbial Technology
Praveen Kumar SrivastavaMukesh Kapoor

Abstract

A GH 26 endo-mannanase from Bacillus sp. CFR1601 was purified to homogeneity (Mw ∼39kDa, specific activity 10,461.5±100IU/mg). Endo-mannanase gene (manb-1601, 1083bp, accession No. KM404299) was expressed in Escherichia coli BL21 (DE3) and showed typical fingerprints of α/β proteins in the far-UV CD. A high degree of conservation among amino acid residues involved in metal chelation (His-1, 23 and Glu-336) and internal repeats (122-152 and 181-212) was observed in endo-mannanases reported from various Bacillus sp. Thermal inactivation kinetics suggested that metal ions are quintessential for stabilization of ManB-1601 structure as holoenzyme (Ea 87.4kcal/mol, ΔH 86.7kcal/mol, ΔS 186.6cal/k/mol) displayed better values of thermodynamic parameters compared to metal-depleted ManB-1601 (Ea 47kcal/mol, ΔH 45.7kcal/mol, ΔS 64.7cal/k/mol). EDTA treatment of ManB-1601 not only lead to transitions in both secondary and tertiary structure but also promulgated the population of conformational state that unfolds at lower temperature. ManB-1601 followed a three-state process for thermal inactivation wherein loss of tertiary structure preceded the concurrent loss of secondary structure and activity.

References

Oct 5, 1990·Journal of Molecular Biology·S F AltschulD J Lipman
Dec 10, 1999·The Journal of Biological Chemistry·E Sudharshan, A G Rao
Nov 6, 2002·Journal of Molecular Biology·Joel D A TyndallMalcolm D Walkinshaw
Mar 26, 2003·Proceedings of the National Academy of Sciences of the United States of America·Ornella MaglioWilliam F DeGrado
Apr 30, 2003·The Journal of Biological Chemistry·Mudeppa Devaraja GoudaNaikankatte Ganesh Karanth
Jun 26, 2003·Nucleic Acids Research·Elisabeth GasteigerAmos Bairoch
Jun 30, 2004·Journal of Molecular Biology·Jannick Dyrløv BendtsenSøren Brunak
Jul 27, 2005·Current Opinion in Structural Biology·Ewan R G MainLynne Regan
Nov 23, 2005·Bioinformatics·Konstantin ArnoldTorsten Schwede
Jun 5, 2007·Biochimica Et Biophysica Acta·T C JyothiA G Appu Rao
Oct 24, 2007·Journal of Biotechnology·Montarop YamabhaiBancha Buranabanyat
Apr 4, 2008·Applied Microbiology and Biotechnology·L R S Moreira, E X F Filho
May 24, 2011·Biochimica Et Biophysica Acta·Yuya KumagaiTadashi Hatanaka
May 31, 2011·Biochimica Et Biophysica Acta·Jean Borges BertoldoHernán Terenzi
Dec 14, 2011·Journal of Structural Biology·Camila Ramos dos SantosMario Tyago Murakami
Feb 9, 2012·Applied Microbiology and Biotechnology·Prakram Singh ChauhanNaveen Gupta
Jun 15, 2012·Journal of Agricultural and Food Chemistry·Li-Jung YinShann-Tzong Jiang

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Citations

Apr 20, 2019·The Journal of Biological Chemistry·Viktoria BågenholmHenrik Stålbrand
Oct 17, 2017·Applied Microbiology and Biotechnology·Mario Cezar Rodrigues ManoGláucia Maria Pastore
Aug 14, 2019·Biotechnology and Applied Biochemistry·Monia BlibechHichem Chouayekh
Oct 10, 2020·Critical Reviews in Biotechnology·Gaurav Singh Kaira, Mukesh Kapoor
Jan 2, 2021·Frontiers in Bioengineering and Biotechnology·Aneesa Dawood, Kesen Ma
Feb 6, 2019·Biochemical and Biophysical Research Communications·Gaurav Singh Kaira, Mukesh Kapoor
Apr 30, 2019·International Journal of Biological Macromolecules·Gaurav Singh KairaMukesh Kapoor
Nov 27, 2021·Preparative Biochemistry & Biotechnology·Yangcun SunJingping Ge

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