Purification and characterization of two forms of endo-?-1,4-mannanase from a thermotolerant fungus, IMI 385708 (formerly IMI 158749)

Puchart, Vladimı́r; Vršanská, Mária; Svoboda, Pavel; Pohl, Jan; Ögel, Zümrüt B.; Biely, Peter

doi:10.1016/j.bbagen.2004.06.022

Cited by 92 publications

(88 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…By contrast, endo-acting GH5 mannanases often contain cellulose-targeted CBMs (8,43,44), and thus the function of GH5 and GH26 C. japonicus mannanases proposed here is likely to have a generic biolog-FIGURE 6. The mannanase repertoire of C. japonicus.…”

Section: Discussionmentioning

confidence: 99%

The Cellvibrio japonicus Mannanase CjMan26C Displays a Unique exo-Mode of Action That Is Conferred by Subtle Changes to the Distal Region of the Active Site

Cartmell

Topakas

Ducros

et al. 2008

Journal of Biological Chemistry

View full text Add to dashboard Cite

The microbial degradation of the plant cell wall is a pivotal biological process that is of increasing industrial significance. One of the major plant structural polysaccharides is mannan, a ␤-1,4-linked D-mannose polymer, which is hydrolyzed by endoand exo-acting mannanases. The mechanisms by which the exoacting enzymes target the chain ends of mannan and how galactose decorations influence activity are poorly understood. Here we report the crystal structure and biochemical properties of CjMan26C, a Cellvibrio japonicus GH26 mannanase. The exoacting enzyme releases the disaccharide mannobiose from the nonreducing end of mannan and mannooligosaccharides, harnessing four mannose-binding subsites extending from ؊2 to ؉2. The structure of CjMan26C is very similar to that of the endo-acting C. japonicus mannanase CjMan26A. The exo-activity displayed by CjMan26C, however, reflects a subtle change in surface topography in which a four-residue extension of surface loop creates a steric block at the distal glycone ؊2 subsite. endoActivity can be introduced into enzyme variants through truncation of an aspartate side chain, a component of a surface loop, or by removing both the aspartate and its flanking residues. The structure of catalytically competent CjMan26C, in complex with a decorated manno-oligosaccharide, reveals a predominantly unhydrolyzed substrate in an approximate 1 S 5 conformation. The complex structure helps to explain how the substrate "side chain" decorations greatly reduce the activity of the enzyme; the galactose side chain at the ؊1 subsite makes polar interactions with the aglycone mannose, possibly leading to suboptimal binding and impaired leaving group departure. This report reveals how subtle differences in the loops surrounding the active site of a glycoside hydrolase can lead to a change in the mode of action of the enzyme.The plant cell wall represents the dominant source of organic carbon in the biosphere and as such supports many facets of terrestrial and marine life. Access to this valuable source of carbon is mediated by extensive microbial enzyme consortia, which generate sugars that are utilized by microbial ecosystems to the benefit of plants, mammalian herbivores, and insects. These degradative enzymes are increasingly deployed in industrial processes, and it is apparent that their use in producing second generation, lignocellulosebased, biofuels is of considerable environmental significance (1, 2). Among the major polysaccharides in softwoods and angiosperms are the mannans. These polysaccharides comprise a backbone of ␤-1,4-linked D-mannopyranose sugars (known as "mannan") or a heterogeneous combination of ␤-1,4-D-mannose and ␤-1,4-D-glucose units (termed "glucomannan"), which can be decorated with ␣-1,6-galactose side chains to yield "galactomannan" and "galactoglucomannan," respectively (3). For complete enzymatic degradation, the galactose decorations are removed by ␣-galactosidases (4, 5), whereas the internal glycosidic linkages in mannans are cleaved by endo-␤-1,4 mannanases ...

show abstract

Section: Discussionmentioning

confidence: 99%

The Cellvibrio japonicus Mannanase CjMan26C Displays a Unique exo-Mode of Action That Is Conferred by Subtle Changes to the Distal Region of the Active Site

Cartmell

Topakas

Ducros

et al. 2008

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…However, only a few thermostable β-mannanases have been characterised from these (Puchart et al 2004; Yang et al 2015). Keeping this point in mind we evaluated a thermophilic fungus, M. cinnamomea NFCCI 3724 for optimised production of β-mannanase on PKC using the response surface methodology approach.…”

Section: Introductionmentioning

confidence: 99%

Experimental design of response surface methodology used for utilisation of palm kernel cake as solid substrate for optimised production of fungal mannanase

et al. 2016

View full text Add to dashboard Cite

The results obtained from this work strongly indicate that the solid state fermentation (SSF) system using the palm kernel cake (PKC) as a substrate is an economical method for the production of β-mannanase at extremely low operational cost based on the fact that PKC is one of the cheap and abundant agro-waste by-products of the palm oil industry. Under initial conditions, i.e. 2 mm particle size of PKC, the moisture ratio of 1:1 of PKC:moistening agent and pH 7, Malbranchea cinnamomea NFCCI 3724 produced 109 U/gram distribution of the substrate (gds). The production of β-mannanase was optimised by the statistical approach response surface methodology (RSM) using independent variables, namely initial moisture (12.5), pH (9.0) and solka floc (100 mg). Noticeably, six fold enhancement of β-mannanase production (599 U/gds) was obtained under statistically optimised conditions. HPLC results revealed that β-mannanase is an endo-active enzyme that generated manno-oligosaccharides with a degree of polymerisation (DP) of 3 and 4. Semi-native PAGE analysis revealed that M. cinnamomea produced three isoforms of mannanase. Selective production of oligosaccharide makes M. cinnamomea β-mannanase an attractive enzyme for use in food and nutraceutical industries.

show abstract

“…-1,4-Mannanase has been isolated from bacteria (Araki, 1983 ;Akino et al, 1988;Talbot et al, 1990;Braithwaite et al, 1995;Nakajima and Matsuura, 1997;Li et al, 2000;Politz et al, 2000;Kansoh and Nagieb, 2004;Li et al, 2006), fungi (Johnson, 1990;Stalbrand et al, 1993;Kurakake et al, 2001;Puchart et al, 2004;Naganagouda et al, 2009), higher plants (Shimahara et al, 1975;Marraccini et al, 2001), and mollusks (Yamaura and Matsumoto, 1993;Yamaura et al, 1996;Xu et al, 2002a andOotsuka et al, 2006). Compared with bacterial and fungal enzymes, molluscan enzymes have not been well investigated, i.e., only four -1,4-mannanases have been investigated in Pomacea insularus (Yamaura and Matsumoto, 1993), Littorina brevicula (Yamaura et al, 1996), Mytilus edulis (Xu et al, 2002a and b), and Haliotis discus hannai (Ootsuka et.…”

Section: Introductionmentioning

confidence: 99%

An endo-β-1,4-mannanase, AkMan, from the common sea hare Aplysia kurodai

Zahura¹,

Rahman²,

Inoue³

et al. 2010

Comparative Biochemistry and Physiology Part B: Biochemistry an

View full text Add to dashboard Cite

Purification and characterization of two forms of endo-?-1,4-mannanase from a thermotolerant fungus, IMI 385708 (formerly IMI 158749)

Cited by 92 publications

References 35 publications

The Cellvibrio japonicus Mannanase CjMan26C Displays a Unique exo-Mode of Action That Is Conferred by Subtle Changes to the Distal Region of the Active Site

The Cellvibrio japonicus Mannanase CjMan26C Displays a Unique exo-Mode of Action That Is Conferred by Subtle Changes to the Distal Region of the Active Site

Experimental design of response surface methodology used for utilisation of palm kernel cake as solid substrate for optimised production of fungal mannanase

An endo-β-1,4-mannanase, AkMan, from the common sea hare Aplysia kurodai

Contact Info

Product

Resources

About