Site of secretion and properties of endogenous endo-β-1,4-glucanase components from Reticulitermes speratus (Kolbe), a Japanese subterranean termite

Watanabe, Hirofumi; Nakamura, Masaru; Tokuda, Gaku; Yamaoka, Ikuo; Scrivener, A.M.; Noda, Hiroaki

doi:10.1016/s0965-1748(97)00003-9

Cited by 113 publications

(61 citation statements)

References 26 publications

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“…Cellulase is a very important hydrolytic enzyme. Over the years, several authors have purified and reported properties of cellulase from a wide range of termite species including Nasutitermes walkeri (Schultz et al, 1986), Macrotermes mulleri (Rouland et al, 1988), Reticulitermes speratus (Watanabe et al, 1997), Hodotermopsis sjostesti and Nasutitermes takasagoensis (Fujita et al, 2008). Previously, Fagbohunka et al (2014) only partially purified cellulase from Ametermes eveuncifer and carried out inhibition studies along with other enzymes.…”

Section: Discussionmentioning

confidence: 99%

“…Findings by Tokuda and Watanabe (2007) showed that cellulases present in the flagellate-free termites, Nasutitermes takasagoensis and Nasutitermes walkeri were produced by symbiotic bacteria present in the hind gut of these termites, although cellulase activities in the guts of flagellate-free termites were significantly lower than those of flagellate-harbouring termites (Tokuda et al, 2004;. Cellulase characterized from various higher and lower termites have been shown to be similar in a number of properties in some bacteria and fungi (Watanabe et al, 1997). Properties of cellulase from various termites can therefore be compared with those of microorganisms which also play a role in the digestion of cellulose in the gut of termites.…”

Section: Discussionmentioning

confidence: 99%

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Purification and Characterization of Cellulase from Termite Ametermes eveuncifer (Silverstri) Soldiers

Fagbohunka¹,

Okonji²,

Ayinla³

2016

IJB

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Cellulase enzyme was purified and characterized from termite soldiers (Ametermes eveuncifer) using 70% ammonium sulphate precipitation, ion exchange chromatography and affinity chromatography. The enzyme isolated had a specific activity of 5.04 U/mg with a percentage yield of 11.7%. The enzyme showed maximum activity at 50 0 C and pH 8. The enzyme was not inhibited by Ba 2+ at a concentration of 1mM and Pb 2+ at 10 mM concentration but was inhibited by other metal ions at 1 mM and 10 mM concentrations of their salts (NaCl, KCl, MnCl 2 , and NiCl 2 ) ,

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Purification and Characterization of Cellulase from Termite Ametermes eveuncifer (Silverstri) Soldiers

Fagbohunka¹,

Okonji²,

Ayinla³

2016

IJB

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“…Termites efficiently degrade woody cellulose through a symbiotic collaboration with gut microorganisms, and they absorb the degradation products as nutrients (Nakashima et al, 2002;Watanabe et al, 1997;Zhou et al, 2007). In the first step of cellulose degradation, termites secrete an endo-β-1,4-glucanase from their salivary glands that enzymatically reduces the size of cellulose.…”

Section: Introduction 1)mentioning

confidence: 99%

A New α-Amylase from Reticulitermes speratus KMT1

Park¹,

Ham²,

Ahn

et al. 2014

Journal of the Korean Wood Science and Technology

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Termites are wood pests that cause vast economic damage every year. They digest both cellulose and starch, but the enzymes for starch digestion have not been well characterized. We obtained complete amino acid sequence information on the KME1 α-amylase from Reticulitermes speratus KMT1 through analysis of total mRNA sequences. The KME1 enzyme has two α-amylase domains and is 68% identical to the α-amylase from Blattellager manica, its closest relative in the GenBank database. Some unique features of its conserved region and its distant evolutionary relationship to other insect α-amylases suggest that KME1 is a new type of α-amylase.

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“…Complete depolymerization of cellulose to glucose requires another sort of cello-oligosaccharide-degrading enzyme, 1,4-b-glucosidase (EC 3.2.1.21). Thus far, cellulolytic enzymes have been isolated and characterized from bacteria [2], fungi [2], plants [3], molds [4], microbes [5], arthropods [6][7][8][9][10][11], nematodes [12], mollusks [13][14][15][16][17][18][19] and sea urchin [20].…”

Section: Introductionmentioning

confidence: 99%

Purification and biochemical characterization of a cellulase from the digestive organs of the short-spined sea urchin Strongylocentrotus intermedius

et al. 2012

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We isolated a cellulase from the digestive organs of the short-spined sea urchin Strogylocentrotus intermedius using a combination of ion-exchange chromatography and gel filtration together with an assay for carboxymethylcellulase activity. The isolated cellulase was stained as a single band by Congo red. The molecular weight of the isolated cellulase, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reducing conditions, was 59 kDa. The isolated cellulase exhibited hydrolytic activity toward carboxymethyl cellulose, with an optimum temperature and pH of 30°C and pH 8.0, respectively. The thermal stability of the enzyme was characterized by determining the temperature at which activity decreased by 50 % with treatment for 30 min at pH 7.0 and found to be 32°C. Cellulase activity remained at a high level at 5-20°C, which is the growth temperature of the short-spined sea urchin. These results confirm that the short-spined sea urchin should preferably be reared at a water temperature of \20°C.

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Site of secretion and properties of endogenous endo-β-1,4-glucanase components from Reticulitermes speratus (Kolbe), a Japanese subterranean termite

Cited by 113 publications

References 26 publications

Purification and Characterization of Cellulase from Termite Ametermes eveuncifer (Silverstri) Soldiers

Purification and Characterization of Cellulase from Termite Ametermes eveuncifer (Silverstri) Soldiers

A New α-Amylase from Reticulitermes speratus KMT1

Purification and biochemical characterization of a cellulase from the digestive organs of the short-spined sea urchin Strongylocentrotus intermedius

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