Kinetic study on the ?-glucosidase-catalysed reaction of Trichoderma viride cellulase

Montero, Manuel; Romeu, A

doi:10.1007/bf00170085

Cited by 22 publications

(16 citation statements)

References 11 publications

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“…The results reported in this work (Fig. 3) show that endoglucanase and glucosidase retained 50% of their activities at pH 5.0 after 18.2 and 10.3 h at 60oc, respectively, whereas at 70°C the respective values were 6.5 and 3.1 h. These values competed favourably with those reported for certain cellulolytic microorganisms (Srivastava et al, 1984;Hong et al, 1986;Montero and Romeu, 1992). In Table 3 the maximum enzyme yields produced simultaneously in the present work are compared with those reported for other endoglucanase and 13-glucosidase hyperproducing fungi.…”

Section: Resultssupporting

confidence: 61%

Controlling simultaneous production of endoglucanase and beta-glucosidase by Fusarium oxysporum in submerged culture

et al. 1995

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The simultaneous production of endoglucanase and fl-glucosidase by Fusarium oxysporum was investigated in submerged culture. Consecutive optimization of growth conditions resulted in the correction of large activity differences, observed during production of enzymes, and substantially enhanced low enzyme yields. At optimum growth conditions yields as high as 1650 and 232 U per g of carbon source of endoglucanase and fi-glucosidase were obtained respectively competing favourably with those reported for microorganisms grown on the same car&m source. The most important kinetic characteristics of the enzymes were the high temperature optima of endoglucanase (6~C) and fl-glucosidase (65°C) and the exceptionally high thermostability of endoglucanase, The latter enzyme retained 50Ue of the activity at pH 5.0 after approximately 6.5 h at 7~C

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Section: Resultssupporting

confidence: 61%

Controlling simultaneous production of endoglucanase and beta-glucosidase by Fusarium oxysporum in submerged culture

et al. 1995

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“…As shown in Table 2, IC50 (concentration of the inhibitor required to cause 50% inhibition) values of cyclic alcohol and the corresponding D glucopyranosides used were determined using pNP G and the above three enzymes. Although all alcohols tested had no inhibitory activity for glucosidases from A. niger and T. viride, a relatively 27) and T. viride 28) are also shown. weak inhibitory activity for sweet almond enzyme was observed.…”

Section: Resultsmentioning

confidence: 89%

Enzymatic Syntheses of Cycloalkyl .BETA.-D-Glucopyranosides and Their Inhibition Activity for Plant .BETA.-Glucosidase

高田¹,

小川²

2004

J. Appl. Glycosci.

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Various models have been proposed for the reaction mechanism of glycosylase in the transition state, 1 4) but a reasonable model remains to be established. The oxocarbonium ion model has been applied to interpret the reaction mechanism of many glycosylases such as lysozyme, 5,6) glucoamylase 7) and glucosidase. 8) In this mechanism, when the glycosidic bond is cleaved, a glycosyl oxocarbonium ion intermediate is formed for catalysis. Evidence of the role of the transition state intermediates came from inhibition studies involving validamine, 9) N substituted valiolamine derivatives, 10) acarbose, 11) nojirimycin, 12) 1 deoxy nojirimycin 13) and N substituted derivatives of 1 deoxynojirimycin. 14) These inhibitors have been designed, synthesized and purified from plant extracts or the culture broth of microorganisms as the analogues of the charge and or the shape of the oxocarbonium ion like transition state intermediates. 15) They have an easily pro-tonated basic nitrogen atom in the position of the anomeric oxygen or the ring oxygen atom. However, the incorporation of a nitrogen positive center into a pyranose ring requires a relatively long reaction sequence. 16) As its structural similarity with the oxocarbonium ion like transition state intermediates, many researchers have performed their inhibition studies on glycosylases using glucono 1,5 lactone. 17 19) This compound is a relatively strong inhibitor toward glucosidases and has no nitrogen atom in a pyranose ring. However, it has been pointed out that their tendency to undergo hydrolytic ring opening under mildly basic conditions and the conversion into glucono 1,4 lactone (inactive) are the great disadvantage of the measurement of inhibition constants. 18,19) We therefore attempted to prepare more convenient glucosidase inhibitors by enzymatic method, which have rather simple chemical structures without a nitrogen atom in the position of the anomeric oxygen or the ring oxygen atom, and are quite stable in an aqueous solution. MATERIALS AND METHODSMaterials. Cyclopropanemethanol (CPAM) was purchased from Kanto Kagaku Co., Ltd. (Japan). Cyclopentanol (CPE) and cyclopentanemethanol (CPEM) were obtained from Lancaster Co., Ltd. (England). p Nitorophenyl glucopyranoside (pNP G) was a product of Nihon Shokuhin Kako Co., Ltd. (Tokyo). The highly purified glucosidases from Aspergillus niger and Trichoderma viride were generous gifts from Dr. T. Unno, Nihon Shokuhin Kako Co., Ltd. (Japan) and Dr. G. Okada, Shizuoka University (Japan), respectively. The purified sweet almond glucosidase was purchased from Sigma Aldrich (USA). These purified glucosidases were used for the inhibitory studies. On the other hand, glucosidases from Trichoderma reesei (Cellcrust) and A. niger (Novozyme 188) were obtained from Novo Nordisk A S, and the enzymes from T. viride (Meicelase) and sweet almond (BGH 101) were purchased from Meiji Seika Kaisha, Ltd. (Japan) and Toyobo Co., Ltd. (Japan), respectively. These enzymes were used for the preparation of cycloalkyl D J. Appl. Glycosci., 5...

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“…6 for the range of concentrations used). Figure 7 shows that addition of the ␤-glucosidase increased hydrolysis significantly, possibly by decreasing the inhibitory effect of cellobiose on CBHI (Montero and Romeu, 1992;Philippidis et al, 1993;Kruus et al, 1995). The increase in digestion was also evident in mixture B.…”

Section: Effects Of Total Concentration Of the Optimized Mixturementioning

confidence: 75%

“…Since ␤-glucosidase can reduce the inhibitory effects of cellobiose (Montero and Romeu, 1992;Philippids et al, 1993;Walker et al, 1993;Kruus et al, 1995), we determined the minimal amount of ␤-glucosidase needed to relieve the cellobiose inhibition (Fig. 2).…”

Section: Results and Discussion (1) ␤-Glucosidase Effectsmentioning

confidence: 99%

Factorial optimization of a six-cellulase mixture

Kim

Irwin

Walker

et al. 1998

Biotechnol. Bioeng.

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Kinetic study on the ?-glucosidase-catalysed reaction of Trichoderma viride cellulase

Cited by 22 publications

References 11 publications

Controlling simultaneous production of endoglucanase and beta-glucosidase by Fusarium oxysporum in submerged culture

Controlling simultaneous production of endoglucanase and beta-glucosidase by Fusarium oxysporum in submerged culture

Enzymatic Syntheses of Cycloalkyl .BETA.-D-Glucopyranosides and Their Inhibition Activity for Plant .BETA.-Glucosidase

Factorial optimization of a six-cellulase mixture

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