Kinetic characterization of a crude β-d-glucosidase from Aspergillus wentii Pt 2804

Srivastava, Smita; Gopalkrishnan, K. S.; Ramachandran, K.B.

doi:10.1016/0141-0229(84)90005-x

Cited by 40 publications

(13 citation statements)

References 7 publications

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“…The result of this work shows that Penicillium oxalicum was able to utilize all the substrates used in our study for growth. The cellulolytic enzymes were substrate dependent as reported previously (Jorgensen et al, 2005;Srivastava et al, 1984).…”

Section: Discussionmentioning

confidence: 99%

Optimization of cellulase production by <i>Penicillium oxalicum</i> using banana agrowaste as a substrate

Shah¹,

Kalia

Patel

2015

J. Gen. Appl. Microbiol.

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Section: Discussionmentioning

confidence: 99%

Optimization of cellulase production by <i>Penicillium oxalicum</i> using banana agrowaste as a substrate

Shah¹,

Kalia

Patel

2015

J. Gen. Appl. Microbiol.

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“…The aspergilli are known to be good producers of extracellular P-glucosidase ( SRIVASTAVA et al 1984, DUFF 1985, WASE et al 1985, VOLFOVA and KYSLIKOVA 1987 and Aspergillus niduluns in particular, in addition to producing p-glucosidase (BAGGA and SANDHU 1987), represents one of the best model systems for such studies (TIMBERLAKE and HAMER 1986).…”

Section: P-i 4-glucosidase Constitutes An Important Component Of Celmentioning

confidence: 99%

Qualitative and quantitative changes in β‐1,4‐glucosidase accompanying growth of Aspergillus nidulans

Sharma¹,

Bagga²,

Sandhu³

1990

J. Basic Microbiol.

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A comparative study of the wild type A. nidulans and a mutant strain aco-T69 (lacking conidia and cleistothecia) revealed the better production of beta-1,4-glucosidase in the former. The relative distribution of the enzyme levels in various morphological structures viz. somatic hyphae, spores and cleistothecia also showed a variation. Highest specific activity was found in the cleistothecial extracts. The electrophoretic analysis of the wild type strain demonstrated the presence of three isoenzymes of beta-1,4-glucosidase i.e. beta-GLU I, beta-GLU II and beta-GLU III, the number of which varies from one to three during the growth of the organism. The parallel study of the mutant strain showed complete absence of beta-GLU II. All three forms were present in the somatic hyphae and cleistothecial extracts while spore extracts depicted the absence of beta-GLU III in the wild type.

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“…The half-life of enzymes was calculated from the values of thermal decay constants at different temperatures. 39 …”

Section: Temperature/activity Profiles and Thermal Stabilitymentioning

confidence: 99%

Kinetic behaviour and stability of Escherichia coli ATCC27257 alkaline phosphatase immobilised in soil humates

et al. 2003

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Alkaline phosphatase (EC 3.1.3.1) extracted from Escherichia coli ATCC27257 was immobilised by co-flocculation with soil humates in the presence of Ca 2þ . The effects of time, temperature, pH and concentration of enzyme and support on immobilisation were studied. Between 58 and 92% of the added phosphatase was strongly bound to the humates, depending on the conditions of immobilisation used. Some characteristics of the humate-phosphatase complexes and of the free enzyme were compared. The enzymatic complexes showed values of K m (2.22 mM) and activation energy (33.4 kJ mol À1 ) similar to those of the free enzyme (2.00 mM and 27.6 kJ mol À1 ). The pH/activity profiles revealed no change in terms of shape or optimum pH (10.5) upon immobilisation of alkaline phosphatase. However, the immobilised enzyme showed maximal activity in the range of 80-100°C, while the free enzyme had its highest activity at 60°C. The thermal stability of alkaline phosphatase was enhanced by complexation to the soil humates.

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Kinetic characterization of a crude β-d-glucosidase from Aspergillus wentii Pt 2804

Cited by 40 publications

References 7 publications

Optimization of cellulase production by <i>Penicillium oxalicum</i> using banana agrowaste as a substrate

Optimization of cellulase production by <i>Penicillium oxalicum</i> using banana agrowaste as a substrate

Qualitative and quantitative changes in β‐1,4‐glucosidase accompanying growth of Aspergillus nidulans

Kinetic behaviour and stability of Escherichia coli ATCC27257 alkaline phosphatase immobilised in soil humates

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