Aminoacylase pellets

Hirano, Ken‐ichi; Karube, Isao; Suzuki, Shuichi

doi:10.1002/bit.260190303

Cited by 25 publications

(8 citation statements)

References 9 publications

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“…Use of fungal pellets for immobilization of biomass and enzyme have also been described by Anderson [20]. Pellets of Aspergillus niger species have been used as an effective immobilized enzyme support for glucose oxidase and aminoacylase [21].…”

Section: Introductionmentioning

confidence: 99%

Understanding the morphology of fungi

Pazouki

Panda

2000

Bioprocess Engineering

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Filamentous fungi comprise an industrially very important collection of microorganisms, since they are used for the production of a wide variety of products ranging from primary metabolites to secondary metabolites and further on to industrial enzymes (such as proteases, lipases and antibiotics). It is known that fungal morphology is often considered as one of the key parameters in industrial production. For the production of fungal metabolite products, the desired morphology varies from one product to another. Many parameters affect the morphology of fungi during the process of fermentation, among them speed of agitation, speci®c growth rate, dissolved oxygen, number of spores or conidia per liter of fermentation broth are important and should be considered when higher yield is desired in the process. It is, therefore, of considerable importance to understand the mechanism underlying the morphology of the cell, its growth and product formation by ®lamentous fungi. Such knowledge may be used in the optimization of the microbial process. Several literatures with various fungi to study their morphology, relating enzyme or product production to the character of the fungi in the study is reviewed. It is also considered that how the process parameters affects the morphology. The aim of this communication is to review the relevant literature to understand the morphology of ®lamentous fungi. List of symbols bhyphal density, lm/tip D i impeller diameter, m D pellet diameter (in Eqs. 4 and 5), mm D r dilution rate, h )1 k constant, number of section used for branching (in Eq. 7) K c constant K r constant (in Eq. 5) K r linear colony radial growth rate (in Eq. 1), lm/h L e mean length of main hyphae, lm L e *mean dimensionless length, lm L t mean total length of hyphae, lm L hgu mean length of hyphal growth unit, lm M 0 dry weight of mycelia at time t 0 , g M 1 dry weight of mycelia at time t 1 , g n number of disrupted pellets N impeller speed, h )

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Section: Introductionmentioning

confidence: 99%

Understanding the morphology of fungi

Pazouki

Panda

2000

Bioprocess Engineering

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“…Aminoacylase (EC 3.5.1.14) and D-glucose oxidase (EC 1.1.3.4) have been bound on to mycelial pellets of Aspergillus ochraceus by the co-cross-linking method (Section II,C,l,c), using glutaraldehyde and albumin (Hirano et al, 1977;Karube et aL, 1977c). By using the metal-chelation method (Section II,B,2), glucoamylase (EG 3.2.1.3), α-amylase (EC 3.2.1.1), and a protease have been coupled to titanium(IV)-treated Saccharomyces cerevisiae cells.…”

Section: E Miscellar^eous Methods Of Whole-cell Immobilizationmentioning

confidence: 99%

Immobilized Living Cells and Their Applications

Kennedy

Cabral

1983

Immobilized Microbial Cells

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“…Enzyme leakage from microbial pellets has been observed earlier. Hirano et al (1977) reported leakage of 68% of aminoacylase activity during incubation for 4 days of A. ochraceus pellets at p H 7.0 and 20 ° C in 0.05 M phosphate buffer. In pellets of Mortierella vinacea vat.…”

Section: Repeated Lactose Hydrolysismentioning

confidence: 99%

Mycelia-associated ?-galactosidase activity in microbial pellets of Aspergillus and Penicillium strains

Réczey

Stålbrand

Hahn-Härerdal³

et al. 1992

Appl Microbiol Biotechnol

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Pellet formation and production of myceliaassociated fl-galactosidase were investigated in 15 Aspergillus and Penicillium strains. Mycelia-associated enzyme activity was measured in sonicated homogenates. The properties of the mycelia-associated fl-galactosidas6 of A. phoenicis QM 329 was investigated. The p H optim u m of the mycelia-associated enzyme was 4.0. The optimum temperature under assay conditions was 70°C and the optimum temperature for repeated lactose hydrolysis was 60 ° C. Repeated batch hydrolysis of lactose was made with pellets from five Aspergillus strains. A. phoenicis QM 329 showed the least enzyme leakage from the pellets during hydrolysis. From repeated lactose hydrolysis experiments it was estimated that 50% of the mycelia-associated fl-galactosidase activity remained after 1300 h.

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Aminoacylase pellets

Cited by 25 publications

References 9 publications

Understanding the morphology of fungi

Understanding the morphology of fungi

Immobilized Living Cells and Their Applications

Mycelia-associated ?-galactosidase activity in microbial pellets of Aspergillus and Penicillium strains

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