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  • 1
    Electronic Resource
    Electronic Resource
    β-glucanases of the yeast Pichia polymorpha (1975)
    Springer
    Archives of microbiology 104 (1975), S. 201-206 
    Details
    ISSN: 1432-072X
    Keywords: Pichia polymorpha ; β-Glucanases ; Laminarin ; Pustulan ; β-Glucosidase ; Yeast Protoplasts ; Micromonospora chalcea ; Helix pomatia
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Fractionation of proteins secreted into the culture medium by intact cells and protoplasts of Pichia polymorpha showing enzyme activity against laminarin, pustulan or p-nitrophenyl-β-d-glucopyranoside has been performed, and the results compared with those obtained with cell-free extracts and lysed protoplasts. Fractionation with DEAE Sephadex A50 has proved to be the best method, yielding at least three fractions which hydrolyse laminarin. One of these fractions was active on both laminarin and pustulan. Filtration on Sephadex G-100 column only yielded one active preparation. Evidence supporting the conclusion that there are three different β-glucanases located in the periplasmic space is presented.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00447325
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    On the effect of glucono-δ-lactone on the yeast Pichia polymorpha (1976)
    Springer
    Archives of microbiology 109 (1976), S. 157-161 
    Details
    ISSN: 1432-072X
    Keywords: Pichia polymorpha ; Streptomyces venezuelae RA ; Penicillium italicum ; β-Glucanase ; Glucono-δ-lactone
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Investigation has been made into the action of glucono-δ-lactone on living cells of Pichia polymorpha in relation to the uptake of D-(U-14C) glucose, and the incorporation of (2-14C) uracil and L-(U-14C)-threonine into RNA and protein respectively. Other factors such as the action of glucono-δ-lactone on cell morphology and on enzymic synthesis have also been studied. The action of this compound on β-glucanase has been found to take place in the hydrolytic power and not in the synthesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00425129
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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