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  • 1
    Electronic Resource
    Electronic Resource
    Analysis of astaxanthin and other carotenoids from several Phaffia rhodozyma mutants (1995)
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 43 (1995), S. 1396-1399 
    Details
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/jf00053a049
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  • 2
    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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  • 3
    Electronic Resource
    Electronic Resource
    Genetic determination of polygalacturonase production in wild-type and laboratory strains of Saccharomyces cerevisiae (1997)
    Springer
    Archives of microbiology 167 (1997), S. 284-288 
    Details
    ISSN: 1432-072X
    Keywords: Key words Polygalacturonase ; Saccharomyces ; cerevisiae ; Genetic determination ; Mutants ; Complementation groups
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The genetic determination of polygalacturonase (PG) production in Saccharomyces cerevisiae was studied by biochemical and classical genetic techniques. Crosses of PG+ strains with PG– strains showed that in the haploid wild-type-derived strain, two structural genes were involved in the production of a hydrolysis halo on plates with polygalacturonic acid. However, in the case of PG+ laboratory strain IM1-8b, the phenotype was controlled by only one structural gene although the analysis of PG– IM1-8b mutants demonstrated the existence of at least two complementation groups. All these genetic results were assessed biochemically by means of cation-exchange chromatography. Two enzymes were separated in the wild-type strain, and only one in the laboratory strain. The three enzymes had different K m values, molecular masses, and optimal pHs for activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050445
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  • 4
    Electronic Resource
    Electronic Resource
    Isolation and characterization of a mutant of Saccharomyces cerevisiae affected in the FLO1 locus (1996)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 137 (1996), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract A non-flocculent strain of Saccharomyces cerevisiae was selected after EMS mutation of a flocculent and heterozygous FLO1 locus diploid. The analysis of 25 asci from this diploid showed in all cases segregation 0F:4NF, thus confirming that it was probably affected in the desired gene. After sporulation and dissection of asci, three haploid strains were chosen, which were altered in the locus FLO1. Crossing these three strains with two other ones having markers for ADE1 and pho11::LEU2, we could map the mutation at ca. 4.3 cM and ca. 37.7 cM from the PHO11 and ADE1 loci respectively.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1996.tb08082.x
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  • 5
    Electronic Resource
    Electronic Resource
    Genetic evidence of a new flocculation suppressor gene in Saccharomyces cerevisiae (1993)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 112 (1993), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The flocculation character in strain IM1-8b of Saccharomyces cerevisiae is controlled by a single and dominant gene shown to be allelic to FLO1. Such a gene has been both mitotically and meiotically mapped on the right arm of chromosome I at 4.7 cM from PHO11. The phenotype was suppressed by a single gene of wide distribution among non-flocculent strains (proposed as fsu3) that, however, was unable to suppress other FLO1 genes in other flocculent strains.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1993.tb06418.x
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  • 6
    Electronic Resource
    Electronic Resource
    Chemical Changes and Visual Appearance of Albacore Tuna as Related to Frozen Storage (1999)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 64 (1999), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Fresh albacore tuna (Thunnus alalunga) were frozen and stored at –18°C and –25°C for 1 yr. Chemical and visual analyses were carried out at 1, 3, 6, 9 and 12 mo storage. Storage time correlated (P〈0.05) with the low loss of moisture at –18°C, slight reduction of TVBN at –25°C and low increases of DMA, TMA, and TBARS at both temperatures. TMAO concentration (p=0.07), drip loss on cooking (p=0.52), peroxide value (p=0.059), FFA concentration (p=0.33) and pH (p=0.20)did not change significantly with period of storage but −25°C resulted in a lower production of DMA and FFA than −18°C. Results from chemical analyses correlated well with basic visual appearance.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1999.tb09853.x
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  • 7
    Electronic Resource
    Electronic Resource
    Production of pectic enzymes in yeasts (1999)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 175 (1999), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: When grown in the appropriate medium, several yeast species produce pectinases able to degrade pectic substances. It is mainly exocellular endopolygalacturonases that break pectins or pectate down by hydrolysis of α-1,4-glycosidic linkages in a random way. Biochemical characterisation of these enzymes has shown that they have an optimal pH in the acidic region and an optimal temperature between 40 and 55°C. Their production by yeasts is a constitutive feature and is repressed by the glucose concentration and aeration. Pectic substances and their hydrolysis products are used as carbon sources by a limited number of yeasts and hence these enzymes must be involved in the colonisation of different parts of plants, including fruits. The first yeast pectic enzyme (encoded by the PSE3 gene) was cloned from Tichosporon penicillatum. Recently, a polygalacturonase-encoding gene from Saccharomyces cerevisiae has been cloned and overexpressed in several strains and the gene for an extracellualar endopolygalacturonase from Kluyveromyces marxianus has also been described. Taking all the results together, the idea is now emerging that this type of yeast enzyme could offer an alternative to fungal enzymes for industrial applications.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1999.tb13595.x
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  • 8
    Electronic Resource
    Electronic Resource
    Mutagenesis of key amino acids alters activity of a Saccharomyces cerevisiae endo-polygalacturonase expressed in Pichia pastoris (2002)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 210 (2002), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: A polygalacturonase (PG)-encoding gene from Saccharomyces cerevisiae (PGU1) was successfully expressed in the methylotrophic yeast Pichia pastoris. PG secretion was efficiently directed by the S. cerevisiaeα-factor signal sequence, while the native (PGU1) leader peptide was unable to direct protein export in P. pastoris. The level of PGU1 activity achieved in P. pastoris was significantly enhanced when compared to activity using the same gene in S. cerevisiae. Expression of PG proteins, engineered by site-directed mutagenesis, in P. pastoris showed that aspartic acid residues at positions 179, 200, and 201, and histidine 222 were essential for enzyme activity. Mutation of the two potential glycosylation sites in PGU1 showed that the two residues individually (N318D, N330D) did not affect secreted enzyme activity, but the double mutant caused a 50% reduction in enzyme activity when compared to the wild-type PGU1 transformant.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2002.tb11179.x
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  • 9
    Electronic Resource
    Electronic Resource
    Presence of non-supressive, M2-related dsRNAs molecules in Saccharomyces cerevisiae strains isolated from spontaneous fermentations (1999)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 181 (1999), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Total dsRNA extractions in five killer K2 strains of Saccharomyces cerevisiae isolated from spontaneous fermentations revealed the presence of a novel dsRNA fragment (which we named NS dsRNA) of approximately 1.30 kb, together with L and M2 dsRNAs. NS dsRNA appeared to be encapsidated in the same kind of viral particles as L and M2 dsRNA. Northern blot hybridization experiments indicated that NS dsRNA was derived from M2 dsRNA, likely by deletion of the internal A+U-rich region. However, unlike S dsRNAs (suppressive forms derived from M1 dsRNA in K1 killers), NS dsRNA did not induce exclusion of the parental M2 dsRNA when the host strain was maintained for up to 180 generations of growth.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1999.tb08846.x
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  • 10
    Electronic Resource
    Electronic Resource
    Curing of the killer character of Saccharomyces cerevisiae with acridine orange (1989)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 65 (1989), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Acridine orange, an intercalating dye usually employed in the curing of bacterial plasmids, was tested for its ability to cure K1 and K2 killer strains (laboratory and wine strains). The results showed a high curing percentage of the killer character. This was demonstrated by the loss of M1 or M2 dsRNAs (responsible for toxin production and resistance to it) and because the meiotic products exhibited non-Mendelian segregation. The curing percentages varied, depending on the strain but not on the killer type, and showed similar efficiency as compared with other known curing agents.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1989.tb03628.x
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