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  • Biochemistry and Biotechnology
  • 1970-1974  (501)
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  • 1
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The processing of fermentor-grown, edible yeast involves the removal of water. This can be accomplished through concentration followed by drum or spray drying. This study presents the essential physical properties of yeast solutions necessary for calculation of production economics. In addition, our initial studies of vacuum concentration show that some of the cell leakage necessary for good drying characteristics occurs. The residence time during concentration is also sufficient, to yield 1-2 log cycles of kill which are mandatory since the final product, should contain no viable cells.
    Additional Material: 1 Ill.
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  • 2
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: One important economical method for producing singlecell protein is to spray dry the cultured cells. This study presents some preliminary data on the effects of spray drying on cell viability. Under conditions similar to those for the production of spray-dried milk, 4-5 log cycles destruction occurred. The results indicate that, the activation energy for thermal destruction of yeast was reduced from the normal heat treatment value of 84 kcal/°K mole to about 38 kcal/°K mole.
    Additional Material: 1 Ill.
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 12 (1970), S. 145-154 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 3 Ill.
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 12 (1970) 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 12 (1970), S. 157-158 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 12 (1970), S. 159-166 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Streptomyces mannosidase, like the enzyme from other sources, is shown to require a divalent cation for enzyme activity. N-Ethylmaleimide pretreatment of enzyme-containing cells eliminated the requirement of aeration for enzyme activity. Methyl-α-D-mannoside was found to be a strong inhibitor of the hydrolysis of both p-nitrophenyl-α-D-mannoside and mannosidost reptomycin. The enzyme is bound at or near the surface of the cell and is inactivated by sonic oscillation. Small participate matter containing most of the activity can be released from the cells into water, such release being inhibited by phosphate, Tris, or sodium chloride.
    Additional Material: 7 Tab.
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  • 7
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 12 (1970), S. 167-178 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The possibility to use microorganisms as human food is limited by several factors. The intact cell is resistant to digestion, the cell wall is unbalanced in essential amino acids, and the nucleic acids are said to be harmful. For using single cell protein as food it may thus be necessary to disrupt the cell wall and separate the protein from nucleic acid. This paper is concerned with the production and properties of extracellular enzymes able to lyse cell walls of microorganisms. Soil bacteria and actinomycetes have been cultivated and lytic enzymes from these organisms have been used to lyse living cells of the yeast like organism E. ashbyii. Efforts were also made to use these enzymes for lysing cell of a Methanomonas sp.
    Additional Material: 7 Ill.
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  • 8
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 12 (1970), S. 179-212 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: B. subtilis NRRL B3411 neutral protease has been extensively purified by solvent, and salt fractional ion, pigment removal with DEAE-cellulose followed by chromatography on hydroxylapatite, and a final passage through a Sephadex G-100 column. The neutral protease was shown to be homogeneous by disc gel and cellulose acetate electrophoresis, gel filtration chromatography, and ultra-centrifugation. The molecular weight was determined by osmometry and ultracentrifugation to be about 38-42,000 and the amino acid composition and zinc content determined. The general properties of the enzyme, pH-activity relationship, stability, effect of inhibitors, and specificity are discussed. Comparative studies were carried out on the B. subtilis NRRL B3411 and B. subtilis var. amylosacchariticus neutral proteases and these enzymes were found to be indistinguishable by the methods used, but quite distinct from the thermostable enzyme thermolysin from B. thermoprotcolyticus.
    Additional Material: 11 Ill.
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  • 9
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 12 (1970), S. 251-271 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The amylase of Bacillus subtilis NRRL B3411 has been purified and partially characterized. The specific activity can be increased from 300,000 units/g to 6,000,000 units/g with a 60% recovery of total units. The purified material consists of one major and one trace anodic component as determined by disc gel electrophoresis. The molecular weight was 48,000 as determined by bio-gel filtration; the molecular weight was 44,900 ± 2400 as determined by sedimentation equilibrium methods. This purified enzyme is stable at, 70°C in the presence of 0.01 M Ca++ and 0.1 M NaCl over a broad pH range from 5.5-9.5. The pH activity profile indicates optimum activity at pH 6.0. This amylase exhibits maximum activity at 60°C. The enzyme is a liquefying α-amylase as determined by analysis of hydrolysis products and immunological studies.
    Additional Material: 12 Ill.
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  • 10
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 12 (1970), S. 213-249 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The alkaline proteases of B. subtilis NRRL B3411, B. pumilis, and B. licheniformis have been isolated by fractionation followed by ion exchange chromatography and their homogeneity demonstrated. General enzyme properties of the B. sublitis NRRL B3411 alkaline protease have been studied and attempts made to differentiate a group of alkaline proteases. It is clear that the alkaline proteases known as Subtilisins or Subtilopeptidases are not, exclusive to B. subtilis but are common to many Bacilli and therefore the generic name Bacillopeptidases has been proposed. It is clear too that on the basis of the effect of pH on activity, amino acid composition, esterase activity, and immunological cross-reactions the Bacillopeptidases can be divided into two groups or types: (a) Bacillopcptidase A (Subtilisin A or Subtilopeptidase A) which includes Subtilisin Carlsberg, B. licheniformis, and B. pumilis alkaline proteases; (b) Bacillopeptidase B (Subtilisin B or Subtilopeptidase B) which includes B subtilis NRRL B3411, Subtilisin Novo, Subtilisin BPN' (Nagarse), alkaline protease Daiwa Kasei, and (probably) B. subtilis var. amylosacchariticus. At present, no further differentiation is possible and whether or not the enzymes within group A or B are identical remains an open question. Methods for examination of crude enzyme mixtures or fermentation beers are described and from the examination of a number of crude enzymes and fermentation beers it appears that organisms producing Bacillopeptidase A do not produce neutral protease or amylase, while organisms producing Bacillopeptidase B produce a neutral protease and amylase as well.
    Additional Material: 12 Ill.
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