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Cultivation ofCandida blankii in simulated bagasse hemicellulose hydrolysate (1992)

Meyer, Petrus S. ; Preez, James C. ; Kilian, Stephanus G.

Springer

Journal of industrial microbiology and biotechnology 9 (1992), S. 109-113

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ISSN: 1476-5535

Keywords: Candida blankii ; Biomass ; d-Xylose ; l-Arabinose ; Acetate

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology

Notes: Summary All fourCandida blankii isolates evaluated for growth in simulated bagasse hemicellulose hydrolysate utilized the sugars and acetic acid completely. The utilization ofd-xylose,l-arabinose and acetic acid were delayed by the presence ofd-glucose, but after glucose depletion the other carbon sources were utilized simultaneously. The maximum specific growth rate of 0.36 h−1 and cell yield of 0.47 g cells/g carbon source assimilate compared with published results obtained withC. utilis. C. blankii appeared superior toC. utilis for biomass production from hemicellulose hydrolysate in that it utilizedl-arabinose and was capable of growth at higher temperatures.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF01569741

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Michaelis complexes of porcine pancreatic elastase with 7-[(alkylcarbamoyl)amino]-4-chloro-3-ethoxyisocoumarins: Translational sampling of inhibitor position and kinetic measurements (1992)

Plaskon, R. Richard ; Kam, Chih-Min ; Burgess, Edward M. ; [et al.]

New York, NY : Wiley-Blackwell

Proteins: Structure, Function, and Genetics 13 (1992), S. 141-151

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ISSN: 0887-3585

Keywords: serine protease ; MNDO Hamiltonian ; SCF charges ; energy minimization ; dissociation constant ; inhibitor design ; catalytic mechanism ; Chemistry ; Biochemistry and Biotechnology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Medicine

Notes: A step leading to the formation of the covalent complexes between porcine pancreatic elastase (PPE) and 7-[(alkylcarbamoyl)amino]-4-chloro-3-ethoxyisocoumarins (alkylHNCO-EICs) is the formation of the non-covalent Michaelis complex. No average structures are available for the Michaelis complexes of PPE with alkylHNCO-EICs. We present the results of an initial step in obtaining these structures and have determined kinetic constants as well. The kinetic results indicate that formation of the Michaelis complex is what differentiates the effectiveness of these inhibitors in inactivating PPE. The structural and kinetic results together suggest that the structure of the Michaelis complex is necessary for the design of potent alkylHNCO-EIC inhibitors of PPE. Two novel alkylHNCO-EICs are predicted to be the best inhibitors of this series. An alternate mechanism for serine protease inhibition is also proposed. Evidence for, and studies that may add support to, the hypothesized mechanism are discussed. © 1992 Wiley-Liss, Inc.

Additional Material: 7 Ill.