Hydrolysis of whey by whole cells of Kluyveromyces bulgaricus immobilized in calcium alginate gels and in hen egg white

1985 ◽  
Vol 22 (6) ◽  
pp. 438-441 ◽  
Author(s):  
M. Decleire ◽  
N. van Huynh ◽  
J. C. Motte ◽  
W. De Cat
Keyword(s):  
Calcium Alginate ◽  
Egg White ◽  
Whole Cells ◽  
Hen Egg White ◽  
Alginate Gels ◽  
Calcium Alginate Gels ◽  
Hydrolysis Of ◽  
Hen Egg

Hydrolysis of milk lactose by immobilized ?-galactosidase-hen egg white powder

1984 ◽  
Vol 26 (8) ◽  
pp. 901-904 ◽  
Author(s):  
Rajni Kaul ◽  
S. F. D'Souza ◽  
G. B. Nadkarni
Keyword(s):  
Egg White ◽  
White Powder ◽  
Egg White Powder ◽  
Hen Egg White ◽  
Hydrolysis Of ◽  
Hen Egg

Hydrolysis of hen egg white ovomucin

1997 ◽  
Vol 205 (5) ◽  
pp. 329-334 ◽  
Author(s):  
Sabine Moreau ◽  
Françoise Nau ◽  
Michel Piot ◽  
Catherine Guerin ◽  
Gerard Brule
Keyword(s):  
Egg White ◽  
Hen Egg White ◽  
Hydrolysis Of ◽  
Hen Egg

scholarly journals Industrial kinetic resolution of d,l-pantolactone by an immobilized whole-cell biocatalyst

RSC Advances ◽  
2021 ◽  
Vol 11 (48) ◽  
pp. 30373-30376
Author(s):  
Qiu-Hua Zhang ◽  
Liu Yang ◽  
Yi-Bin Tang ◽  
Liu-Nv Huang ◽  
Wen-Fang Luo
Keyword(s):  
Pichia Pastoris ◽  
Calcium Alginate ◽  
Kinetic Resolution ◽  
Whole Cell ◽  
Whole Cells ◽  
Whole Cell Biocatalyst ◽  
Alginate Gels ◽  
Calcium Alginate Gels ◽  
Immobilized Whole Cells

Immobilized whole-cells of Pichia pastoris harboring recombinant d-lactonase were entrapped in calcium alginate gels and used as an efficient biocatalyst for catalytic kinetic resolution of d,l-pantolactone.

scholarly journals The effects of tyrosine nitration on the structure and function of hen egg-white lysozyme

1996 ◽  
Vol 315 (2) ◽  
pp. 473-479 ◽  
Author(s):  
Paul G. RICHARDS ◽  
David J. WALTON ◽  
John HEPTINSTALL
Keyword(s):  
Cell Wall ◽  
Egg White ◽  
Structure And Function ◽  
Tyrosine Nitration ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
And Function ◽  
Hydrolysis Of ◽  
Hen Egg

We have investigated the effects of tyrosine nitration (to form the weak acid, 3-nitrotyrosine) at positions 23 or 20 plus 23, on the structure and function of hen egg-white lysozyme. Enzyme activity against Micrococcus luteus cell-wall fragments or soluble substrates exhibits two phenomena. (a) A decrease in Km and kcat for the hydrolysis of soluble oligo- and poly-saccharides, resulting in only minor changes in the catalytic efficiency (kcat/Km) upon nitration. (b) The hydrolysis of M. luteus cell-wall fragments appeared to be dominated by electrostatic interactions with the protein, giving a decrease in enzyme activity as the 3-nitrotyrosyl group became ionized. Removal of the cell-wall anionic polymer, teichuronic acid, from M. luteus abolished this effect. The 3-nitrotyrosine group was also found to act as a fluorescence quencher of exposed tryptophan residues in lysozyme.

scholarly journals Selective hydrolysis of hen egg white lysozyme at Asp-X peptide bonds promoted by oxomolybdate

2014 ◽  
Vol 136 ◽  
pp. 73-80 ◽  
Author(s):  
Karen Stroobants ◽  
Phuong Hien Ho ◽  
Eva Moelants ◽  
Paul Proost ◽  
Tatjana N. Parac-Vogt
Keyword(s):  
Egg White ◽  
Hen Egg White Lysozyme ◽  
Selective Hydrolysis ◽  
Peptide Bonds ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Hydrolysis Of ◽  
Hen Egg

Inactivation of hen egg-white lysozyme. The azide radical

1997 ◽  
Vol 94 ◽  
pp. 356-364 ◽  
Author(s):  
M Faraggi ◽  
E Bettelheim ◽  
M Weinstein
Keyword(s):  
Egg White ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Hen Egg
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