S. Visser

发表

Specificity of a cell-envelope-located proteinase (PIII-type) from Lactococcus lactis subsp. cremoris AM1 in its action on bovine β-casein

S. Visser, A. Robben, C. Slangen, 1991, Applied Microbiology and Biotechnology.

Peptide substrates for chymosin (rennin). Isolation and substrate behaviour of two tryptic fragments of bovine kappa casein.

S. Visser, C. Slangen, P. J. VAN ROOIJEN, 1980, European journal of biochemistry.

Characterization of the anti-HIV effects of native lactoferrin and other milk proteins and protein-derived peptides.

B. Berkhout, D. Meijer, L. Beljaars, 2002, Antiviral research.

The antiviral activity of the milk protein lactoferrin against the human immunodeficiency virus type 1

B. Berkhout, I. Recio, S. Visser, 2004, Biometals.

Phenotyping of bovine milk proteins by reversed-phase high-performance liquid chromatography.

S. Visser, C. Slangen, H. Rollema, 1991, Journal of chromatography.

Action of a cell-envelope proteinase (CEPIII-type) from Lactococcus lactis subsp. cremoris AM1 on bovine κ-casein

S. Visser, A. Robben, C. Slangen, 1994, Applied Microbiology and Biotechnology.

Preparation and characterization of monoclonal antibodies directed against bovine β-casein

P. Oudshoorn, G. Simons, S. Visser, 1994 .

Partial purification and characterization of two aminotransferases from Lactococcus lactis subsp. cremoris B78 involved in the catabolism of methionine and branched-chain amino acids

H. Gruppen, G. Smit, A. Alting, 2000 .

Spectrophotometric assay of plasmin and plasminogen in bovine milk.

S. Visser, H. Rollema, J. Poll, 1983 .

Proteolytic Enzymes and Their Relation to Cheese Ripening and Flavor: An Overview

S. Visser, 1993 .

[Specificity of bovine plasmin in its action on bovine alfa s2-casein]

S. Visser, K. J. Slangen, A. C. Alting, 1989 .

Peptide substrates for chymosin (rennin). Kinetic studies with peptides of different chain length including parts of the sequence 101-112 of bovine k-casein.

S. Visser, K. Kerling, P. J. VAN ROOIJEN, 1976, Biochimica et biophysica acta.

A study of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Improved purification, relative molecular mass, and amino acid composition.

W. V. van Berkel, G. Voordouw, S. Visser, 1979, European journal of biochemistry.

Identification of a new genetic variant of bovine beta-casein using reversed-phase high-performance liquid chromatography and mass spectrometric analysis.

W. V. van Dongen, S. Visser, C. Slangen, 1995, Journal of chromatography. A.

Reversed-phase high-performance liquid chromatographic separation of bovine kappa-casein macropeptide and characterization of isolated fractions.

S. Visser, C. Slangen, J. Haverkamp, 1996, Journal of chromatography. A.

Determination of molecular mass distributions of whey protein hydrolysates by high-performance size-exclusion chromatography

S. Visser, A. Robben, C. Slangen, 1992 .

Antibacterial and binding characteristics of bovine, ovine and caprine lactoferrins : a comparative study

I. Recio, S. Visser, 2000 .

Studies on polypeptides. Part IX: Combination of solid‐phase and classical methods of peptide synthesis in the preparation of 1‐13[13‐Leucine] bovine pancreatic ribonuclease

E. Havinga, S. Visser, K. Kerling, 2010 .

Method for the isolation of bovine β-lactoglobulin from a cheese whey protein fraction and physicochemical characterization of the purified product

H. Gruppen, S. Visser, P. Caessens, 1997 .

Peptide substrates for chymosin (rennin): Conformational studies of κ-casein and some κ-casein-related oligopeptides by circular dichroism and secondary structure prediction

S. Visser, K. Kerling, J. Raap, 1983 .

Isolation and characterization of beta- and gamma-caseins from horse milk.

R. Jenness, S. Visser, R. Mullin, 1982, The Biochemical journal.

Two ion-exchange chromatographic methods for the isolation of antibacterial peptides from lactoferrin. In situ enzymatic hydrolysis on an ion-exchange membrane.

I. Recio, S. Visser, 1999, Journal of chromatography. A.

Bitter flavour in cheese. 2. Model studies on the formation and degradation of bitter peptides by proteolytic enzymes from calf rennet, starter cells and starter cell fractions

S. Visser, 1983 .

Proteoloytic enzymes and their action on milk proteins

S. Visser, 1981 .

Antibacterial and antiviral effects of milk proteins and derivatives thereof.

B. Berkhout, I. Recio, S. Visser, 2003, Current pharmaceutical design.

Identification of two distinct antibacterial domains within the sequence of bovine alpha(s2)-casein.

I. Recio, S. Visser, 1999, Biochimica et biophysica acta.

Characterization of bovine kappa-casein fractions and the kinetics of chymosin-induced macropeptide release from carbohydrate-free and carbohydrate-containing fractions determined by high-performance gel-permeation chromatography.

S. Visser, C. Slangen, J. V. van Riel, 1986, The Biochemical journal.

A comparative study of volatile compounds in the water-soluble fraction of various types of ripened cheese

C. D. Jong, R. Dekker, S. Visser, 1997 .

Use of Mass Spectrometry To Rapidly Characterize the Heterogeneity of Bovine α-Lactalbumin

S. Visser, C. Slangen, 1999 .

Identification of peptides obtained via hydrolysis of bovine casein by chymosin using HPLC and mass spectrometry.

P. Minkiewicz, J. Dziuba, S. Visser, 2000 .

Isolation and comparative characterization of components that contribute to the flavour of different types of cheese

S. Visser, W. Engels, 1994 .

Development of cheese flavour from peptides and amino acids by cell-free extracts of Lactococcus lactis subsp. cremoris B78 in a model system

S. Visser, W. Engels, 1996 .

On the specificity of chymosin (rennin) in its action on bovine beta-casein

S. Visser, K. J. Slangen, 1977 .

Is bovine β-casein G a true genetic variant?

S. Visser, 2000 .

Determination of milk proteins by capillary electrophoresis.

S. Visser, N. de Jong, C. Olieman, 1993, Journal of chromatography. A.

beta-lactoglobulin hydrolysis. 2. Peptide identification, SH/SS exchange, and functional properties of hydrolysate fractions formed by the action of plasmin.

H. Gruppen, A. Voragen, W. Daamen, 1999, Journal of agricultural and food chemistry.

High-performance liquid chromatography of bovine caseins with the application of various stationary phases

S. Visser, H. Rollema, K. J. Slangen, 1986 .

Action of plasmin on bovine β-casein in a membrane reactor

H. Noorman, S. Visser, C. Slangen, 1989, Journal of Dairy Research.

Plasmin Hydrolysis of β-Casein: Foaming and Emulsifying Properties of the Fractionated Hydrolysate

H. Gruppen, G. V. Aken, A. Voragen, 1997 .

Functionality of beta-casein peptides: importance of amphipathicity for emulsion-stabilizing properties.

H. Gruppen, A. Voragen, S. Visser, 1999, Journal of agricultural and food chemistry.

Some bitter peptides from rennet-treated casein. A method for their purification, utilizing chromatographic separation on silica gel

S. Visser, G. Hup, K. J. Slangen, 1975 .

beta-lactoglobulin hydrolysis. 1. Peptide composition and functional properties of hydrolysates obtained by the action of plasmin, trypsin, and Staphylococcus aureus V8 protease.

H. Gruppen, A. Voragen, S. Visser, 1999, Journal of agricultural and food chemistry.

Method for the production of antibacterial peptides from biological fluids at an ionic membrane. Application to the isolation of nisin and caprine lactoferricin

I. Recio, S. Visser, C. Slangen, 2000 .

Comparative Study of Action of Cell Wall Proteinases from Various Strains of Streptococcus cremoris on Bovine αs1-, β-, and κ-Casein

S. Visser, C. Slangen, F. Exterkate, 1986 .

Quantification of chymosin action on nonlabeled kappa-casein-related peptide substrates by ultraviolet spectrophotometry: description of kinetics by the analysis of progress curves.

S. Visser, H. Rollema, 1986, Analytical biochemistry.

Peptide substrates for chymosin (rennin). Kinetic studies with bovine kappa-casein-(103-108)-hexapeptide analogues.

S. Visser, K. Kerling, P. J. VAN ROOIJEN, 1977, Biochimica et biophysica acta.

Action of a cell wall proteinase (PI) from Streptococcus cremoris HP on bovine β-casein

S. Visser, C. Slangen, F. Exterkate, 1988, Applied Microbiology and Biotechnology.

Peptide substrates for chymosin (rennin). Interaction sites in kappa-casein-related sequences located outside the (103-108)-hexapeptide region that fits into the enzyme's active-site cleft.

S. Visser, C. Slangen, P. J. VAN ROOIJEN, 1987, The Biochemical journal.

Studies on polypeptides. Part X: Synthesis of 1‐13[10‐Homoarginine, 13‐Leucine] bovine pancreatic ribonuclease by combined solid‐phase and classical methods

E. Havinga, S. Visser, K. Kerling, 2010 .

Studies on polypeptides VI: Synthesis of protected hexa‐ and octa‐peptide hydrazides related to the N‐terminal part of bovine pancreatic ribonuclease a using the solid‐phase method

E. Havinga, S. Visser, K. Kerling, 2010 .

Studies on polypeptides. Part XI: Fragment condensation by azide coupling with a polymer‐bound peptide. The synthesis of 1‐13[10‐Citrulline, 13‐Leucine] bovine pancreatic ribonuclease

S. Visser, K. Kerling, 2010 .