Protease susceptibility of beta-lactoglobulin adsorbed on stainless steel surface as evidence of contribution of its specific segment to adsorption.
beta-Lactoglobulin (beta-Lg) is a major constituent of fouling deposits in the dairy industry. To determine the interaction between beta-Lg and stainless steel surfaces, beta-Lg irreversibly adsorbed on stainless steel particles was subjected to lysyl endopeptidase treatment and the course of fragmentation was compared with that observed for beta-Lg in solution. The results showed a distinct difference between the courses of fragmentation: a fragment (residues 102-135) was liberated readily from beta-Lg in solution but scarcely from beta-Lg irreversibly adsorbed on stainless steel particles. This result strongly suggests that residues 102-135 include a segment primarily responsible for the interaction of beta-Lg with stainless steel surfaces. This supports our previous results [Sakiyama et al., J. Biosci. Bioeng., 88, 536-541 (1999)] that showed that residues 125-135 of beta-Lg have a strong affinity toward stainless steel surfaces and probably a major contribution to the adsorption of beta-Lg.
Sakiyama
Takaharu
T
Department of Bioscience and Biotechnology, Faculty of Engineering, Okayama University, Japan. sakiyama@s.kaiyodai.ac.jp
Aya
Atsuko
A
Embutsu
Mari
M
Imamura
Koreyoshi
K
Nakanishi
Kazuhiro
K
D000327:Adsorption; D004866:Equipment Contamination / Q000517:prevention & control*; D007782:Lactoglobulins / Q000737:chemistry*; D008422:Materials Testing; D010447:Peptide Hydrolases / Q000737:chemistry*; D011485:Protein Binding; D013193:Stainless Steel / Q000737:chemistry*
D007782:Lactoglobulins; D013193:Stainless Steel; D010447:Peptide Hydrolases