%0 Journal Article %1 Neiser1999 %A Neiser, S. %A Draget, K. I. %A Smidsrod, O. %C THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLAND %D 1999 %I ELSEVIER SCI LTD %J Food Hydrocolloids %K ; ;; BSA [ISI:] alginate; beef binding gel-gel gels; interactions; multicomponent protein-polysaccharide proteins; steaks; structured %N 6 %P 445 -- 458 %T Interactions in bovine serum albumin-calcium alginate gel systems %V 13 %X Young's modulus of heat-denatured gels of calcium alginate and bovine serum albumin (BSA) was determined and compared to the modulus of BSA gels containing sodium alginate and to pure BSA gels. Ionic strength, pH, and calcium concentration were varied. The BSA Ca-alginate gels were either prepared with D-glucono-delta-lactone (GDL) and CaCO3 to induce alginate gelation before the gelation of BSA, or by soaking heat-denatured BSA/Na-alginate gels in a CaCl2 solution. BSA/Ca-alginate gels were stronger than BSA/Na-alginate gels at all conditions, and stronger than pure BSA gels up to higher pH values and up to somewhat higher ionic strengths than BSA/Na-alginate gels. The strength of BSA/Ca-alginate gels was highly dependent on the strength of the alginate gel. This was shown by variation of the calcium concentration and by soaking the gels in EDTA, NaCl, and CaCl2 solutions. When BSA/Na-alginate or BSA/Ca-alginate gels prepared at optimum conditions were soaked in solutions of higher ionic strength or pH, no reduction in gel strength was observed. Consequently, they were much stronger than gels that were prepared directly at high pH or ionic strength. The results may suggest that the alginate network in a BSA/Ca-alginate gel increases the effectiveness of electrostatic BSA-alginate cross-links or entanglements. However, other explanations are also possible. (C) 1999 Elsevier Science Ltd. All rights reserved.

@article{Neiser1999, __markedentry = {[phpts:6]}, abstract = {Young's modulus of heat-denatured gels of calcium alginate and bovine serum albumin (BSA) was determined and compared to the modulus of BSA gels containing sodium alginate and to pure BSA gels. Ionic strength, pH, and calcium concentration were varied. The BSA Ca-alginate gels were either prepared with D-glucono-delta-lactone (GDL) and CaCO3 to induce alginate gelation before the gelation of BSA, or by soaking heat-denatured BSA/Na-alginate gels in a CaCl2 solution. BSA/Ca-alginate gels were stronger than BSA/Na-alginate gels at all conditions, and stronger than pure BSA gels up to higher pH values and up to somewhat higher ionic strengths than BSA/Na-alginate gels. The strength of BSA/Ca-alginate gels was highly dependent on the strength of the alginate gel. This was shown by variation of the calcium concentration and by soaking the gels in EDTA, NaCl, and CaCl2 solutions. When BSA/Na-alginate or BSA/Ca-alginate gels prepared at optimum conditions were soaked in solutions of higher ionic strength or pH, no reduction in gel strength was observed. Consequently, they were much stronger than gels that were prepared directly at high pH or ionic strength. The results may suggest that the alginate network in a BSA/Ca-alginate gel increases the effectiveness of electrostatic BSA-alginate cross-links or entanglements. However, other explanations are also possible. (C) 1999 Elsevier Science Ltd. All rights reserved.}, added-at = {2011-11-04T13:47:04.000+0100}, address = {THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, OXON, ENGLAND}, author = {Neiser, S. and Draget, K. I. and Smidsrod, O.}, authoraddress = {Norwegian Univ Sci & Technol, Dept Biotechnol, Norwegian Biopolymer Lab, N-7491 Trondheim, Norway.}, biburl = {https://www.bibsonomy.org/bibtex/22c991ad24642b0eea5a7edbe8cfed7e2/pawelsikorski}, citedref = {ANDRESEN IL, 1977, CARBOHYD RES, V58, P271 ; CAI R, 1997, J FOOD SCI, V62, P1129 ; CLARK AH, 1986, FUNCTIONAL PROPERTIE, P203 ; CLARK AH, 1995, BIOPOLYMER MIXTURES, P37 ; CLARK AK, 1982, PROGR FOOD NUTRIT SC, V6, P149 ; CLARKE AD, 1988, J FOOD SCI, V53, P1266 ; DEJONG HGB, 1949, COLLOID SCI, V2, P232 ; DRAGET KI, 1989, APPL MICROBIOL BIOT, V31, P79 ; DRAGET KI, 1991, CARBOHYD POLYM, V14, P159 ; DRAGET KI, 1993, HYDROBIOLOGIA, V261, P563 ; DRAGET KI, 1998, CARBOHYD POLYM, V35, P1 ; EVENSON MA, 1978, CLIN CHIM ACTA, V89, P341 ; FLORY PJ, 1944, CHEM REV, V35, P51 ; GRASDALEN H, 1983, CARBOHYD RES, V118, P255 ; IMESON AP, 1977, J SCI FOOD AGR, V28, P661 ; MARTINSEN A, 1989, BIOTECHNOL BIOENG, V33, P79 ; MARTINSEN A, 1991, CARBOHYD POLYM, V15, P171 ; MEANS WJ, 1986, J FOOD SCI, V51, P60 ; MEANS WJ, 1987, J FOOD SCI, V52, P252 ; MORRISSEY PA, 1992, BIOCH FOOD PROTEINS, P125 ; NEISER S, 1998, FOOD HYDROCOLLOID, V12, P127 ; PARK JM, 1992, MACROMOLECULES, V25, P290 ; PETERS T, 1985, ADV PROTEIN CHEM, V37, P161 ; PICULELL L, 1992, ADV COLLOID INTERFAC, V41, P149 ; PICULELL L, 1994, GUMS STABILISERS FOO, V7, P309 ; PICULELL L, 1995, BIOPOLYMER MIXTURES, P13 ; RICHARDSON RK, 1981, BRIT POLYM J, V13, P11 ; SCHMIDT GR, 1986, 4603054, US ; SHIMADA K, 1981, J AGR FOOD CHEM, V29, P15 ; SKJAKBRAEK G, 1986, INT J BIOL MACROMOL, V8, P330 ; SMIDSROD O, 1965, ACTA CHEM SCAND, V19, P329 ; SMIDSROD O, 1972, ACTA CHEM SCAND, V26, P71 ; STADING M, 1992, FOOD HYDROCOLLOID, V6, P455 ; STEINER AB, 1948, 2441729, US ; TANFORD C, 1955, J AM CHEM SOC, V77, P6414 ; TANFORD C, 1956, J PHYS CHEM-US, V60, P225 ; TOLSTOGUZOV VB, 1983, J TEXTURE STUD, V14, P183 ; TOLSTOGUZOV VB, 1986, FUNCTIONAL PROPERTIE, P385 ; TOLSTOGUZOV VB, 1995, FOOD HYDROCOLLOID, V9, P317 ; TRELOAR LRG, 1975, PHYSICS RUBBER ELAST ; TROUT GR, 1989, MEAT SCI, V25, P163 ; YASUDA K, 1986, J FOOD SCI, V51, P1289}, interhash = {2f5ebfeffbc4f57dacf027d780bb1f10}, intrahash = {2c991ad24642b0eea5a7edbe8cfed7e2}, isifile-dt = {Article}, isifile-ga = {258EG}, isifile-j9 = {FOOD HYDROCOLLOID}, isifile-nr = {42}, isifile-pi = {OXFORD}, isifile-rp = {Smidsrod, O, Norwegian Univ Sci & Technol, Dept Biotechnol, Norwegian ; Biopolymer Lab, Sem Saelands Vei 6-8, N-7491 Trondheim, Norway.}, isifile-sc = {Chemistry, Applied; Food Science & Technology}, isifile-tc = {5}, issn = {0268-005X}, journal = {Food Hydrocolloids}, keywords = {; ;; BSA [ISI:] alginate; beef binding gel-gel gels; interactions; multicomponent protein-polysaccharide proteins; steaks; structured}, language = {English}, month = NOV, number = 6, owner = {phpts}, pages = {445 -- 458}, publisher = {ELSEVIER SCI LTD}, size = {14 p.}, sourceid = {ISI:000083824700002}, timestamp = {2011-11-04T13:47:18.000+0100}, title = {Interactions in bovine serum albumin-calcium alginate gel systems}, volume = 13, year = 1999 }