Adhesive properties of soy proteins modified by sodium dodecyl sulfate and sodium dodecylbenzene sulfonate

A study was conducted on adhesive and water-resistance properties of soy protein isolates modified by sodium dodecyl sulfate (SDS) (0.5, 1, and 3%) and sodium dodecylbenzene sulfonate (SDBS) (0.5, 1, and 3%) and applied on walnut, cherry, and pine plywoods. Soy proteins modified by 0.5 and 1% SDS showed greater shear strengths than did unmodified protein. One percent SDS modification had the highest shear strength within each wood type tested. Soy proteins modified with 0.5 and 1% SDBS also showed greater shear strengths than did the unmodified protein. The 1% SDBS-modified soy protein had the highest shear strength in all wood samples tested. Compared to the unmodified protein, the modified proteins also exhibited higher shear strengths after incubation with two cycles of alternating relative humidity and zero delamination rate and higher remaining shear strengths after three cycles of water soaking and drying. These results indicate that soy proteins modified with SDS and SDBS have enhanced water resistance as well as adhesive strength. Possible mechanisms for the effects of SDS and SDBS also are discussed.     

大豆7S与11S球蛋白尿素变性后的粘接性质研究

随着人们对环境保护意识的增加和地球有限资源的缺乏,大豆蛋白在胶粘剂工业中的应用也越来越显示出强大的吸引力,鉴于前人的研究成果,文章研究了大豆7S和11S球蛋白经过尿素变性后在松木、樱桃木和胡桃木上的粘接强度和湿润能力。结果表明在不同的木块上不同胶粘剂有不同的粘接强度和湿润性能。7S大豆蛋白尿素变性后在硬木上有较好的湿润性。1M尿素变性赋予11S蛋白的粘接强度最高,3M尿素变性后,7S蛋白在硬木上的粘接强度大于11S蛋白。蛋白质的二级结构测量表明β-折叠对于3 M尿素变性后的大豆蛋白在硬木上的粘接强度起着重要作用,而无规则卷曲是降低1 M尿素变性7S大豆蛋白粘接强度的主要因素。     

Thermal and mechanical properties of plastics molded from urea-modified soy protein isolates

Soy protein has been considered as a potential alternative of some petroleum polymers in the manufacture of plastics. The purpose of this investigation was to characterize the thermal and mechanical properties of plastics made from urea-modified soy protein. Soy protein isolate was separated from the defatted soy flour, modified with various urea concentrations, and compression-molded into plastics. Differential scanning calorimetry showed that the temperatures of denaturation and the enthalpies of denaturation of the modified soy protein decreased as urea concentrations increased above 1 M. At the same urea concentration, molded plastics made from the modified soy proteins showed a similar temperature of denaturation as the modified soy protein, but a lower enthalpy of denaturation. Tensile strength and Young's modulus of the molded plastics from the modified soy proteins increased as urea concentration increased and reached their maximum values at 8 M urea modification. Both storage modulus and glass transition temperature of the plastics from the modified soy proteins increased as urea concentration increased. The plastics made from the 2 M urea-modified soy proteins showed improvements in elongation, tough fracture behavior, and water resistance. The urea may function as a denaturant, a plasticizer, and a filler.     

Soy proteins as plywood adhesives: formulation and characterization

Soybean proteins have great potential as bio-based adhesives. The objectives of our study were to develop and characterize formaldehyde-free soybean wood adhesives with improved water resistance. Second-order response surface regression models were used to determine the effects of soy protein isolate concentration, sodium chloride, and pH on adhesive performance. All three variables affected both dry and wet strengths of bonded wood specimens. The optimum operation zone for preparing adhesives with improved water resistance is at a protein concentration of 28% and pH 5.5. Sodium chloride had negative effects on adhesive performance. Soy adhesives modified with 0.5% sodium chloride had dry strength, wet strength, and boiling strength of bonded specimens comparable to nonmodified soy adhesives. Rheological study indicated that soy adhesives exhibited shear thinning behavior. Adhesives modified with sodium chloride showed significantly lower viscosity and yield stress. Sodium chloride-modified soy adhesives formed small aggregates and had low storage moduli, suggesting reduced protein–protein interactions. These formaldehyde-free soy adhesives showed strong potential as alternatives to commercial formaldehyde-based wood adhesives.     

尿素变性对大豆分离蛋白粘接强度和分子结构的影响

大豆分离蛋白基胶粘剂由于具有环境友好性、生物降解性和可再生性而受到人们的关注。研究了尿素变性对大豆分离蛋白粘接强度及对蛋白分子结构的影响。结果表明,蛋白质经过尿素变性后,随着尿素浓度的增加,蛋白质分子展开的程度过大反而对粘接强度有不利的影响。在对榉木进行粘接时,1mol/L尿素变性获得的粘接强度最大。     

Shear strength and water resistance of modified soy protein adhesives

Soy protein polymers recently have been considered as alternatives to petroleum polymers to ease environmental pollution. The use of soy proteins as adhesives for plywood has been limited because of their low water resistance. The objective of this research was to test the water resistance of adhesives containing modified soy proteins in walnut, maple, poplar, and pine plywood applications. Gluing strength and water resistance of wood were tested by using two ASTM standard methods. Glues with modified soy proteins had stronger bond strength than those containing unmodified soy proteins. Plywood made with glue containing urea-modified proteins had higher water resistance than those bonded with glues containing alkali-modified and heat-treated proteins. After three 48-h cycles of water-soaking, followed by 48 h of air-drying, no delamination was observed for either walnut or pine specimens glued with the urea-modified soy protein adhesives. Gluing strength for wood species with smooth and oriented surface structure was lower than for those with rough, randomly oriented, surface structures. Wood species with greater expansion of dimensions during water-soaking had a higher delamination rate than those showing less expansion.     

Urea-Modified Soy Globulin Proteins (7S and 11S): Effect of Wettability and Secondary Structure on Adhesion

This investigation characterized wettability and adhesive properties of the major soy protein components conglycinin (7S) and glycinin (11S) after urea modification. Modified 7S and 11S soy proteins were evaluated for gluing strength with pine, walnut, and cherry plywood and for wettability using a bubble shape analyzer. The results showed that different adhesives had varying degrees of wettability on the wood specimens. The 7S soy protein modified with urea had better wettability on cherry and walnut. The 11S soy protein modified with 1M urea had better wettability on pine. The 1M urea modification gave 11S soy protein the greatest bonding strength in all the wood specimens. The 3M urea modification gave 7S soy protein stronger adhesion on cherry and walnut than did 11S protein; but with pine, 11S soy protein had greater adhesion strength than 7S soy protein. Measurement of protein secondary structures indicated that the β-sheet played an important role in the adhesion strength of 3M urea-modified soy protein in cherry and walnut, while random coil was the major factor reducing adhesion strength of 7S soy protein modified with 1M urea.     

Soy protein adhesion enhanced by glutaraldehyde crosslink

Soy protein has been considered as an alternative to partly replace petroleum‐based polymers for adhesive applications. The weakness of protein‐based adhesive is poor water resistance, which limits its outdoor applications. The objective of this research was to improve the water resistance of soy protein adhesive by introducing crosslinkage between amino groups of amino acid residue. Laboratory prepared soy protein isolate (SPI) was used in this study. Glutaraldehyde at concentrations of 4, 20, 40, and 80 μM was used as the crosslinking reagent for SPI modification. Adhesive properties of soy protein modified by glutaraldehyde, as well as thermal and morphological properties, were investigated. Crosslinking‐induced protein conformation and structure changes through decrease of amino groups and adding of hydrophobic groups, subsequently affect adhesive performance of SPI. At optimum glutaraldehyde concentration (20 μM), dry, wet, and soak strengths of modified SPI increased to 31.5, 115, and 29.7%, respectively, compared with unmodified SPI. © 2007 Wiley Periodicals, Inc. J Appl Polym Sci 104: 130–136, 2007     

Modification of soy proteins and their adhesive properties on woods

Adhesive properties of trypsin-modified soy proteins (TMSP) on woods were investigated. A simple method developed in our laboratory, consisting of measuring the force required to shear the bond between glued wood pieces in the Instron universal testing machine, was used to examine adhesive strength of modified soy proteins on wood. Adhesive strength of TMSP was measured for cold-pressed (ambient temperature for 2 h) and hot-pressed (60, 80, 100, and 120°C for times varying from 0.5 to 2.5 h) woods. Of the woods examined, soft maple gave the highest strength [743 Newtons (N) at a protein glue concentration of 2 mg/cm²]. For soft maple and cold-pressing, TMSP at 2 mg/cm² gave twice the adhesive strength of unmodified protein controls, 743 vs. 340 N. Also, the adhesive strength of TMSP increased from 284 to 743 N as glue concentration was increased from 1 to 2 mg/cm². However, hot-pressing of wood pieces beyond 1 h at 120°C and 30% relative humidity resulted in decreased adhesive strengths of TMSP compared to controls. Further, adhesive strengths of hot-pressed glued wood samples decreased when the relative humidity at which they were kept for curing increased from 30 to 60%. This negative effect of increased humidity on adhesive strengths of glued wood pieces was not observed with cold-pressed TMSP.     

Thermal properties and adhesion strength of modified soybean storage proteins

Soy proteins have shown great potential for adhesive and resin applications. This investigation characterized the thermal and adhesive properties of the major soy protein components conglycinin (7S) and glycinin (11S) after chemical modification. These globulins were extracted from defatted soy flour, then modified with either sodium hydroxide, sodium dodecyl sulfate (SDS), or urea. Modified 7S, 11S, and mixtures of 7S and 11S at varying ratios were evaluated for gluing strength with cherry veneer plywood and for thermal denaturation using DSC. Adhesive strength and water resistance were significantly improved for all proteins modified with sodium hydroxide. Gluing strength and water resistance were improved for SDS- and ureamodified proteins containing greater portions of 7S globulins. The opposite behavior was observed for proteins containing large amounts of 11S globulins. DSC results showed that the temperatures of denaturation (T _d ) decreased for the proteins modified with sodium hydroxide or urea, whereas the T _d values of proteins modified with SDS were similar to the unmodified proteins. These results suggested that, at the concentrations studied, sodium hydroxide or urea could denature soybean protein more effectively than SDS, resulting in lower protein thermal stability. Soybean proteins with high ratios of 11S had more ordered structures, as evidenced by the high enthalpy values of protein denaturation observed in DSC measurements.