物理预处理—蛋白酶控制水解联合改性对大豆分离蛋白功能特性的影响研究
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摘要
大豆蛋白由于产量高、营养丰富、价格便宜而受到了广泛的关注,但其功能特性较差,严重限制了其在食品中的应用。本论文研究了双螺杆挤压和超声波两种物理预处理手段对SPI酶解过程和酶解产物功能特性的影响,然后进一步研究改性产物的理化性质、界面性质和结构,着眼于形成大豆蛋白质改性的新方法,期望发现“加工方法—结构变化—功能特性”之间的关系,为功能性大豆蛋白系列产品的开发提供理论和方法的指导。
研究了不同温度的挤压预处理对SPI酶解过程和酶解产物功能特性的影响。结果发现与SPI相比,ESPIH-120?160℃对Pan和Pap的酶解敏感性都增强了,其中ESPI-140℃的酶解敏感性最好。挤压预处理-蛋白酶水解联合改性可以显著改善SPI的PR,效果比单纯酶解改性好。ESPIH-140℃-Pan的PR在一定DH范围内(DH=8.0–10.0%)达到90%左右,且其NSI值在pH=3?11范围内具有较好的稳定性。ESPIH-140℃-Pap的最大PR值为80.6%,但NSI值在等电点(pH=4.5)附近明显下降。挤压预处理-蛋白酶水解联合改性不能改善SPI的热诱导凝胶性能。在本论文中,制备乳状液(20% v/v葵花籽油,pH=7.0)的乳化剂浓度为1.6%(w/v),在此条件下SPI形成的乳状液具有较大的平均粒径(d43≈30.9μm)。挤压预处理-Pan酶解联合改性能够显著改善SPI的乳化能力,效果比单纯Pan酶解改性好。其中ESPIH-140℃-Pan在DH=8.0?9.1%时制备的乳状液的平均粒径(d43=2.0μm)为所有样品中最小。而挤压预处理-Pap酶解联合改性不能改善SPI的乳化能力。
ESPI-140℃对Pan的敏感性提高,酶解变得强烈而广泛,使酶解产物的水解度(DH)、氮溶指数(NSI)、分子量分布、表面疏水性(H0)和二级结构都发生了显著的变化。在本论文所采用的条件下,SPI和SPIH-Pan制备的乳状液在均质过程中发生了桥联絮凝,在21天的静置贮存期间内出现了乳析;而ESPIH-140℃-Pan-9.1%能够制备出粒径细小的乳状液,该乳状液在贮存期间具有良好的对抗乳析和液滴聚集的稳定性。与对照SPI和SPIH-Pan-1.0%相比,ESPIH-140℃-Pan-9.1%界面活性较低;但具有较高的Fad(s67.6%)和较小的Гsat(2.8 mg/m2)。SPIH-Pan乳状液和ESPIH-140℃-Pan乳状液的|ζ|-电势都大于25 mV,具有良好的静电排斥效果。蛋白溶解性显著提高和分子柔性的增大是ESPIH-140℃-Pan-9.1%乳化能力改善的主要原因。
研究了不同功率的超声预处理对SPI酶解过程和酶解产物功能特性的影响。结果发现超声预处理能够使分散液中蛋白颗粒粒径减小。与SPI相比,USPI-200?600W对Pan和Pap的酶解敏感性都增强了,其中USPI-400W和USPI-600W的酶解敏感性较好。超声预处理-蛋白酶水解联合改性可以显著改善SPI的PR,效果比单纯酶解改性好。USPIH-400W-Pan-11.8%和USPIH-400W-Pap-2.9%的PR值分别为84.7%和86.1%,在中性和碱性条件下具有较高的NSI值;在酸性条件下,NSI值会显著下降。USPIH-400W-Pap-2.9%的等电点向酸性方向偏移,位于pH 3?4。超声预处理-蛋白酶水解联合改性对SPI热诱导凝胶性能的改善效果与单纯酶解改性效果相当。超声预处理-蛋白酶水解联合改性可以显著改善SPI的乳化能力,效果比单纯酶解改性好。USPIH-400W-Pap-1.3%制备的乳状液的平均粒径(d43=7.2μm)为所有USPIH乳状液中最小。
SPIH-Pap制备的乳状液在均质过程中发生了桥联絮凝,在21天的静置贮存期间内出现了乳析。而USPIH-400W-Pap乳化能力和乳析稳定性明显改善。与SPI和SPIH-Pap-0.6%相比,USPIH-400W-Pap-1.3%能够在较低的浓度下(3.0% w/v)制备出粒径细小且稳定的乳状液(d43 = 1.8μm)。SPIH-Pap乳状液和USPIH-400W-Pap乳状液的|ζ|-电势都大于25 mV,具有良好的静电排斥效果。超声预处理(400W)后,α-7S和A-11S的酶解敏感性提高,大豆蛋白中不同亚基的酶解变的迅速而协调,使USPIH-400W-Pap在一定DH范围内既具有良好的溶解性,又具有较高的H0,说明生成了许多具有界面活性的可溶性蛋白或肽,因此具有良好的乳化性能。
The use of soy proteins has been of increased interest, primarily attributed to its steady supply, high nutritional and low cost. However, the poor functional properties have limited the application of soy protein isolates (SPI) in food industry. Effects of two physical pre-treatment, twin-screw extrusion and power ultrasound, on the enzymatic hydrolysis and hydrolysates functional properties of SPI have been investigated. Various physicochemical properties, surface properties and secondary structural of modified SPI have also been studied in relation to DH and functional properties. The aim of this paper was to explore new methods for functionality modification of soy proteins, and by study the relationship between“processing method structure characteristics ? good functionalities”, the underpinning mechanisms of improved functionalities for modified SPI can be clarified, which can give academic and practical guide for the processing of soy protein product.
Effects of extrusion pre-treatment with different temperature (120℃, 140℃,160℃) on the enzymatic hydrolysis and functional properties of soy protein isolates (SPI) have been investigated. Results showed that comparing with SPI, the accessibility of the different extrusion pre-treated SPI (ESPI-120?160℃) was improved marked, with the ESPI-140℃showed the best performance. Combined modification of extrusion-enzymatic hydrolysis can markedly improve the protein recovery (PR) of SPI, which showed a much better effect than that of enzymatic hydrolysis alone. ESPIH-140℃-Pan (ESPI hydrolysate-140℃-Pan) had a PR of ca. 90% in the range of DH=8.0–10.0%, and exhibited a stable nitrogen solubility index (NSI) value among pH=3?11. The highest PR of ESPIH-140℃-Pap was 80.6%, but the NSI will decrease markedly around iso-electric point (pH=4.5). Combined modification of extrusion-enzymatic hydrolysis can not improve the heat-induced gelation properties of SPI. In this paper, the emulsifier concentration selected to make emulsions was set to be 1.6% (w/v), and the emulsion formed by SPI at this concentration had a large mean diameter (d43≈30.9μm). Extrusion-Pan hydrolysis can marked improved the emulsifying capability of SPI, with much better effect than that of enzymatic hydrolysis alone. Emulsions formed by ESPIH-140℃-Pan with DH=8.0?9.1% showed a smallest d43 (2.0μm) among all the sample emulsions. However, Extrusion-Pap hydrolysis can not improve the emulsifying capability of SPI.
Extrusion pre-treatment caused a marked improvement in the accessibility of SPI to Pan-hydrolysis, resulting in changes in degree of hydrolysis (DH), protein solubility (PS), surface hydrophobicity (H0) and molecular weight distributions (MWD) for ESPIH-140℃-Pan. It was observed that emulsion systems formed by control SPI or SPIH-Pan were unstable over a quiescent storage period of 21days, due to bridging flocculation and creaming. However, ESPIH-140℃-Pan-9.1% was capable of producing a very fine emulsion (d43 = 2.01μm) which remained stable over a long term quiescent storage. As compared with control SPI and SPIH-Pan-1.0%, ESPIH-140℃-Pan-9.1% appeared to be less surface active, but had a much higher Fads (67.6%) and a significantly lowerГsat (2.8 mg/m2). The |ζ|-potential of all SPIH-Pan and ESPIH-140℃-Pan were larger than 25 mV, which showed substantial electrostatic repulsion. It was suggested that significantly increased protein solubility and molecular flexibility could be the main reasons for the greatly improved emulsifying capability of ESPIH-140℃-Pan-9.1%.
Effects of ultrasound pre-treatment with different power (200W, 400W, 600W) on the enzymatic hydrolysis and functional properties of SPI have been investigated. Results showed that comparing with SPI, the accessibility of the different ultrasound pre-treated SPI (USPI-200?600W) was improved marked, with the USPI-400W showed the best performance. Combined modification of ultrasound-enzymatic hydrolysis can markedly improve the PR of SPI, which showed a better effect than that of enzymatic hydrolysis alone. USPIH-400W-Pan-11.8% and USPIH-400W-Pap-2.9% had PR of 84.7% and 86.1% respectively. Their NSI increased slightly in basic conditions but decreased markedly at acidic conditions. The iso-electric point of USPIH-400W-Pap-2.9% showed a shift to pH 3?4. Combined modification of Ultrasound-enzymatic hydrolysis exhibited a equivalent improvement on heat-induced gelation properties of SPI to that of enzymatic hydrolysis alone. Ultrasound-enzymatic hydrolysis can marked improved the emulsifying capability of SPI, with much better effect than that of enzymatic hydrolysis alone. Emulsions formed by USPIH-400W-Pap-1.3% showed a smallest d43 (7.2μm) among all the USPIH emulsions.
Emulsion formed by SPIH-Pap became unstable over a quiescent storage of 21 days, due to bridging flocculation and creaming. In contrast, USPIH-400W-Pap exhibited much better emulsifying capability and creaming stability under similar conditions. And as compared with control SPI and SPIH-Pap-0.6%, USPIH-400W-Pap-1.3% was capable of forming stable emulsions with small droplet sizes (d43 = 1.8μm) and at a much lower protein concentration (3.0% w/v). The |ζ|-potential of all SPI-Pap and USPIH-400W-Pap were larger than 25 mV, which showed substantial electrostatic repulsion. After ultrasound pre-treatment, the accessibility ofα-7S and A-11S was improved, and the enzymatic hydrolysis of USPI-400W became fast and harmonious. In some DH range, not only USPIH-400W-Pap had good protein solubility, but also had high H0, which indicated that a lot of surface active proteins or peptides were created. As a result, emulsifying capability was improved.
研究了不同温度的挤压预处理对SPI酶解过程和酶解产物功能特性的影响。结果发现与SPI相比,ESPIH-120?160℃对Pan和Pap的酶解敏感性都增强了,其中ESPI-140℃的酶解敏感性最好。挤压预处理-蛋白酶水解联合改性可以显著改善SPI的PR,效果比单纯酶解改性好。ESPIH-140℃-Pan的PR在一定DH范围内(DH=8.0–10.0%)达到90%左右,且其NSI值在pH=3?11范围内具有较好的稳定性。ESPIH-140℃-Pap的最大PR值为80.6%,但NSI值在等电点(pH=4.5)附近明显下降。挤压预处理-蛋白酶水解联合改性不能改善SPI的热诱导凝胶性能。在本论文中,制备乳状液(20% v/v葵花籽油,pH=7.0)的乳化剂浓度为1.6%(w/v),在此条件下SPI形成的乳状液具有较大的平均粒径(d43≈30.9μm)。挤压预处理-Pan酶解联合改性能够显著改善SPI的乳化能力,效果比单纯Pan酶解改性好。其中ESPIH-140℃-Pan在DH=8.0?9.1%时制备的乳状液的平均粒径(d43=2.0μm)为所有样品中最小。而挤压预处理-Pap酶解联合改性不能改善SPI的乳化能力。
ESPI-140℃对Pan的敏感性提高,酶解变得强烈而广泛,使酶解产物的水解度(DH)、氮溶指数(NSI)、分子量分布、表面疏水性(H0)和二级结构都发生了显著的变化。在本论文所采用的条件下,SPI和SPIH-Pan制备的乳状液在均质过程中发生了桥联絮凝,在21天的静置贮存期间内出现了乳析;而ESPIH-140℃-Pan-9.1%能够制备出粒径细小的乳状液,该乳状液在贮存期间具有良好的对抗乳析和液滴聚集的稳定性。与对照SPI和SPIH-Pan-1.0%相比,ESPIH-140℃-Pan-9.1%界面活性较低;但具有较高的Fad(s67.6%)和较小的Гsat(2.8 mg/m2)。SPIH-Pan乳状液和ESPIH-140℃-Pan乳状液的|ζ|-电势都大于25 mV,具有良好的静电排斥效果。蛋白溶解性显著提高和分子柔性的增大是ESPIH-140℃-Pan-9.1%乳化能力改善的主要原因。
研究了不同功率的超声预处理对SPI酶解过程和酶解产物功能特性的影响。结果发现超声预处理能够使分散液中蛋白颗粒粒径减小。与SPI相比,USPI-200?600W对Pan和Pap的酶解敏感性都增强了,其中USPI-400W和USPI-600W的酶解敏感性较好。超声预处理-蛋白酶水解联合改性可以显著改善SPI的PR,效果比单纯酶解改性好。USPIH-400W-Pan-11.8%和USPIH-400W-Pap-2.9%的PR值分别为84.7%和86.1%,在中性和碱性条件下具有较高的NSI值;在酸性条件下,NSI值会显著下降。USPIH-400W-Pap-2.9%的等电点向酸性方向偏移,位于pH 3?4。超声预处理-蛋白酶水解联合改性对SPI热诱导凝胶性能的改善效果与单纯酶解改性效果相当。超声预处理-蛋白酶水解联合改性可以显著改善SPI的乳化能力,效果比单纯酶解改性好。USPIH-400W-Pap-1.3%制备的乳状液的平均粒径(d43=7.2μm)为所有USPIH乳状液中最小。
SPIH-Pap制备的乳状液在均质过程中发生了桥联絮凝,在21天的静置贮存期间内出现了乳析。而USPIH-400W-Pap乳化能力和乳析稳定性明显改善。与SPI和SPIH-Pap-0.6%相比,USPIH-400W-Pap-1.3%能够在较低的浓度下(3.0% w/v)制备出粒径细小且稳定的乳状液(d43 = 1.8μm)。SPIH-Pap乳状液和USPIH-400W-Pap乳状液的|ζ|-电势都大于25 mV,具有良好的静电排斥效果。超声预处理(400W)后,α-7S和A-11S的酶解敏感性提高,大豆蛋白中不同亚基的酶解变的迅速而协调,使USPIH-400W-Pap在一定DH范围内既具有良好的溶解性,又具有较高的H0,说明生成了许多具有界面活性的可溶性蛋白或肽,因此具有良好的乳化性能。
The use of soy proteins has been of increased interest, primarily attributed to its steady supply, high nutritional and low cost. However, the poor functional properties have limited the application of soy protein isolates (SPI) in food industry. Effects of two physical pre-treatment, twin-screw extrusion and power ultrasound, on the enzymatic hydrolysis and hydrolysates functional properties of SPI have been investigated. Various physicochemical properties, surface properties and secondary structural of modified SPI have also been studied in relation to DH and functional properties. The aim of this paper was to explore new methods for functionality modification of soy proteins, and by study the relationship between“processing method structure characteristics ? good functionalities”, the underpinning mechanisms of improved functionalities for modified SPI can be clarified, which can give academic and practical guide for the processing of soy protein product.
Effects of extrusion pre-treatment with different temperature (120℃, 140℃,160℃) on the enzymatic hydrolysis and functional properties of soy protein isolates (SPI) have been investigated. Results showed that comparing with SPI, the accessibility of the different extrusion pre-treated SPI (ESPI-120?160℃) was improved marked, with the ESPI-140℃showed the best performance. Combined modification of extrusion-enzymatic hydrolysis can markedly improve the protein recovery (PR) of SPI, which showed a much better effect than that of enzymatic hydrolysis alone. ESPIH-140℃-Pan (ESPI hydrolysate-140℃-Pan) had a PR of ca. 90% in the range of DH=8.0–10.0%, and exhibited a stable nitrogen solubility index (NSI) value among pH=3?11. The highest PR of ESPIH-140℃-Pap was 80.6%, but the NSI will decrease markedly around iso-electric point (pH=4.5). Combined modification of extrusion-enzymatic hydrolysis can not improve the heat-induced gelation properties of SPI. In this paper, the emulsifier concentration selected to make emulsions was set to be 1.6% (w/v), and the emulsion formed by SPI at this concentration had a large mean diameter (d43≈30.9μm). Extrusion-Pan hydrolysis can marked improved the emulsifying capability of SPI, with much better effect than that of enzymatic hydrolysis alone. Emulsions formed by ESPIH-140℃-Pan with DH=8.0?9.1% showed a smallest d43 (2.0μm) among all the sample emulsions. However, Extrusion-Pap hydrolysis can not improve the emulsifying capability of SPI.
Extrusion pre-treatment caused a marked improvement in the accessibility of SPI to Pan-hydrolysis, resulting in changes in degree of hydrolysis (DH), protein solubility (PS), surface hydrophobicity (H0) and molecular weight distributions (MWD) for ESPIH-140℃-Pan. It was observed that emulsion systems formed by control SPI or SPIH-Pan were unstable over a quiescent storage period of 21days, due to bridging flocculation and creaming. However, ESPIH-140℃-Pan-9.1% was capable of producing a very fine emulsion (d43 = 2.01μm) which remained stable over a long term quiescent storage. As compared with control SPI and SPIH-Pan-1.0%, ESPIH-140℃-Pan-9.1% appeared to be less surface active, but had a much higher Fads (67.6%) and a significantly lowerГsat (2.8 mg/m2). The |ζ|-potential of all SPIH-Pan and ESPIH-140℃-Pan were larger than 25 mV, which showed substantial electrostatic repulsion. It was suggested that significantly increased protein solubility and molecular flexibility could be the main reasons for the greatly improved emulsifying capability of ESPIH-140℃-Pan-9.1%.
Effects of ultrasound pre-treatment with different power (200W, 400W, 600W) on the enzymatic hydrolysis and functional properties of SPI have been investigated. Results showed that comparing with SPI, the accessibility of the different ultrasound pre-treated SPI (USPI-200?600W) was improved marked, with the USPI-400W showed the best performance. Combined modification of ultrasound-enzymatic hydrolysis can markedly improve the PR of SPI, which showed a better effect than that of enzymatic hydrolysis alone. USPIH-400W-Pan-11.8% and USPIH-400W-Pap-2.9% had PR of 84.7% and 86.1% respectively. Their NSI increased slightly in basic conditions but decreased markedly at acidic conditions. The iso-electric point of USPIH-400W-Pap-2.9% showed a shift to pH 3?4. Combined modification of Ultrasound-enzymatic hydrolysis exhibited a equivalent improvement on heat-induced gelation properties of SPI to that of enzymatic hydrolysis alone. Ultrasound-enzymatic hydrolysis can marked improved the emulsifying capability of SPI, with much better effect than that of enzymatic hydrolysis alone. Emulsions formed by USPIH-400W-Pap-1.3% showed a smallest d43 (7.2μm) among all the USPIH emulsions.
Emulsion formed by SPIH-Pap became unstable over a quiescent storage of 21 days, due to bridging flocculation and creaming. In contrast, USPIH-400W-Pap exhibited much better emulsifying capability and creaming stability under similar conditions. And as compared with control SPI and SPIH-Pap-0.6%, USPIH-400W-Pap-1.3% was capable of forming stable emulsions with small droplet sizes (d43 = 1.8μm) and at a much lower protein concentration (3.0% w/v). The |ζ|-potential of all SPI-Pap and USPIH-400W-Pap were larger than 25 mV, which showed substantial electrostatic repulsion. After ultrasound pre-treatment, the accessibility ofα-7S and A-11S was improved, and the enzymatic hydrolysis of USPI-400W became fast and harmonious. In some DH range, not only USPIH-400W-Pap had good protein solubility, but also had high H0, which indicated that a lot of surface active proteins or peptides were created. As a result, emulsifying capability was improved.
引文
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