Page 167 - 《精细化工》2022年第1期

第 1 期 马天怡，等: L-精氨酸/L-赖氨酸改性大豆分离蛋白乳化性 ·157·

而 pH 对照组中油滴分布不均匀，且排列紧密，有 [10] JIANG J, CHEN J, XIONG Y L. Structural and emulsifying
properties of soy protein isolate subjected to acid and alkaline
可能发生了油滴聚集现象。CLSM 的结果与图 6B pH-shifting processes[J]. Journal of Agricultural and Food
中稳定性结果一致。 Chemistry, 2009, 57(16): 7576-7583.
[11] WANG Y S, LIU C Q, MA T Y, et al. Physicochemical and
functional properties of γ-aminobutyric acid-treated soy proteins[J].
3 结论 Food Chemistry, 2019, 295: 267-273.
[12] GORNALL A G, BARDAWILL C J, DAVID M M. Determination of
采用两种质量浓度均为 1、3 g/L 的 L-Arg、L-Lys serum proteins by means of the biuret reaction[J]. Journal of
Biological Chemistry, 1949, 177(2): 751-766.
分别改性 SPI，系统研究了这两种氨基酸对 SPI 结
[13] JIANG J, XIONG Y L, CHEN J. pH Shifting alters solubility
构、物理化学性质及溶解性、乳化性的影响。主要 characteristics and thermal stability of soy protein isolate and its
globulin fractions in different pH, salt concentration, and temperature
结论如下：
conditions[J]. Journal of Agricultural and Food Chemistry, 2010,
（1）L-Arg、L-Lys 均能有效地提高 SPI 的溶解 58(13): 8035-8042.
[14] WANG Y S, XIONG Y L, RENTFROW G K, et al. Oxidation
性，这为 SPI 基于溶解度的功能性提升提供了基础。
promotes cross-linking but impairs film-forming properties of whey
（2）L-Arg、L-Lys 加入 SPI 溶液中，通过改变 proteins[J]. Journal of Food Engineering, 2013, 115(1):11-19.
溶液 pH 及与蛋白之间非共价相互作用，进而促进 [15] ZHANG W W, LIU C Q, ZHAO J, et al. Modification of structure
and functionalities of ginkgo seed proteins by pH-shifting
SPI 疏水性基团（比如：Trp 残基）折叠；显著降低 treatment[J]. Food Chemistry, 2021, 358: 129862.
SPI 在溶液中的粒径大小，并促进蛋白带电量。 [16] WANG Y S (王耀松), ZHANG W W (张唯唯), MA T Y (马天怡)，
et al. Influence of oxidative modification by malondialdehyde on
（3）L-Arg、L-Lys 能够显著提高 SPI 乳化活性 structure and emulsifying properties of walnut protein[J]. Scientia
和乳化稳定性。 Agricultura Sinica (中国农业科学), 2020, 53(16): 3372-3384.
[17] WANG Y S, ZHAO J, ZHANG W W, et al. Modification of
（4）L-Arg、L-Lys 对 SPI 结构及功能性的影响 heat-induced whey protein gels by basic amino acids[J]. Food
随着浓度增加而增强。总体上来看，L-Arg 比 L-Lys Hydrocolloids, 2020, 100: 105397.
[18] LAM R S H, NICKERSON M T. Food proteins: A review on their
更有效地提高 SPI 溶解性和乳化活性。 emulsifying properties using a structure-function approach[J]. Food
总之，天然碱性氨基酸能够有效提升植物蛋白 Chemistry, 2013, 141(2): 975-984.
[19] WU G L, WANG S J, TIAN Z, et al. Elucidating the weak
的乳化性。以上研究一方面挖掘了碱性氨基酸的功 protein-protein interaction mechanisms behind the liquid-liquid
能性并扩大了它们在食品体系中的应用范围，另一 phase separation of a mAb solution by different types of additives[J].
European Journal of Pharmaceutics and Biopharmaceutics, 2017,
方面为蛋白功能改进提供了一种方法和理论基础。 120: 1-8.
[20] LI S Y, ZHENG Y D, XU P, et al. L-Lysine and L-arginine inhibit
参考文献： myosin aggregation and interact with acidic amino acid residues of
myosin: The role in increasing myosin solubility[J]. Food Chemistry,
[1] MA T Y (马天怡), ZHANG W W (张唯唯), HE Z D (何振东), et al. 2018, 242: 22-28.
Recent advances on basic amino acids modifying functionalities of [21] LI S Y, LI L X, ZHU X X, et al. Conformational and charge changes
food proteins[J]. Fine Chemicals (精细化工), 2021, 38(2): 294-305. induced by L-arginine and L-lysine increase the solubility of chicken
[2] ARAKAWA T, EJIMA D, TSUMOTO K, et al. Suppression of myosin[J]. Food Hydrocolloids, 2019, 89: 330-336.
protein interactions by arginine: A proposed mechanism of the [22] STÄRTZEL P. Arginine as an excipient for protein freeze-drying: A
arginine effects[J]. Biophysical Chemistry, 2007, 127(1/2): 1-8. mini review[J]. Journal of Pharmaceutical Sciences, 2018, 107(4):
[3] CHEN X, ZOU Y F, HAN M Y, et al. Solubilisation of myosin in a 960-967.
solution of low ionic strength L-histidine: Significance of the [23] HAYES D G, SOLAIMAN D K Y, ASHBY R D. Biobased
imidazole ring[J]. Food Chemistry, 2016, 196: 42-49. surfactants: Synthesis, properties, and applications[M]. Cambridge:
[4] GUO X Y, PENG Z Q, ZHANG Y W, et al. The solubility and Academic Press and AOCS Press, 2019: 413-445.
conformational characteristics of porcine myosin as affected by the [24] ARAKAWA T, TSUMOTO K. The effects of arginine on refolding of
presence of L-lysine and L-histidine[J]. Food Chemistry, 2015, 170: aggregated proteins: Not facilitate refolding, but suppress aggregation[J].
212-217. Biochemical and Biophysical Research Communications, 2003,
[5] LI L X, CHEN L, NING C, et al. L-Arginine and L-lysine improve 304(1): 148-152.
the physical stability of soybean oil-myosin emulsions by changing [25] BAYNES B M, WANG D I C, TROUT B L. Role of arginine in the
penetration and unfolding behaviors of interfacial myosin[J]. Food stabilization of proteins against aggregation[J]. Biochemistry, 2005,
Hydrocolloids, 2020, 98: 105265. 44(12): 4919-4925.
[6] ZHU X C, LI L X, LI S Y, et al. L-Arginine/L-lysine improves [26] LANGE C, RUDOLPH R. Suppression of protein aggregation by
emulsion stability of chicken sausage by increasing electrostatic L-arginine[J]. Current Pharmaceutical Biotechnology, 2009, 10(4): 1-7.
repulsion of emulsion droplet and decreasing the interfacial tension [27] HU Y, ARORA J, JOSHI S B, et al. Characterization of excipient
of soybean oil-water[J]. Food Hydrocolloids, 2019, 89: 492-502. effects on reversible self-association, backbone flexibility, and solution
[7] SINGH P, KUMAR R, SABAPATHY S N, et al. Functional and properties of an IgG1 monoclonal antibody at high concentrations:
edible uses of soy protein products[J]. Comprehensive Reviews in Part 1[J]. Journal of Pharmaceutical Sciences, 2020, 109: 340-352.
Food Science and Food Safety, 2008, 7(1): 14-28. [28] GAO R C, SHI T, SUN Q C, et al. Effects of L-arginine and L-
[8] CRAIG R, WOODHEAD J L. Structure and function of myosin histidine on heat-induced aggregation of fish myosin: Bighead carp
filaments[J]. Current Opinion in Structural Biology, 2006, 16(2): (Aristichthys nobilis)[J]. Food Chemistry, 2019, 295: 320-326.
204-212. [29] SHUKLA D, TROUT B L. Interaction of arginine with proteins and
[9] MU B N, XU H L, LI W, et al. Spinnability and rheological the mechanism by which it inhibits aggregation[J]. The Journal of
properties of globular soy protein solution[J]. Food Hydrocolloids, Physical Chemistry B, 2010, 114(42): 13426-13438.
2019, 90: 443-451. （下转第 163 页）