食品科学 ›› 2013, Vol. 34 ›› Issue (21): 10-15.doi: 10.7506/spkx1002-6630-201321003

• 基础研究 • 上一篇    下一篇

pH值偏移处理豌豆分离蛋白的胶凝性质

蒋 将1,李开放1,刘元法1,*,熊幼翎2   

  1. 1.江南大学食品学院,江苏 无锡 214122;2.肯塔基大学动物与食品科学系,列克星顿 40546,美国
  • 收稿日期:2013-08-30 修回日期:2013-10-28 出版日期:2013-11-15 发布日期:2013-10-28
  • 通讯作者: 刘元法 E-mail:foodscilyf@163.com
  • 基金资助:

    国家自然科学基金项目(30471225);“十二五”国家科技支撑计划项目(2012BAD28B04)

Gelation Properties of Pea Protein Isolate underwent pH-shifting Treatment

JIANG Jiang1,LI Kai-fang1,LIU Yuan-fa1,*,XIONG You-ling L.2   

  1. 1. School of Food Science and Technology, Jiangnan University, Wuxi 214122, China;
    2. Department of Animal and Food Sciences, University of Kentucky, Lexington 40546, USA
  • Received:2013-08-30 Revised:2013-10-28 Online:2013-11-15 Published:2013-10-28
  • Contact: LIU Yuan-fa E-mail:foodscilyf@163.com

摘要:

豌豆分离蛋白(PPI)经pH值偏移处理后,高级结构的变化会导致其功能性质的变化。本研究针对pH值偏移处理前后豌豆分离蛋白胶凝特性的变化,研究对比不同处理豌豆分离蛋白的最小胶凝质量浓度(MGC)、氨基酸组成、凝胶特性以及参与成胶的蛋白亚基。结果表明:pH值偏移处理改性后的PPI具有更低的MGC(从16g/100mL降低到14g/100mL)。与碱改性PPI对照组相比较,添加0.1mol/L NaCl或者10mmol/L CaCl2的存在可以使凝胶强度明显提高,分别高达4倍和9倍,转谷氨酰胺酶(TG)和10mmol/L CaCl2的加入使凝胶强度提高11倍。为进一步揭示蛋白分子间相互作用的强弱,对添加不同种类和浓度盐离子的溶胶体系进行频率(0.1~10Hz)扫描,发现碱性pH值偏移处理PPI对溶胶体系G’和G”的提升与所形成的凝胶体系的强度有很好的对应关系。总之,碱性pH值处理的蛋白由于分子内的作用力增强,因此加热过程中形成更稳定的凝胶网络结构。

关键词: 豌豆蛋白, pH值偏移处理, 胶凝强度, 亚基组成, 流变动力学

Abstract:

The tertiary structure of pea protein can be modified by pH-shifting treatments to bring about enhanced functional
properties. To exploit the application potential of pea protein isolate (PPI) as a novel protein ingredient, this research
focused on the gelation properties of PPI under different processing treatments. The minimum gelling concentration (MGC)
was reduced from 16 g/100 mL for native PPI to 14 g/100 mL after either acid (pH 1.5) or alkaline (pH 12) treatment. These
three types of PPI were subjected to 0.1 mol/L and 0.6 mol/L NaCl or 5, 10 mmol/L and 20 mmol/L CaCl2, and the samples
with 0, 0.1 mol/L NaCl and 10 mmol/L CaCl2 were also treated with 0.1% microbial transgluaminase (TGase) to elucidate
the effect of salts and TGase on gel strength. It was found that the pH 12 treatment markedly improved the PPI gel strength
(up to 9 fold), and the presence of TGase further enhanced the gelling potential of PPI (by 11 fold) (P < 0.05). Dynamic
rheology tests showed greater shear storage (G’) and loss (G”) moduli for pH 12 treated PPI than for untreated SSP at all
oscillatory frequencies tested (0.1—10 Hz), indicating stronger intermolecular interactions in the protein matrix of the
thermal gels comprised of alkaline pH-treated PPI.

Key words: pea protein isolate, pH-shifting treatment, gelation strength, subunit composition, dynamic rheology

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