CN116268423B - 活性成分-蛋白质冷凝胶及其制备方法和应用 - Google Patents
活性成分-蛋白质冷凝胶及其制备方法和应用 Download PDFInfo
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Abstract
本发明涉及一种活性成分‑蛋白质冷凝胶及其制备方法和应用,属于蛋白质凝胶制备领域。本发明所述的蛋白质冷凝胶是水溶性蛋白质溶解后加热变性,待冷却后添加活性成分诱导成胶,其活性成分有维生素C、维生素C和氯化钙、维生素C钙三种方式,活性成分诱导形成蛋白质冷凝胶的同时实现活性成分的包埋固化,本发明方法简单高效,制成的凝胶质量好,凝胶强度可调控,活性成分包埋效果好且稳定性高,可应用于食品、保健品或化妆品中。
Description
技术领域
本发明涉及一种活性成分-蛋白质冷凝胶及其制备方法和应用,属于蛋白质凝胶制备领域。
背景技术
维生素C(VC)是一种酸性的水溶性维生素,维生素C钙(VC-Ca)是维生素C的钙盐衍生物,它们具有良好的抗氧化性以及预防和治疗坏血病等生理功能,在食品、制药和化妆品领域有突出作用。但由于烯二醇与内酯环羰基共扼效应的影响,维生素C结构不稳定,在加工或贮藏过程中受到pH变化、高温、氧气、光照、水分和过渡金属离子等因素的影响,容易发生氧化或水解反应而丧失活性。近年来,包埋技术是将活性成分与环境因素隔离,提高其稳定性的新型途径之一。但是,维生素C的水溶性不利于其的高效包埋;常见包埋方法如喷雾干燥等由于加工过程中的高温等条件易造成活性成分的损失。
蛋白质(如乳清蛋白、大豆蛋白、酪蛋白等)作为天然的两亲性材料,具有高营养品质的同时还能通过响应外界刺激,并调节构象变化形成水凝胶。蛋白质水凝胶在保持网络结构的同时膨胀并捕获大量的溶剂,有可能达到亲水活性成分的封装、保护和递送。乳清分离蛋白(WPI)主要是由β-乳球蛋白、α-乳白蛋白、牛血清白蛋白和免疫球蛋白组成,营养价值高,易消化吸收,并且具有良好的功能特性,如凝胶性、乳化性和起泡性等。传统的热处理凝胶法不可避免地会造成蛋白质过度和不均匀聚集,并使得热敏成分失去活性。因此,蛋白质冷凝胶在包埋活性成分方面更具优势,通常由蛋白质变性和聚集两步法制备。在聚集步骤中,葡糖酸内酯、金属离子等被广泛被用作交联剂。然而,葡糖酸内酯作为酸性交联剂,服用过多时容易引起高血糖反应和腹痛等消化道不良症状。寻找一种活性成分诱导形成蛋白质冷凝胶的同时实现活性成分的包埋固化的方法,能够提高活性成分的稳定性,也能拓展蛋白质冷凝胶在食品、保健品或化妆品等领域中的应用。
发明内容
本发明要解决的技术问题是,提供一种活性成分-蛋白质冷凝胶及其制备方法,活性成分诱导形成蛋白质冷凝胶的同时实现活性成分的包埋固化,避免了在聚集步骤额外交联剂的使用,方法简单高效,凝胶质量好,凝胶强度可调控,活性成分包埋效果好,本发明同时提供了所述蛋白质冷凝胶的应用。
本发明所述的蛋白质冷凝胶是由活性成分诱导形成的,并且包埋固化所述活性成分的冷凝胶,所述活性成分为维生素C、维生素C与氯化钙的组合或维生素C钙。
本发明所述的活性成分-蛋白质冷凝胶的制备方法,包括以下步骤:
(1)将蛋白质加入水中溶解,调节pH至中性,加热使蛋白质变性后,冷却到室温,得到变性的蛋白溶液;
(2)将活性成分加入变性的蛋白溶液中,搅拌均匀后静置,得到所述活性成分-蛋白质冷凝胶。
优选的,蛋白质水溶液的浓度为60-100mg/mL,优选100mg/mL。
优选的,蛋白质为乳清蛋白、大豆蛋白和酪蛋白中的一种或多种。
优选的,步骤(1)中,水优选去离子水或超纯水,为达到水溶性蛋白质充分溶解的目的,可在搅拌均匀后将溶液置于4℃冷藏10-12h,pH调节剂可选择1M的NaOH和HCl溶液;加热使蛋白质变性的步骤加热温度≥65℃。
优选的,活性成分为维生素C时,添加维生素C至pH为4.0-6.0时停止,优选pH为4.0或6.0。
优选的,活性成分为维生素C与氯化钙的组合时,先添加维生素C调节pH至3.5-4.0,再添加氯化钙至浓度为15-100mM,优选先添加维生素C调节pH至3.5,再添加氯化钙至终浓度为40mM。
优选的,活性成分为维生素C钙时,添加维生素C钙至浓度为15-58mM,优选15.6mM。
优选的,步骤(2)中,热变性的蛋白溶液需冷却至室温才可加入活性成分,优选使用磁力搅拌器在1200rpm速度下加入活性成分,并在搅拌均匀后,置于4℃冷藏10-12h促进冷凝胶形成。
本发明所述的活性成分-蛋白冷凝胶可应用于食品、保健品或化妆品中。
所述活性成分-蛋白质冷凝胶可应用于高效包埋和保护一种或多种热敏感的亲水性功能因子。
与现有技术相比,本发明具备以下有益效果:
1、本发明所述蛋白质冷凝胶的制备方法,简单高效,可在活性成分诱导形成蛋白质冷凝胶的同时可实现活性成分的包埋固化,避免了在聚集步骤额外交联剂的使用。
2、本发明所述蛋白质冷凝胶质量好,具有优异的质构特性和持水力,可调的凝胶强度以及致密均匀的凝胶结构。
3、本发明所述蛋白质冷凝胶活性成分包埋效果好且稳定性高。尤其是维生素C的保留率均高于80%。
4、本发明所述蛋白质冷凝胶的制备方法可适应不同产品的需求。本发明提供了三种活性成分的添加方案,维生素C酸化范围在pH值为4.0-6.0,在维生素C酸化条件下添加15-100mM氯化钙,添加维生素C钙15-58mM,并且三种方案均能形成质量良好的凝胶。
附图说明
图1为本发明实施例1制备的维生素C在不同pH条件下诱导的蛋白冷凝胶形成;
图2为本发明实施例2制备的维生素C和氯化钙在不同氯化钙浓度下诱导的蛋白冷凝胶形成;
图3为本发明实施例3制备的维生素C钙在不同浓度下诱导的蛋白质冷凝胶形成;
图4为本发明实施例1制备的维生素C诱导的蛋白质冷凝胶激光共聚焦显微镜图;
图5为本发明实施例2制备的维生素C和氯化钙诱导的蛋白质冷凝胶激光共聚焦显微镜图;
图6为本发明实施例3制备的维生素C钙诱导的蛋白质冷凝胶激光共聚焦显微镜图;
图7为本发明实施例1制备的维生素C诱导的蛋白质冷凝胶在3种解离剂中浸泡0h和24h后蛋白质的溶解情况;
图8为本发明实施例2制备的维生素C和氯化钙诱导的蛋白质冷凝胶在3种解离剂中浸泡0h和24h后蛋白质的溶解情况;
图9为本发明实施例3制备的维生素C钙诱导的蛋白质冷凝胶在3种解离剂中浸泡0h和24h后蛋白质的溶解情况;
其中,标注pH值、Ca 2+浓度、VC-Ca浓度代表实施例中相应的凝胶样品。
具体实施方式
下面结合实施例对本发明作进一步描述。
需要说明的是:在实际操作中,温度控制允许有1℃的波动温差,实施例中用到的所有原料除特殊说明外,均为市购。
实施例1
本发明所述活性成分-蛋白质冷凝胶的制备方法,包括以下步骤:
(1)将乳清蛋白加入超纯水中,使浓度为100mg/mL,充分搅拌后置于4℃冷藏12h,保证蛋白充分水合;
使用NaOH溶液(1M)调节蛋白溶液pH至7.0,置于恒温水浴槽中85℃加热30min,冷却至室温后,得到变性的蛋白溶液;
(2)在变性的蛋白溶液中,利用在1200rpm速度搅拌下逐滴添加维生素C(250mg/mL),利用pH计监测样品的pH值分别至6.5、6.0、5.0、4.0、3.5,搅拌均匀后,4℃冷藏12h,在pH值为6.0、5.0和4.0条件下得到维生素C诱导的蛋白质冷凝胶。
实施例2
本发明所述活性成分-蛋白质冷凝胶的制备方法,包括以下步骤:
(1)将乳清蛋白加入超纯水中,使浓度为100mg/mL,充分搅拌后置于4℃冷藏12h,保证蛋白充分水合;
使用NaOH溶液(1M)调节蛋白溶液pH至7.0,置于恒温水浴槽中85℃加热30min,得到热变性的蛋白溶液;
(2)热变性的蛋白溶液冷却至室温后,利用磁力搅拌器在1200rpm速度下逐滴添加维生素C(250mg/mL),利用pH计监测样品的pH值至3.5,再逐滴添加氯化钙(5M)至终浓度为25、40、50、75、100mM,搅拌均匀后,4℃冷藏12h,得到维生素C和氯化钙诱导的蛋白质冷凝胶。
实施例3
本发明所述活性成分-蛋白质冷凝胶的制备方法,包括以下步骤:
(1)将乳清蛋白加入超纯水中,使浓度为100mg/mL,充分搅拌后置于4℃冷藏12h,保证蛋白充分水合;
使用NaOH溶液(1M)调节蛋白溶液pH至7.0,置于恒温水浴槽中85℃加热30min,得到热变性的蛋白溶液;
(2)热变性的蛋白溶液冷却至室温后,利用磁力搅拌器在1200rpm速度下逐滴添加维生素C钙(250mg/mL),至终浓度为15.6、24.6、30.4、47.4、58.2mM,搅拌均匀后,4℃冷藏12h,得到维生素C钙诱导的蛋白质冷凝胶。
对上述得到的蛋白质冷凝胶进行检测:
1、成胶结果表观现象分析:
如图1、2、3,维生素C、维生素C和氯化钙、维生素C钙均能成功诱导乳清蛋白形成凝胶。
从图1可以看出,随着维生素C的添加,乳清蛋白溶液(100mg/mL)能在pH 4.0-6.0范围内形成具有不同外观的凝胶,当pH接近乳清蛋白等电点(pI~5.0)时,呈类乳状液的不透明凝胶,这是由于蛋白表面静电斥力几乎为0,蛋白分子发生快速且无序聚集;而当pH在4.0和6.0时,凝胶呈现半透明态,这是由于当pH远离pI时,蛋白表面带电量增多,静电斥力增大,抑制了蛋白质的过度聚集,形成较为均匀的凝胶结构,当维生素C调节pH值为3.5时,由于较强的静电斥力,乳清蛋白恢复到溶液状态。
从图2可以看出,乳清蛋白在维生素C酸化至pH=3.5时,随着Ca2+浓度增大,在浓度25-50mM范围内形成凝胶,这是因为Ca2+可以屏蔽蛋白质表面电荷并形成盐桥,导致蛋白聚集成胶。然而,高浓度Ca2+(75-100mM)导致了凝胶结构的解体,这可能是由于多余的Ca2+诱导蛋白过度聚集导致。
从图3可以看出,在中性条件下,乳清蛋白需要更少的维生素C钙添加量就能成胶,与图2类似,随着维生素C钙添加量的增大(47.4和58.2mM),凝胶结构有一定程度的破坏。这可能是蛋白在中性pH条件下所带负电荷数目远大于pH 3.5时,因此维生素C钙诱导WPI凝胶化所需的Ca2+少于酸性环境下的浓度。
2、蛋白冷凝胶质构特性和持水力
取16g凝胶置于25mL规格的小烧杯中,于4℃冰箱静置24h后使用XT2i物性测试仪对样品硬度、弹性和回复性进行测定。采用P/0.25圆柱形探测头,质地剖面分析(Textureprofile analysis TPA)模式;压缩程度为50%,测前、测后及测试速度均为1mm/s,触发力为2.0g。取1g样品于离心管内,在8000g,20℃条件下离心20min,按以下公式计算持水力:
如表1所示,在实施例1中,在pH=6.0时,维生素C诱导的乳清蛋白冷凝胶有着最好的凝胶特性,硬度、粘性、回弹性和持水力分别为325.8g,-150.0g·sec,0.76和100%。随着pH降低,冷凝胶硬度和回弹性都下降,在pH=5.0时有最低的弹性和持水力(59.3%),表明此时由于净电荷减少,在其等电点附近沉淀和聚集,导致蛋白质对水的亲和力降低,且不利于水分子进入凝胶网络,而在pH=4.0时有较高持水力97%。因此,优先选用pH值为4.0或6.0条件。在实施例2和实施例3中发现,VC酸化以及钙离子的辅助,能够在特定条件下形成持水力100%的凝胶,这能够实现水溶性功能因子的高效包埋固化。但是,随着Ca2+浓度增大,除回弹性外,凝胶硬度、粘性和持水力均发生显著降低,类似的,在实施例3中,随着维生素C钙浓度增大,质构特性和持水力均发生显著降低。这说明Ca2+的加入,它首先提高了凝胶结构的密度,并允许水被束缚在凝胶网络孔隙中。随着Ca2+浓度的进一步增加,则产生了更大的聚合体,导致内部形成较大的孔隙网络,从而降低持水能力。因此,优先选用维生素C酸化至pH=3.5并添加氯化钙(40mM),以及直接添加维生素C钙(15.6mM)两种条件。
表1乳清蛋白冷凝胶质构特性和持水力
注:不同字母表示统计分析差异显著(p<0.05)。
3、激光共聚焦显微镜观察蛋白冷凝胶结构
配制0.1%(w/v%)尼罗兰染液,准确称取一定质量尼罗兰样品粉末,溶于无水乙醇中,避光储存。取0.01g左右的凝胶于2mL离心管中,加入20μL尼罗兰染料溶液,染色比例1:2,震荡使染色均匀。取少量染色后的凝胶于载玻片上并密封,物镜40倍观察,激发波长为633nm。
通过激光共聚焦显微镜观察乳清蛋白冷凝胶结构发现,绿色亮区域为染色的蛋白,黑色区域为蛋白冷凝胶结构内部间隙。如图4所示,在pH值为6.0时,热变性乳清蛋白随着pH值的降低,由于静电排斥力的降低,其微观结构变得更加紧凑和均一,而在pH值为4.0时,蛋白质聚集程度进一步增大导致凝胶内部间隙变大。如图5所示,当pH降低为3.5时,因静电斥力增强,凝胶结构会进一步松散和强度降低,但低浓度Ca2+(40mM)的添加有效地促进了蛋白形成致密均一的凝胶结构,但孔隙会随着Ca2+浓度的增高而扩大。在实施例3制备的凝胶中发现类似效果(图6)。
4、维生素C诱导的蛋白冷凝胶分子间作用力
配置3种解离溶液:S1(0.6M NaCl)、S2(0.6M NaCl+1.5M尿素)和S3(0.6M NaCl+8M尿素),其中0.6M NaCl破坏静电作用,0.6M NaCl+1.5M尿素破坏氢键,0.6M NaCl+8M尿素破坏疏水作用。取1g左右的胶体,分别溶解于5mL解离剂中,观察浸泡0h和24h后的蛋白溶解情况。
如图7,维生素C引起的交联使得蛋白在0.6M NaCl和0.6M NaCl+1.5M尿素中浸泡24h后依旧保留大部分凝胶结构,表明此时蛋白发生了非离子键和氢键导致的聚集。而在0.6MNaCl+8M尿素中浸泡24h后,凝胶结构被显著破坏,此时蛋白质大部分被溶解,表明在pH6.0和4.0条件下疏水相互作用是稳定乳清蛋白凝胶化的主要动力。如图8,在维生素C酸化条件下引入40mM钙离子,大部分蛋白质凝胶结构在0.6M NaCl+8M尿素中浸泡24h后被破坏,因此疏水相互作用依旧是蛋白凝胶化的主要驱动力。然而,随着钙离子浓度的增大,蛋白质凝胶结构越能在0.6M NaCl+8M尿素中得到保留。类似的现象在实施例1-3的蛋白冷凝胶中发现(如图9)。当引入高浓度钙离子和维生素C钙时,乳清蛋白冷凝胶交联力可能是是金属离子与蛋白质链中金属官能团之间的金属配位(金属配体相互作用),该相互作用被认为强于大多数非共价相互作用,但弱于典型的共价键相互作用,因而不能被解离剂破坏。
5、维生素C在蛋白冷凝胶中的保留率和实际含量
采用离心联合高效液相色谱法测定维生素C的保留率和实际含量,维生素C采用高效液相色谱HPLC(Waters,MA,USA)测定,采用2695分离模块、2998PDA检测器和T3色谱柱(5μm,4.6mm×250mm),流动相为甲醇:甲酸:水=3:30:970(v/v),流速1mL/min,柱温为35℃,洗脱并检测维生素C含量。取0.45g的凝胶,加入30mL超纯水,在10000rpm条件下高速剪切2min,取0.5mL的剪切后的溶液,加入1mL的偏磷酸溶液(4.5%,w/v),涡旋1min,然后在4℃,3500g条件下离心5min,取上清液,过0.45μm水系膜,利用HPLC测定峰面积,根据所得标准曲线计算维生素C含量,按以下公式计算维生素C保留率和实际含量:
如表1所示,关于持水力的结果,我们发现在pH=4或6(实施例1),VC+Ca2+40mM(实施例2)和VC-Ca 15.62mM(实施例3)的持水力为100%或接近100%,具有良好的维生素C封装能力。进一步测定维生素C的保留率,如表2所示,发现所有样品的保留率均>80%,其中,保留率随pH的降低而降低(实施例1),这是由于维生素C在酸化过程中的脱氢和进一步降解导致;回收率也随着维生素C钙的添加而降低,这可能是蛋白过度聚集导致维生素C随着水分的析出而流失,以及维生素C在中性环境下自然氧化导致。实际上,在凝胶过程中,维生素C损失的程度都在可接受的范围内。
表2乳清蛋白冷凝胶终维生素C保留率和含量
注:不同字母表示统计分析差异显著(p<0.05)。
凝胶样品中维生素C含量如表2所示,由于体系pH越低,所需要的维生素C添加量越高,因此维生素C酸化至pH=3.5并添加Ca2+诱导乳清蛋白冷凝胶中(实施例2)含有最高的VC含量(约48mg/g凝胶),同时,其酸性环境也在理论上保证了VC的稳定性。而在pH=6.0条件下,VC含量最低,约为3mg/g凝胶。
显然,上述实施例仅仅是为清楚地说明所作的举例,并非对实施方式的限定,对于所属领域的普通技术人员来说,在上述说明的基础上还可以做出其它不同形式变化或变动,这里无需也无法对所有的实施方式予以穷举,而由此所引申出的显而易见的变化或变动仍处于本发明创造的保护范围之中。
Claims (6)
1.一种活性成分-蛋白质冷凝胶的制备方法,其特征在于,包括以下步骤:
(1)将乳清蛋白加入水中,使乳清蛋白水溶液的浓度为60-100mg/mL,充分搅拌保证蛋白充分水合,调节乳清蛋白水溶液pH至中性,加热使蛋白质变性后,冷却至室温后,得到变性的乳清蛋白溶液;
(2)将活性成分加入变性的乳清蛋白溶液中,搅拌均匀后静置,使所述活性成分诱导乳清蛋白冷凝胶;
所述活性成分为维生素C、维生素C与氯化钙的组合或维生素C钙;
当所述活性成分为维生素C时,将维生素C加入变性的乳清蛋白溶液中,直至溶液的pH至4.0-6.0;
当所述活性成分为维生素C与氯化钙的组合时,先将维生素C加入变性的乳清蛋白溶液中,直至溶液的pH至3.5-4.0,再添加氯化钙至浓度为25-50mM;
当所述活性成分为维生素C钙时,将维生素C钙加入变性的乳清蛋白溶液中,使维生素C钙终浓度为15.6-30.4mM。
2.如权利要求1所述方法,其特征在于,所述步骤(1)中乳清蛋白水溶液的浓度为100mg/mL。
3.如权利要求1所述方法,其特征在于,加热温度≥65℃。
4.如权利要求1所述方法,其特征在于,所述步骤(1)中充分搅拌保证蛋白充分水合具体步骤为充分搅拌后置于4℃冷藏12h,保证蛋白充分水合。
5.权利要求1-4任一项所述方法制备得到的活性成分-蛋白质冷凝胶。
6.权利要求5所述的活性成分-蛋白冷凝胶在制备食品、保健品或化妆品中的应用。
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