CN1283168C - 发泡性改进的改性乳清蛋白组合物 - Google Patents
发泡性改进的改性乳清蛋白组合物 Download PDFInfo
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- CN1283168C CN1283168C CNB02824320XA CN02824320A CN1283168C CN 1283168 C CN1283168 C CN 1283168C CN B02824320X A CNB02824320X A CN B02824320XA CN 02824320 A CN02824320 A CN 02824320A CN 1283168 C CN1283168 C CN 1283168C
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- lactalbumin
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- phospholipase
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Abstract
本发明涉及将含有乳清蛋白的水溶液与磷脂酶相接触来改进乳清蛋白制品发泡性的方法。用磷脂酶处理乳清蛋白制品的结果导致,与未用磷脂酶处理的乳清蛋白相比,用磷脂酶处理的乳清蛋白在搅拌时其泡抹容积膨胀率和泡抹稳定性改进。
Description
发明领域
本发明涉及乳清蛋白的改性方法和发泡性改进的改性乳清蛋白组合物。
发明背景
乳清是干酪制备的副产品。传统上,乳清作为没用的废料或作为肥料或动物饲料。食品加工业将乳清蛋白制品作为固体蛋清(egg white solids)的替代品而用于为多种配制食品增添特性。由于乳清蛋白的感官特性和功能特性以及与固体蛋清相比较低的成本,故其可作为食品加工业中重要且有用的原料来源。
乳清蛋白用于食品加工业的一个优势是其发泡性。搅拌乳清蛋白可以形成泡沫,所形成的泡沫可用于,例如,低热量甜食、冰淇淋和糖果制品中。然而,乳清蛋白在如下的发泡性上比固体蛋清差,包括较弱的可搅拌性以及在搅拌后较差的泡沫稳定性。
已知,很多方法可用于改进乳清蛋白的发泡性。例如,Philips等,美国专利:5,580,491中记载了对乳清蛋白改性以改进乳清蛋白发泡性的非酶方法。Blecker等,“Modification of the interfacial proterties of whey byenzymatic hydrolysis of the residual fat”,Food Macromolecules and Colloids,85-59页(1995)中记载了通过用脂肪酶进行酶水解来改性乳清蛋白的酶方法。Chen,WO 01/06867中也记载了通过使用蛋白酶改性乳清蛋白制品来改进其发泡性的酶方法。
尽管已经取得上述以及其它的进展,不过本领域中仍然需要一种改进乳清蛋白制品发泡性和感官特性的方法。
发明概述
本发明提供了一种改进乳清蛋白制品发泡性的方法。将含有乳清蛋白的水溶液与磷脂酶相接触来制备本发明所述的改性乳清蛋白制品。用磷脂酶处理的结果导致,与未用磷脂酶处理的乳清蛋白相比,用磷脂酶处理的乳清蛋白在搅拌时其泡抹容积膨胀率(foam overrun)和泡抹稳定性增强。此外,用磷脂酶处理乳清蛋白不会给改性乳清蛋白制品或用改性乳清蛋白制品制备的泡沫制品带来不需要的风味。
本发明还涉及磷脂酶在制造用乳清蛋白成分所制备的产品中的用途,其中用磷脂酶处理乳清蛋白成分。本发明还涉及采用上述任一种方法制备的产品。
附图说明
图1:显示了磷脂酶处理对乳清蛋白浓缩物泡沫容积膨胀率的影响。
图2:显示了磷脂酶处理对乳清蛋白浓缩物泡沫稳定性的影响,以泡沫还液时间(Drainage time)进行检测。
发明详述
可以采用将将含有乳清蛋白的水溶液与磷脂酶相接触的方法来制备在搅拌时发泡性增强的乳清蛋白制品。可采用本领域已知的任何方法获得乳清蛋白。优选地,采用一种或多种干酪乳清的超滤、电渗析、蒸发脱水和反渗透的方法获得乳清蛋白。参见,例如U.S.专利:3,547,900和Horton等,Food Technol.,26:30(1972)。乳清来自可使用的任何乳酪,包括切达干酪(cheddar cheese)、瑞士硬干酪(Swiss cheese)、mozzarella干酪等。通常包含β-乳球蛋白和/或α-乳清蛋白的乳清蛋白制品可通过商业途径例如从Davisco(Le Sueur MN)、Bio-isolates PLC(Deeside,UK)、NZMP北美(SantaRosa CA)、Formost Farms (BARABOO WI)、MD Foods(Union NJ)和Avenmore WATERFORD(Monroe WI)处以乳清蛋白浓缩物(concertrates)(WPC)或乳清蛋白分离物(isolates)(WPI)的形式获得。在优选的实施方案中,乳清蛋白为乳清蛋白浓缩物。
本发明所使用的术语“磷脂酶”是指涵盖具有如本说明书所述针对磷脂的酶活性的酶。磷脂由在外位(sn-1)和中位(sn-2)被两分子脂肪酸酯化并在第三位被磷酸酯化的丙三醇组成;该磷酸相应地可被酯化为氨基醇。磷脂酶是参与磷脂水解的酶类。磷脂酶活性可分为几种类型,包括磷脂酶A1和磷脂酶A2,它们可水解一个脂肪酰基(分别在sn-1和sn-2位),形成溶血磷脂;而溶血磷脂酶,及磷脂酶B,则水解溶血磷脂中剩下的脂酰基。本说明说使用的术语磷脂酶包括磷脂酶A1、磷脂酶A2或磷脂酶B及其组合。
磷脂酶处理可通过一个或多个磷脂酶,如两个或多个磷脂酶,包括,但不限于同时使用A和B型、A1和A2、A1和B、A2和B或用两种同型而不同种类的磷脂酶进行处理。也包括仅用一种类型的磷脂酶处理乳清蛋白,所述磷脂酶例如A1、A2或B。在本发明的优选实施方案中,采用仅具有磷脂酶活性或基本上仅具有磷脂酶活性且其中的磷脂酶活生不是酶的副活性的酶来提供磷脂酶活性。
所述磷脂酶可以是任意源性的,例如源自动物(如,例如哺乳动物)、例如源自胰腺(如牛或猪的胰腺)、或源自蛇毒液或蜜蜂毒液。或者,磷脂酶可以是微生物源性的,例如源自丝状真菌、酵母或细菌,例如下述属或种:曲霉属,例如黑曲霉;网柄菌属(Dictyostelium),例如盘基网柄菌(D.discoideum);毛霉属,例如M.javanicus,M.mucedo,M.subtilissimus;链孢菌属,例如脉胞菌(N.crassa);根毛霉属,例如R.pusillus;根霉属,例如R.arrhizus,R.iaponicus,R.stolonifer;核盘菌属,例如S.libertiana;毛癣菌属,例如红色毛癣菌(T.rubrum);Whetzelinia,例如W.sclerotiorum;杆菌属,例如巨大芽孢杆菌(B.megaterium),枯草芽孢杆菌;柠檬酸杆菌属,例如弗氏柠檬酸杆菌(C.freundii);肠杆菌属,例如产气肠杆菌、阴沟肠杆菌(E.cloacae);爱德华菌属,如E.tarda;欧文菌属,例如E.herbicola;埃希杆菌属,例如大肠杆菌;克雷伯氏菌属,例如肺炎克雷伯氏菌;变形菌属,例如P.vulgaris;普罗威登斯菌属,例如P.stuartii;沙门菌属,例如鼠伤寒沙门氏菌;沙雷菌属,例如S.liquefasciens,S.marcescens;志贺菌属,例如福氏志贺氏菌;链霉菌属,例如S.violeceoruber,耶氏菌属,例如结肠耶氏菌。由此,磷脂酶可以是真菌性的,例如来自核菌类真菌,如镰孢菌种、如黄色镰孢菌、F.heterosporum、F.solani或F.oxysporum。磷脂酶还可来自丝状真菌菌株如曲霉属真菌,如Aspergillus awamori,Aspergillus foetidus、日本曲霉,黑曲霉或米曲霉。优选的磷脂源自镰孢属菌株,特别是尖孢镰孢,例如WO 98/26057中所述的DSM 2627菌株,特别是WO 98/26057的权利要求36和SEQ ID NO.2中所述的。在另外的实施方案中,磷脂酶是PCT/DK/00664中所公开的磷脂酶。
用于本发明方法的磷脂酶可以源自或获自本说明书所述的任何来源。本说明书中的术语“源自”是指已经从其天然存在的生物体中分离出来的酶,即酶的氨基酸序列与天然酶相同。术语“源自”还指在宿主生物体中重组制备的酶,重组制备的酶与天然酶相同,或含有修饰的氨基酸序列,例如含有一个或多个缺失的、***的和/或替代的氨基酸,即重组制备的酶是天然氨基酸序列的变体和/或片段,或者是通过现有技术中已知的核酸改组方法所制备的酶。天然酶的含义也包括自然变体。此外,术语“源自”包括通过例如肽合成方法所合成制备的酶。术语“源自”还包括在体内或体外通过例如糖基化、磷酸化等修饰的酶。本说明书中的术语“获自”是指具有与天然酶相同氨基酸序列的酶。该术语包括从其天然存在的生物体中分离出来的酶,或在同类型生物体或其它中重组表达的酶,或通过例如肽合成方法所合成制备的酶。关于重组制备的酶,术语“可获得的”和“源自”是指酶的身份,而不是指重组制备酶的宿主生物体的身份。
可采用任何适用的方法从微生物中获得磷脂酶。例如,可采用本领域中的已知方法发酵适用微生物然后从所得发酵培养液或微生物中获得磷脂酶酶制品。还可以采用重组DNA技术获得磷脂酶。所述技术通常包括培养用重组DNA载体转化的宿主细胞,所述重组DNA载体包含编码所需磷脂酶的DNA序列,且该DNA序列操作性连接于适用的表达信号,从而使其能在允许酶表达的条件下在培养基中表达磷脂酶,并从培养基中回收酶。所述DNA序列还可以整合到宿主细胞的基因组中。所述DNA序列可以是基因组来源、cDNA来源的或合成来源的或上述来源的任意组合,并可以根据本领域中已知的方法分离或合成。
适用的磷脂酶可从商业途径获得。在优选的实施方案中,磷脂酶为胰腺来源的磷脂酶A2,如Lecitase(Novozymes North America,INC.)。
磷脂酶还可以是纯化的磷脂酶。本说明书所使用的术语“纯化的”涵盖了不含源自磷脂酶所来源的生物体的组分的磷脂酶酶蛋白。术语“纯化的”还涵盖了不含来自磷脂酶所来源的天然生物体的组分的磷脂酶酶蛋白,此也被定义为“基本上纯化的”磷脂酶,且可特别指天然存在的磷脂酶以及没有经过基因修饰的,如通过删除、替代或***一个或多个氨基酸残基的磷脂酶。磷脂酶可以是纯化的,仅含少量的其它蛋白。术语“其它蛋白”特别涉及其它酶。本说明书所使用的术语“纯化的”还指除去存在于磷脂酶来源的细胞中的其它成分,特别是其它蛋白和更特别是其它酶。磷脂酶可以是“基本上纯的”,即不含来自制备所述酶的生物体即,例如用于重组制备磷脂酶的宿主生物体的其它成分。优选地,所述酶的纯度为至少75%(w/w),更优选至少80%,至少85%,至少90%,至少95%,至少96%,至少97%,至少98%,或至少99%。在另一优选实施方案中,磷脂酶的纯度为100%。
术语磷脂酶还包括酶催化活性所需要的所有辅助化合物,如,例如可天然存在或不存在于反应***中的合适的受体或辅因子。
磷脂酶可以用任何适用形式用于处理方法中,如采用干粉或颗粒、非尘颗粒(non-dusting granulate)、液态、稳定化液态、或保护酶的形式。颗粒可按照,例如US 4,106,991和US 4,661,452所公开的内容进行制备,并可任选地采用本领域已知的方法进行包衣。液态酶制品的稳定化可,例如,通过加入根据已有方法的稳定剂如糖、糖醇或其它多元醇、乳酸或其它有机酸而实现。保护性酶可根据EP 238,216中所公开的方法进行制备。
本发明方法中的酶处理可通过将磷脂酶分散于含有乳清蛋白水溶液中或在水中将乳清蛋白和磷脂酶混合并使得酶反应持续合适的时间并在合适的温度下发生的方法来实施。通过在含有乳清蛋白的水溶液中加入足以改进乳清蛋白制品发泡性的量的磷脂酶来获得反应混合物。根据本领域已知原理选择适用于所选酶的条件,实施磷脂酶处理。应理解为每一反应条件(如,例如蛋白底物的浓度、酶∶底物比率、pH、温度和时间)都可以根据例如乳清蛋白底物和/或酶的来源而改变。还应理解为可采用通过建立条件矩阵并测试矩阵中不同点的常规实验方法来优化反应条件。
磷脂酶的加入量为有效量。术语“有效量”是指足以实现本说明书所述所需改进的量。在本发明优选的实施方案中,制备包含蛋白浓度为1%~50%w/w,优选约5~40%,最优选约10~20%的乳清蛋白分离物或乳清蛋白浓缩物的水溶液。优选地,磷脂酶的加入量为约0.01~1.0%(w/w),基于脂肪(on fat basis),更优选为约0.02~0.2%(w/w),基于脂肪(假定酶制剂活性为10,000单位/g)。优选地,反应混合物在温度约为25-55℃更优选为40-50℃下孵育或反应。优选地,反应时间为约10-120分钟,更优选为10~60分钟。酶处理可在任何适用的pH下实施,如pH为5~9,更优选为6~8。
可采用分批发酵法,例如在搅拌罐中,或可以是连续,例如一连串搅拌釜反应器,或采用本领域已知的任何方法实施酶处理。
任选地,在酶处理后,除去或减少磷脂酶和/或灭活该酶。因此,在一些实施方案中,本发明方法包括灭活或除去磷脂酶地附加步骤。可采用本领域已知的任何方法实施灭活,所述方法包括,但不限于,将反应混合物的温度增高至超过约70℃以及将反应混合物的pH降低至低于约5.0;将压力增高至超过约6000bar;以及其它任何本领域已知的方法。可通过例如过滤或固定化,包括使用固定化酶除去磷脂酶。采用本领域任何已知的方法检测残余磷脂酶活性可用于检测磷脂酶的灭活或去除。
在一些实施方案中,本发明方法包括一个或多个通过如包括喷雾干燥和冻干的干燥方法以及采用例如脱水或膜过滤方法来实施的浓缩来处理乳清蛋白的附加步骤。
本发明提供了与未改性的乳清蛋白制品相比发泡性改进的改性乳清蛋白制品。增强的发泡性可用下面实施例2中所述内容进行测定。按照给定容积的溶液重量减去相同容积泡沫重量×100来确定发泡容积膨胀率。发泡容积膨胀率的增加可用于定义发泡能力的增加。典型地,本发明方法导致至少约800%的发泡容积膨胀率,优选至少1200%和最优选至少1500%,且增加的发泡能力至少2倍,优选至少5倍于未改性蛋白所表现出的发泡能力。
本发明还提供了与其来源的未改性的乳清蛋白制品相比发泡性增强的改性乳清蛋白制品。按照Philips等,J.Food Sci.55,no.4,1991以及下面实施例3中所描述的方法检测泡沫稳定性,并表示为泡沫起始重量的一半还原为液体(50%drainage)所需要的时间。在优选的实施例中,本发明的改性乳清蛋白制品的泡沫稳定性为至少10分钟,更优选为至少30分钟,最优选为至少60分钟。
根据本发明,改性乳清蛋白易于搅拌成为稳定的泡沫,由此能替代蛋清。因此乳清蛋白制品可用作生产需要高泡沫和稳定泡沫生成组分的多种食品中的组分,所述食品包括(但不限于)烤制品,如糕饼、搅打乳脂(whippedtoppings),糖霜、冻酸奶和奶油冻(mousse)。
具体实施方式
下述实施例只是用于举例说明本发明,而不意味着对本发明范围的限制。
而且,前述参考文件此处一并引入作为参考。
实施例1:冻干乳清蛋白浓缩物
包含78%蛋白的乳清蛋白浓缩物(WPC)(80%干基可溶性WPC,Leprino Foods)用于制备10%蛋白溶液。将一份溶液留作对照(不加入磷脂酶),用1.4LEU Lecitase 10L/g WPC(Novozymes North America,INC.)处理另一份溶液,剩余溶液用40LEU Lecitase 10L/G WPC进行处理。全部三组溶液加热至50℃,30分钟,然后冷却至室温,冰冻过夜。冰冻后,样品进行冻干处理直至形成细粉末。
实施例2:发泡和容积膨胀率的检测
采用150ml的5%上述未处理的和经处理的冻干乳清蛋白浓缩物的分散液以5分钟的间隔搅拌总计15分钟来检测容积膨胀率。将分散液调整为pH为7.00。
用Sunbeam Mastermixer 275Watts双头搅拌器搅拌来自实施1的5%冻干乳清蛋白浓缩物(FDWPC)分散物与5%蛋清蛋白粉末(未处理的)(Ballas Egg Products,用LECO测定含81.83%蛋白)分散物。根据制造商作出的针对蛋清泡沫的优化设置,Mastermixer的速率为11。将蛋白分散液(150mL)注入不锈钢钵中,以5分钟得间隔进行搅拌。在每个5分钟间隔后,停止搅拌器,将搅拌头小心取出以减少对泡沫的破坏。用刮片小心刮出泡沫样品,并将其置于两只预称重的舟皿中,快速用小勺将泡沫充满舟皿,并避免形成大气泡(large air pockets)。用刮片将泡沫顶端刮平,使用称重舟皿可以使每一检测中的体积恒定。记录重量,然后将泡沫放回钵中,继续搅拌。
容积膨胀率图可以反映与泡沫形成期间膜形成相关的整体蛋白相互作用(Phillips等1987),而还液(drainage)则显示了泡沫总体稳定性。用Lecitase10L处理的WPC与未处理的WPC相比,前者充分增加了容积膨胀率百分比(图1)。当使用量为1.4LEU Lecitase 10L/gWPC时,测得的容积膨胀率几乎等于蛋清蛋白测得得容积膨胀率。
实施例3:泡沫稳定性的检测
采用150ml上述未处理和经处理的FDWPC分散液进行总计15分钟的搅拌来检测泡沫稳定性。将分散液调整为pH为7.00。
为检测泡沫稳定性即还液,需要在搅拌钵上钻孔。在开始检测还液前用条带将孔覆盖。将蛋白分散液注入钵中。将钵,搅拌器和蛋白分散液称重,然后以速率11开始搅拌15分钟。搅拌完成时即用计时器开始计时。将钵,搅拌器和泡沫称重以便对搅拌期间丢失的水分定量。然后从钵上除去条带,将预称重的称重舟皿置于孔下。每5分钟测定排掉的水分的重量,记录50%还液量时的时间。
使用Lecitase 10L处理可以加强稳定性的检测。与未处理的FDWPC泡沫样品相比,在第一个5分钟内,平均还液量降低(图2)。未处理和经处理的样品在第二个5分钟内的平均还液量大致相同。这显示出对蛋白的处理确实可以降低10分钟内全部还液的重量。与蛋清蛋白泡沫相比,增加的稳定性并不能保持稳定。蛋清泡沫在观察的第一个10分钟内的还液几乎是可以忽略不计的,而在45分钟后才还液体全部溶液的50%。尽管用Lecitase10L处理的FDWPC泡沫不如蛋清泡沫稳定,然而其比对照组稳定。因此,与未处理的WPC相比,用Lecitase 10L处理WPC可以增强其泡沫容积膨胀率和泡沫稳定性。
实施例4:采用LECO检测蛋白
采用LECO检测FDWPC样品的含氮百分比。将含氮百分比乘6.38即得出蛋白百分比。
实施例5:
采用CEM检测水分(moisture)。
以15秒的间隔采用80%的功率测定FDWPC样品的水分,重量差别为0.2mg。
实施例6:采用Babcock法检测脂肪
检测20%FDWPC样品的脂肪(100g总溶液中20gWPC)。根据EUS-SM-0204检测乳制品中的脂肪的方法采用Babcock法实施检测。
表I显示了用10L Lecitase进行处理时,两组FDWPC的成分分析。四个样品的蛋白百分比,水分百分比和脂肪百分比在数值上是近似的,特别是脂肪百分数。所有采用FDWPC制备的溶液根据蛋白基百分比(w/w)而进行调整。因此,蛋白和脂肪在整个实验过程中可以保持恒定。
表I-FDWPC的成分分析
样品 | 蛋白百分比 | 水分百分比 | 脂肪百分比 | 总计 |
未处理的FDWPC(1) | 84.2 | 0.16 | 0.1 | 84.46 |
40LEULecitase 10L/gWPC FDWPC | 84.2 | 0.16 | 0.1 | 84.46 |
未处理的FDWPC(2) | 81.9 | 0.20 | 0.1 | 82.10 |
1.4LEULecitase 10L/gWPC FDWPC(2) | 83.3 | 0.18 | 0.1 | 83.58 |
Claims (20)
1.一种制备改性乳清蛋白制品的方法,包括用足以在搅拌乳清蛋白制品时可以增强乳清蛋白制品泡沫容积膨胀率和泡沫稳定性的量的磷脂酶处理乳清蛋白制品。
2.根据权利要求1的方法,其中所述乳清蛋白制品是乳清蛋白浓缩物的形式。
3.根据权利要求1的方法,其中所述乳清蛋白制品是乳清蛋白分离物的形式。
4.根据权利要求1的方法,其中所述方法包括将磷脂酶分散入含有乳清蛋白制品的水溶液中。
5.根据权利要求1的方法,其中所述磷脂酶为纯化的磷脂酶。
6.根据权利要求1的方法,其中所磷脂酶磷脂酶A。
7.根据权利要求1的方法,其中所述磷脂酶为磷脂酶A1。
8.根据权利要求1的方法,其中所述磷脂酶为磷脂酶A2。
9.根据权利要求1的方法,其中所述磷脂酶为磷脂酶B。
10.权利要求1的方法,其中所述磷脂酶为磷脂酶A1和A2的组合。
11.根据权利要求1的方法,其中所述磷脂酶为磷脂酶A和B的组合。
12.根据权利要求1的方法,其中所述磷脂酶选自磷脂酶A1、磷脂酶A2、磷脂酶B及它们的任意组合。
13.一种制备改性乳清蛋白制品的方法,包括
a)提供乳清蛋白水溶液;
b)在水溶液中加入磷脂酶以形成反应混合物;
c)孵育所述反应混合物以生成改性乳清蛋白制品,其中所述改性乳清蛋白制品与未处理的乳清蛋白相比,其发泡容积膨胀率和泡沫稳定性得到改进。
14.根据权利要求13的方法,还包括在所述c)之后的灭活磷脂酶的步骤。
15.根据权利要求13或14的方法,其中还包括干燥改性乳清蛋白制品的步骤。
16.根据权利要求13的方法,其中还包括浓缩改性乳清蛋白制品的步骤。
17.根据权利要求13的方法,其中所述乳清蛋白制品是乳清蛋白浓缩物的形式。
18.根据权利要求13的方法,其中所述乳清蛋白制品是乳清蛋白分离物的形式。
19.一种制备泡沫制品的方法,包括:
a)提供乳清蛋白水溶液;
b)在水溶液中加入磷脂酶以形成反应混合物;
c)孵育所述反应混合物以生成改性乳清蛋白制品,
d)将乳清蛋白制品搅拌为泡沫。
20.一种食品,包含通过权利要求1-19任一项的方法制备的改性乳清蛋白制品。
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EP (1) | EP1443825B1 (zh) |
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CN101959423B (zh) * | 2008-03-04 | 2014-10-15 | 森永乳业株式会社 | 乳清蛋白的改性方法 |
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ES2763652T3 (es) | 2013-06-27 | 2020-05-29 | Nestle Sa | Composiciones y productos nutricionales con mejor estabilidad de la emulsión |
FI127641B (en) | 2014-05-30 | 2018-11-15 | Valio Oy | Milk-based mousse and method for its preparation |
CA2980261A1 (en) | 2015-04-14 | 2016-10-20 | Dsm Ip Assets B.V. | Use of phospholipase c |
EP3300606A1 (de) * | 2016-09-28 | 2018-04-04 | DMK Deutsches Milchkontor GmbH | Aufschäumbare milchzubereitung |
EP3806648A1 (en) * | 2018-06-15 | 2021-04-21 | Roquette Freres | Non-vital wheat protein and its production process |
CN115517284B (zh) * | 2022-10-08 | 2023-10-03 | 青岛丹香投资管理有限公司 | 一种应用磷脂酶处理的鸡蛋液体制作蛋糕的方法 |
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ATE410065T1 (de) | 2008-10-15 |
US7897186B2 (en) | 2011-03-01 |
EP1443825B1 (en) | 2008-10-08 |
NZ532678A (en) | 2006-02-24 |
US20030124647A1 (en) | 2003-07-03 |
EP1443825A4 (en) | 2005-08-03 |
DE60229281D1 (de) | 2008-11-20 |
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