CN1909802B - 用酶漂白食物产品的新方法 - Google Patents
用酶漂白食物产品的新方法 Download PDFInfo
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- CN1909802B CN1909802B CN2005800021613A CN200580002161A CN1909802B CN 1909802 B CN1909802 B CN 1909802B CN 2005800021613 A CN2005800021613 A CN 2005800021613A CN 200580002161 A CN200580002161 A CN 200580002161A CN 1909802 B CN1909802 B CN 1909802B
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Abstract
本发明涉及一种生产食物产品的方法,其中,所述食物产品的中间产物形式包含色素,所述方法包括:加入至少一种酶,所述的酶有效于将所述色素直接转化为下述形式,所述形式能使食物产品的至少部分较之生产期间没有加入所述的酶的食物产品白度增加。本发明还涉及从本发明的方法获得的食物产品。
Description
本发明涉及制备具有增加的白度的食物产品的方法以及由此获得的食物产品。
在一些类型的食物产品中,食物产品的至少部分呈现白色看起来是人们所需要的,例如,奶制品中,例如,奶酪、乳清、黄油和奶粉,以及基于面粉的制品中,例如,面包和面条。
但是,此类食物产品的原材料或中间产物都包含色素,其能导致食物产品的米黄色至黄色。此类色素的例子是类胡萝卜素(胡萝卜素和叶黄质)和黄酮。
例如,在白面包中,白色的面包瓤是人们希望看到的属性。可以使用酶,例如,过氧化氢酶、过氧化物酶、脂肪酶和/或脂氧合酶来获得白色的面包瓤,参见例如by P.Gélinas等的‘Oxido-reductases and Lipases asDough-Bleaching Agent’,Gereal Chem,75(6),810-814(1998)。提到的所有酶对于面包瓤来说都有漂白作用。目前,面包烘焙业主要使用具有酶活性的大豆粉,其中含有脂氧合酶。大豆粉中的脂氧合酶能够漂白小麦面粉的色素,这是通过脂氧合酶对脂肪酸进行氧化期间形成的自由基和其它类型的活性氧作用的结果。该反应被称为共氧化。在大豆粉中,存在有三种脂氧合酶,L1、L2和L3,其中,L2和L3具有最好的漂白活性(W.Grosch,G.laskawy and F.Weber,J.Agric.Food Chem 24(1976),456)。大豆粉不仅含有脂氧合酶,其还含有对于漂白作用来说必需的脂肪酸,从而获得更好的漂白效果。
使用大豆作为脂氧合酶来源所伴随的一个缺点是,目前大多数大豆是经过遗传工程改造的(GMO)。因为世界范围内消费者偏好使用非GMO来源的面包改良添加剂,因此极为需要大豆脂氧合酶的替代品。除大豆脂氧合酶L2和L3之外的已知的酶具有缺点,它们的性能不如大豆脂氧合酶那么好。实践中,为获得理想的白色,这些酶需要与辅助因子或其它酶组合使用,以达到理想的面包瓤白度水平。过氧化物酶能非酶性催化通过分子氧的不饱和化合物(例如不饱和脂肪酸)的氧化过程(C.E.Eriksson et.al.JAOS 48(1971)442)。这些被氧化的脂肪酸产生出自由基,该自由基可能能以与脂氧合酶反应产物相似的方式,与面粉色素反应从而得到更少颜色的产品。
本发明的一个目的是提供一种新颖的食物产品,所述食物产品的至少部分具有增加的白度。该目的是通过一种用于生产食物产品的新方法来获得的,其中,所述食物产品的中间产物形式包含色素,所述方法包括:加入至少一种酶,所述的酶有效于将所述色素直接转化为下述形式,所述形式能使食物产品的至少部分较之生产期间没有加入所述的酶的食物产品白度增加。
能将色素直接转化为能增加白度的形式的酶在此处和下文中都被称为漂白酶。这些酶可以通过多种途径来发挥它们对于色素的直接漂白作用。例如,它们可以通过使色素中的不饱和键饱和(例如,通过氢化)来直接转化色素,或者它们可以直接切割色素,形成降解产物。“直接”这个术语表示,这些酶作用于色素,色素本身作为底物。为完成转化不特别排除使用辅助因子。
能直接切割色素的酶在此处和下文中被称为切割酶。根据本发明,合适的切割酶是能切割类胡萝卜素(胡萝卜素和叶黄质)和黄酮的酶。可通过两种不同的方式来切割类胡萝卜素,中心式和偏轴式的。对类胡萝卜素的中心式切割导致类维生素A(C20-化合物)的形成。偏轴式切割可以产生更为多样的化合物组,例如脱落酸。能对类胡萝卜素进行中心式切割的酶例如是β-胡萝卜素15,15’-加单氧酶(EC 1.14.99.36),其被描述于,例如,EP-A-1031623和J.Lintig和K Vogt(2000)J.Biol.Chem.275,11915中。该酶以前被称为β-胡萝卜素15,15’-加双氧酶=EC 1.13.11.21。
使用能进行中心式切割的酶的另一个好处在于类维生素A的形成。它们是视觉的必要组成部分。β-胡萝卜素被切割为两分子视黄醛。该视黄醛可被修饰为视黄醇,其也被称为维生素A。能对类胡萝卜素进行偏轴式切割的酶的例子是9-顺式-环氧类胡萝卜素加双氧酶(例如,X.Qin andJ.A.D.Zeevaart(1999),Proc.Nat.Acad.Science,96,15354)和β-胡萝卜素9’,10’-加双氧酶(例如,Kiefer et al.(2001),J.Bio1.chem.287,14110)。
食物产品的中间产物形式在本文中被定义为在生产过程中,获得食物产品的最终形式之前出现的任何形式。中间产物形式可以包含所用的单独原材料和/或其混合物和/或与添加剂和/或加工助剂的混合物,或者它们随后被加工出的形式。
酶以有效量加入。本领域技术人员通过改变酶剂量及测量色素降解和/或最终食物产品的白度增加,能够容易地确定该有效量。当酶能够转化β-胡萝卜素时,酶的有效量可以表示为β-降解单位的形式(例如Aziz或Zorn单位-见材料和方法)。
食物产品可以从至少一种植物来源的原材料,例如小麦面粉制得。后者已知含有色素,例如,类胡萝卜素(胡萝卜素和叶黄质)和黄酮,其会影响到例如烘焙的面包瓤的颜色。或者,这些色素可能来自植物原材料之外的其它来源,例如,来自奶。类胡萝卜素的例子还包括具有胡萝卜素主链的物质,特别是具有β-胡萝卜素或辣椒黄素主链的,更特别地,α-或β-胡萝卜素、叶黄素、番茄红素、花药黄质、辣椒黄素、玉米黄质、紫黄质、虾青素、角黄素、luteoxanthin、新黄质和各种apo-类胡萝卜素。
用于本发明方法的优选的食物产品是烘焙面包和由小麦面粉和/或其它谷物来源的面粉得到的其它烘焙产品。
例如,对于烘焙的食物产品面包而言,中间产物形式包括,例如,小麦面粉、其与其它面包成分(例如,水、盐、酵母和面包改良组合物)的最初的混合物、混合的面团、揉捏过的面团、发酵后的面团以及部分烘焙的面团。当酶能够转化β-胡萝卜素时,将酶以能提供每kg面粉1至5000个Zorn单位、优选每kg面粉5至1000个Zorn单位、更优选每kg面粉10至500个Zorn单位、以及最优选每kg面粉25至250个Zorn单位的量,加入到小麦面粉和/或来自其它谷物来源的面粉中,或者加入到具有其它面包成分的最初的混合物中。酶还可以与面包改良剂混合物一起或作为其一部分加入,所述混合物混合有本领域已知的其它面团和/或面包改良加工助剂,例如,本领域已知的一种或多种酶(例如,淀粉分解酶,如α-淀粉酶、β-淀粉酶、淀粉葡萄糖苷酶、保鲜(anti-staling)麦芽糖α-淀粉酶,脂肪分解酶,如脂肪酶、磷脂酶、乳脂酶,氧化酶,如葡萄糖氧化酶、己糖氧化酶、漆酶、吡喃糖氧化酶、碳水化合物氧化酶,半纤维素分解酶,如木聚糖酶、阿拉伯呋喃糖苷酶,纤维素分解酶,如内葡聚糖酶(例如,纤维素酶)、纤维二糖水解酶(cellobiohydrolase),蛋白酶和/或本领域已知的化学加工助剂,例如,还原剂和氧化剂(例如,抗坏血酸、谷胱甘肽),乳化剂(例如,DATEM)等。
在一些类型的面条中,白色产品被认为是人们想要的。例如,对于面条而言,中间产物形式包含,例如,小麦面粉,与水、盐和其它面条成分的最初混合物,混合的面团和最终的面条产品,它们可以是新鲜的、经过干燥的、煮过的、蒸过的和/或煎过的。
食物产品还可以是奶制品。奶制品指基于干燥固体而言含有至少10wt%、优选至少30wt%、更优选至少50wt%、进一步更优选至少70wt%或者最优选至少80%的来自奶的组分,优选来自牛奶。来自奶的组分例如是脂肪、蛋白质,例如乳清奶酪凝乳和酪蛋白等。奶,尤其是牛奶,可以天然含有上色化合物,例如类胡萝卜素,例如,β-胡萝卜素。
白色对于例如奶酪、黄油、奶粉或乳清制品来说是非常重要的。例如,对于Feta、Mozzarella、Ricotta等奶酪和蓝奶酪(例如Danish Blue、Roquefort或Gorgonzola)而言,白色被认为是人们需要的。在其中山羊或绵羊奶被牛奶至少部分取代的奶酪中,奶酪的白度可能会成为问题,因为,牛奶中存在β-胡萝卜素。
对于一些奶酪而言,天然的上色剂,例如胭脂或β-胡萝卜素被用作为食物的上色剂。但是,该上色剂将还可能存在于乳清中。当该乳清进一步被加工为例如婴儿配方的时候,乳清制品的颜色就是人们所不想看到的了。对于食物产品软奶酪来说,中间产物包含,例如,奶和奶酪凝乳。
酶可以作为酶制剂加入,或者通过能生产出所述酶的微生物原位产生。酶制剂可以从多种来源获得,例如,从植物、动物和微生物。优选地,酶制剂获得自微生物,因为微生物使得按照可控制的方式以工业规模获得酶成为可能。从微生物获得的酶制剂可通过对选定的微生物菌株进行经典的发酵方法来获得,或者通过对过量表达该酶的微生物进行发酵来获得。微生物可以是细菌、真菌或酵母。合适的微生物的例子是Microcystis、Lepista(例如L.irina)、Cyathus(例如,C.pallidus)、Ganoderma(例如,G.applanatum)、Ischnoderma(例如,I.benzoinum)、Marasmius(例如,M.scorodonius)、Trametes(例如,T.suaveoluens或T.versicolour)、Cryptococcus(例如,C.laurentii)、Hypomyces(例如,H.odoratus)或Phaffia(例如,P.rhodozyma)、Phanerochaete(例如,P.chrysosporium)、Lentinula(例如,L.edodes)、Coprinus(例如,C.cinereus)、Gloeophyllum(例如,G.trabeum)、Ophiostoma(例如,O.piliferum)、Aspergillus(例如,A.niger、A.oryzae、A.nidulans)、Thermomyces(例如,T.lanuginosa)、Sporotrichum(例如,S.thermophile)、Aureobasidium(例如,A.pullulans)、Amorphotheca(例如,A.resinae)、Leucosporidium(例如,L.scottii)、Cunninghamella(例如,C.elegans)。
对产品白度的测量可以通过视觉观察来进行,或者通过对反射的测量来进行,例如通过扫描。在反射测量中,通过三个参数来对颜色定量:L-因子(黑=0,至白=100),a-因子(绿=-60至红=+60)以及b因子(蓝=-60至黄=+60)。在类胡萝卜素的情况下,生产出的产品的b-因子优选尽可能接近于0,优选在10至0之间,更优选在5至0之间,进一步更优选低于1,最优选要小于0.5。
在第二个方面,本发明提供了可通过前文所述的本发明的方法获得的食物产品。这些食物产品的特征在于,较之可通过不包含加入一种或多种能转化中间产物中的色素的酶的生产方法获得的食物产品而言,至少部分具有显著增加的白度。
在另一个方面,本发明提供了能转化色素的酶在漂白食物产品中的用途,例如漂白基于面粉的产品或从奶获得的产品。令人惊奇地,我们发现,在家用去垢剂中,这些酶可被有利地用作为除渍剂。具体而言,已证明所述的酶非常有效于去除带色污渍,例如,棉织物和合成(例如,聚酯)织物的草渍、咖啡或茶渍。此外,这些酶还可用于用酶进行的石漂洗工艺,例如,将蓝牛仔裤的靛蓝染料漂至想要的水平。
材料和方法
测量β-胡萝卜素的转化
根据Aziz测量β-胡萝卜素的降解
可以按照A.Ben Aziz(1971),Phytochemistry 10,1445所述,通过β-胡萝卜素的转化活性来测量酶活。在此,一个酶单位被定义为每分钟能转化1微克β-胡萝卜素的酶的量(下文中被称为Aziz单位)。
根据Zorn来测量β-胡萝卜素的降解
还可以按照Zorn et al.(2003),Appl.Microbiol.Biotechnol.62:331-336,通过β-胡萝卜素的转化活性来测量酶活。在此,一个酶单位被定义为每分钟能转化1微摩尔β-胡萝卜素的酶的量(下文中被称为Zorn单位)。试验按照如下程序来进行:在比色皿中,于27℃,对1.5ml含有酶的样品进行5分钟的预孵育,然后加入100μl的β-胡萝卜素贮液(见下文)。如果必要的话,用pH5.5的柠檬酸/磷酸盐缓冲液来稀释浓缩的培养物上清液(该缓冲液通过将43 ml0.1M柠檬酸与56ml 2M Na2PO4溶液混合来制备)。在处于控温容器中使用分光光度计,在27℃下,450nm处,对吸光度的降低进行15分钟的监测。检查曲线的线性度,根据如下公式,选用曲线的线性部分来计算酶活:
酶活[mU/ml]=(ΔE×Vt)×106/(Vs×d×ε)
其中,U=上面定义的酶活单位;ΔE=450nm处吸光度每分钟的降低;Vt=比色皿内的总体积(ml);Vs=比色皿内的样品体积(ml);ε=β-胡萝卜素的消光系数,其为95,000M-1·cm-1;d=比色皿的厚度(em)。
通过用Aziz单位除以β-胡萝卜素的分子量(=536.85),可以将Aziz酶单位转化为Zorn单位。
制备β-胡萝卜素贮液
按照下述程序来制备β-胡萝卜素贮液:将5mgβ-胡萝卜素和500mgTween-80溶于500ml二氯甲烷。在40℃和800mbar下,于旋转式蒸发器中蒸发二氯甲烷。当几乎所有二氯甲烷都蒸发之后,加入30ml水,在旋转式蒸发器中,最终在氮气流中除去剩余的二氯甲烷。对得到的溶液进行过滤,在容量瓶中用水定容至50ml。该溶液必须贮藏于冷藏条件(冰箱),仅可稳定数天。
漂白食物产品
在按照Gelinas,Cereal Chem.75,810-184(1998)所述从面包瓤或面团中提取类胡萝卜素之后,来对漂白加以测定。如Gelinas(1998)所指明的,通过从面包瓤中提取的中的脂肪来测定类胡萝卜素。
可以通过视觉和通过反射测量来测定食物产品的白度。可以通过对加入了漂白酶的食物产品和没有加入漂白酶的对照进行比较,来进行视觉判断。反射测量可以通过在色彩扫描仪(Hewlett Packard Scanjet ADF)上对食物产品进行扫描来实施。用LabSMART程序(LabSMART,LLC,LoganUtah,USA)来分析这些数据。
实施例1 培养和测定从Marasmius scorodonius中获得的β-胡萝卜素转化 酶的活性
对从Marasmius scorodonius中获得的β-胡萝卜素转化酶进行的培养和活性测定按照Zorn et al.(2003)来进行。就此而言,用来自Marasmiusscorodonius的培养收集物的菌丝体(可从Centraal Bureau voorSchimmelcultures-Utrecht,The Netherlands,保藏号CBS 850.87得到)对补充有乳化的β-胡萝卜素的琼脂平板进行接种。在24℃对这些平板进行14天的培养。用菌丝体接种300ml的摇瓶,其中含有100ml标准营养溶液(SNL,含有30g/升的葡萄糖H2O;4.5g/升的天门冬酰胺H2O;1.5g/升的KH2PO4;0.5g/升的MgSO4;3.0g/升的酵母提取物;1ml/升的灭菌痕量元素溶液,其中含有5mg/l的CuSO4 *5aq、80mg/l FeCl3 *6aq、90ml/l ZnSO4 *7aq、30mg/l MnSO4 *l aq和40mg/l EDTA;灭菌之前用1NNaOH将pH调节为6.0),摇瓶在150rpm的振荡培养器中于24℃被培养7天。检查预培养物,确定没有微生物污染存在,用Ultra Turrax进行均化,将它们用于接种主培养物(在500ml Erlenmeyer瓶中,250mL)。从第二天起,每天取2ml样品,离心以移走菌丝体,以分光光度试验的方式来测量活性。4天的培养之后,β-降解活性为每升不含细胞的上清液中大约0.3个Zorn单位。
实施例2和比较实施例A、B及C 幼面包块(pup loaf)烘焙试验
在标准的烘焙过程中,由200g小麦面粉(160g小麦面粉(Kolibri-Meneba,荷兰)和40克小麦面粉(1bis-Menaba,荷兰)的混合物)、1.4g Fermipan干酵母(DSM Bakery Ingredients,Delft,荷兰)、4g盐、50ppm抗坏血酸、4ppm真菌α-淀粉酶BakezymeP500(DSM FoodSpecialties,Delft,荷兰)、60ppm真菌半纤维素酶BakezymeHS2000(DSM Food Specialties,Delft,荷兰),以及如表1所示的量的β-胡萝卜素降解酶和116ml水,在销式混合器(pin mixer)中处理6分钟15秒来制备幼面包块。面团温度为28℃。混合后,面团被直接分为两块每块150g,揉圆,在醒发(proofing)室中于30℃进行醒发,成型并放入盘中。最后再在30℃进行70分钟的醒发,在225℃下对面团进行20分钟的烘焙。
在室温贮藏于密封盒中24小时后,由烘焙师来评价经烘焙的面包瓤的品质和颜色;对面包瓤进行提取之后来测定类胡萝卜素的含量,如表2所示。
表1酶剂量(表示为每200克面粉的Zorn单位)
酶的形式 | 试验 | 面包块A | 面包块B | 面包块C | 面包块1 |
具有酶活的大豆粉 | Aziz | - | 18.6 | - | - |
大豆脂氧合酶2 | Aziz | - | - | 18.6 | - |
Marasmiusscorodonius | Zorn | - | - | - | 18.6 |
表2面包块的类胡萝卜素含量和视觉鉴定
面包块A | 面包块B | 面包块C | 面包块1 | |
存在的类胡萝卜素% | 100 | 8 | 30 | 5 |
视觉观察 | 黄 | 白 | 黄 | 白 |
从表2可以推断出,通过向面团中加入根据本发明的漂白酶,类胡萝卜素会被降解,导致面包瓤更白。根据本发明的方法的效率好于所用的大豆脂氧合酶2,与具有酶活性的大豆粉的作用至少相当或更好。
实施例3制备微型奶酪
通过Shakeel-Ur-Rehman et al.所述(Protocol for the manufacture ofminiature cheeses in Lait,78 (1998),607-620)来制造微型奶酪。通过在63℃加热30分钟对原始牛奶进行巴氏灭菌。将经过巴氏灭菌的奶转移到广口塑料离心瓶中(每瓶200mL),冷却至31℃。随后,向离心瓶中的每200ml的经巴氏灭菌的奶中加入0.72ml起始培养物DS 5LT1(DSMGist B.V.,Delft,荷兰),让奶熟化20分钟。然后,加入CaCl2(每200mL熟化的奶中加入132μL 1mol.L-1的溶液),随后加入凝结剂(每ml0.04IMCU)。当实验涉及使用漂白酶I或II时,该酶与凝结剂一起加入。
在31℃将奶溶液保持40-50分钟,直到形成凝块。通过张紧线切割器,在架子上以1cm的间隔,手工切割凝块。可以进行2分钟的恢复,然后轻微搅拌10分钟。之后,在30分钟内,在对凝乳/乳清混合物的持续搅拌下,将温度逐渐升至39℃。达到pH6.2后,在室温下,于1,700g对凝乳/乳清混合物进行60分钟的离心。乳清被排走,将凝乳保持于36℃的水浴下。每15分钟将奶酪颠倒一次,直到pH降至5.2-5.3,然后在室温下于1700g离心20分钟。再次排走乳清之后,通过扫描对奶酪漂白进行测定。漂白酶I和II的使用获得了更白的奶酪。
Claims (6)
1.生产食物产品的方法,其中,所述食物产品的中间产物形式包含色素,所述方法包括:加入至少一种酶,所述酶有效于将所述色素直接转化为下述形式,所述形式能使所述食物产品的至少部分较之生产期间没有加入所述酶的食物产品白度增加,其中所述色素是类胡萝卜素,并且其中所述酶是从蒜头状小皮伞(Marasmius scorodonius)的培养物获得的。
2.如权利要求1所述的方法,其中所述食物产品由面粉制得。
3.如权利要求1所述的方法,其中所述食物产品由小麦面粉制得。
4.如权利要求1所述的方法,其中,所述食物产品是乳制品。
5.如权利要求1至4中任意一项所述的方法,其中,所述酶作为从蒜头状小皮伞获得的酶制剂被添加,或者通过能生产所述酶的蒜头状小皮伞原位产生。
6.能将类胡萝卜素直接转化为使得食物产品的至少部分白度增加的形式的酶的用途,其中所述酶是从蒜头状小皮伞(Marasmius scorodonius)的培养物获得的。
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Patent Citations (1)
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CN1244588A (zh) * | 1999-07-21 | 2000-02-16 | 董春明 | 一种马铃薯淀粉的微生物脱色净化法 |
Non-Patent Citations (2)
Title |
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P.Gelinas, E. poitras, C. M. McKinnon, A. Morin.Oxido-Reductases and Lipases as Dough-Blenching Agents.Cereal Chemistry75 6.1998,75(6),810-814. |
P.Gelinas, E. poitras, C. M. McKinnon, A. Morin.Oxido-Reductases and Lipases as Dough-Blenching Agents.Cereal Chemistry75 6.1998,75(6),810-814. * |
Also Published As
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US9198452B2 (en) | 2015-12-01 |
AU2005204455A1 (en) | 2005-07-28 |
JP4602355B2 (ja) | 2010-12-22 |
AR047413A1 (es) | 2006-01-18 |
CA2551776A1 (en) | 2005-07-28 |
EP1703808B1 (en) | 2011-03-16 |
WO2005067735A2 (en) | 2005-07-28 |
WO2005067735A3 (en) | 2005-11-24 |
DK1703808T3 (da) | 2011-06-14 |
CN1909802A (zh) | 2007-02-07 |
US20090175989A1 (en) | 2009-07-09 |
EP1703808A2 (en) | 2006-09-27 |
AU2005204455B2 (en) | 2010-06-24 |
CA2551776C (en) | 2012-09-25 |
JP2010159424A (ja) | 2010-07-22 |
DE602005026903D1 (de) | 2011-04-28 |
JP2007518406A (ja) | 2007-07-12 |
EA011582B1 (ru) | 2009-04-28 |
US20120288919A1 (en) | 2012-11-15 |
ATE501646T1 (de) | 2011-04-15 |
BRPI0506742B1 (pt) | 2014-09-30 |
ZA200605712B (en) | 2008-02-27 |
EA200601310A1 (ru) | 2006-12-29 |
EP2316280A1 (en) | 2011-05-04 |
ES2361641T3 (es) | 2011-06-20 |
IL176677A0 (en) | 2006-10-31 |
BRPI0506742A (pt) | 2007-05-15 |
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