CN101090644A - 肉制品或水产糜制品及其制造方法 - Google Patents
肉制品或水产糜制品及其制造方法 Download PDFInfo
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- CN101090644A CN101090644A CNA2006800015034A CN200680001503A CN101090644A CN 101090644 A CN101090644 A CN 101090644A CN A2006800015034 A CNA2006800015034 A CN A2006800015034A CN 200680001503 A CN200680001503 A CN 200680001503A CN 101090644 A CN101090644 A CN 101090644A
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Abstract
向含有肌肉蛋白质的食材中添加蛋白质脱酰胺酶,使该酶与肌肉蛋白质发生作用,从而得到优质的食品。
Description
技术领域
本发明涉及使用蛋白质脱酰胺酶的肉食肉制品或水产糜制品及其制造方法。
背景技术
人类利用以家畜、家禽为主体的哺乳类或鸟类的骨骼肌组织所代表的肉食、作为鱼类骨骼肌组织的鱼肉、其他脊椎或无脊椎动物的机体组织或器官等作为维持生命所必需的蛋白质供应源。上述动物性蛋白质食品不论起源如何,都含有肌动蛋白、肌球蛋白等共同的肌肉蛋白质,这些蛋白质在食品中表现出共同的加工特性。例如,肌肉蛋白质的功能特性可以列举出:保水性、粘结性、弹性、凝胶化性等。上述特性有助于向香肠或鱼糕等糜制品中混入脂肪或水分,或者赋予肉块接合型制品粘结性或凝胶化性等。上述具有各种功能特性的肌肉蛋白质一般通过加热、冷冻、冷藏、加压等加工处理而发生变性。肌肉蛋白质的变性引出肉本身的香味而赋予美味,另一方面不仅产生加工方面的不良问题如从肉组织流出汁水或随之而来的产率下降等,而且由于原料而给感官方面带来不良影响如肉质***、柔嫩度被破坏、食感变得松散等。例如,在肉食中烹调牛排或カッフラィ等较大块的肉(肉片)时,柔软或多汁是味美的重要要素,但这种肉具有因加热烹饪而***的性质,同时肉汁也趋于流失。另外,蒸鱼糕等水产糜制品若加热过度,则食品过度硬化,柔嫩度被破坏,脱水也趋于增加。
一直以来,已知采用使用有机酸单甘油酯的方法(日本特开昭49-20353号公报)、使用卵磷脂等表面活性剂的方法(日本特开平4-148663号公报)、使用盐类等的方法(日本特开平4-36167号公报)和使用酶的方法(日本特开平4-278063号公报)来抑制由加工处理引起的肉的硬化。作为赋予水产糜制品以柔嫩度的方法,已知将转谷氨酰胺酶和碱金属盐结合使用的方法(日本特开平8-80176号公报)。另外,通过添加多磷酸盐或糖类来解决因加工处理引起的肉的保水能力下降以及产率降低的问题已众所周知。多磷酸盐具有使作为肌肉蛋白质的肌球蛋白和肌动蛋白解离的作用,对于提高肉制品的粘结性和产率具有显著效果,但由于担心阻碍钙的吸收作用等,从消费者的角度考虑也强烈要求排除聚合磷酸盐。此外,采用使转谷氨酰胺酶起作用的方法(日本专利第2630829号)、使用经凝乳酶分解的酪蛋白碱盐和钙离子的混合水溶液的方法(日本特开平3-94624号公报)、使含有氯化钠和淀粉的液体被肉食吸收的方法(日本特开平6-343424号公报)等来改善肉食、鱼肉加工品的保水性或凝胶化性。关于蛋白质脱酰胺酶在肉制品、水产糜制品中的应用,已知向香肠中添加利用蛋白质脱酰胺酶进行脱酰胺化的大豆蛋白质的方法(日本特开2000-50887号公报)。这样,对于由肌肉蛋白质的变性而引起的食品加工中的各种问题,虽然对每种情况都采取了各种解决方法,但是近来消费者需求多样化,上述对策还很难说是充分的。
尚需说明的是,日本特开2000-50887号公报中记载着蛋白质脱酰胺酶作用于肌球蛋白、肌动蛋白等肉蛋白质,但只记载着蛋白质脱酰胺酶对肉蛋白质的反应性,关于使该酶与含有肌肉蛋白质的原料作用的效果并没有具体记载。即,日本特开2000-50887号公报中公开的技术提高了食材中添加的分离蛋白质的功能性(可溶性、分散性、起泡性、泡沫稳定性、乳化性、乳化稳定性等),关于下述的本申请发明的效果,即针对肉制品、水产糜制品,提高其加热后的产率、抑制保存中脱水的效果、改善食感使之顺滑、柔嫩且柔软的效果既没有记载也没有暗示。在日本特开2000-50887号公报中,作为原料添加的脱酰胺化大豆蛋白质在最终制品中仅含极少量,而且该蛋白质是在80℃下加热处理30分钟得到的,因此酶失活、在香肠中该酶对肉蛋白质并不起作用,在这方面也与本发明的制造方法有所区别这当然是不言而喻的。
发明内容
本发明提供可以抑制含有肌肉蛋白质的食品因加工(加热、冷冻、冷藏等)、保存中产生的该蛋白质变性而引起的产率下降、脱水,保持柔嫩且柔软的食感,抑制味道、风味劣化的食品和上述食品的制造方法。
鉴于上述课题,本发明人等进行了深入研究,结果发现:通过向含有肌肉蛋白质的食材中添加蛋白质脱酰胺酶并使该酶与肌肉蛋白质发生作用可以解决上述课题,从而完成了本发明。即,本发明内容如下。
1.肉制品或水产糜制品的制造方法,其特征在于:向含有肌肉蛋白质的食材中添加蛋白质脱酰胺酶,使该酶与该肌肉蛋白质发生作用。
2.上述1的方法,其特征在于:肌肉蛋白质为来源于畜肉、鸟肉、鱼肉、软体动物或甲壳类的肌肉蛋白质。
3.上述1或2的方法,其特征在于:相对于1g食材而言蛋白质脱酰胺酶的添加量为0.01~100单位。
4.肉制品或水产糜制品,其特征在于:其是通过上述1至3中任一项的方法得到的。
5.肉食软化剂,其特征在于:该肉食软化剂含有蛋白质脱酰胺酶。
本发明中的蛋白质脱酰胺酶具有直接作用于蛋白质的酰氨基进行脱酰胺而不伴有肽键断裂和蛋白质交联的作用。只要具有该作用即可,对其种类没有特别限定。这种酶的例子有日本特开2000-50887号公报或日本特开2001-21850号公报中公开的酶,但并不特别受限于此。蛋白质脱酰胺酶可以使用由产生蛋白质脱酰胺酶的微生物培养液制备的酶。对蛋白质脱酰胺酶的制备中使用的微生物没有特别限定。
关于由微生物培养液制备蛋白质脱酰胺酶的方法,可以使用公知的蛋白质分离、纯化方法(离心、UF浓缩、盐析、使用离子交换树脂等的各种层析法等)。例如,将培养液离心除去菌体,之后组合盐析、层析法等可以得到目标酶。当从菌体内回收酶时,例如通过加压处理、超声波处理等将菌体破碎,之后按照与上述同样的方法进行分离、纯化,可以得到目标酶。尚需说明的是,可以通过过滤、离心处理等事先从培养液中回收菌体,之后再进行上述一系列的工序(菌体的破碎、分离、纯化)。可以通过冷冻干燥、减压干燥等干燥方法将酶粉末化,此时可以使用适当的赋形剂、干燥助剂。
本发明的蛋白质脱酰胺酶的活性按照将日本特开2000-50887号公报记载的方法改良后的方法、即下述方法来测定。
(1)向100μl含30mM Z-Gln-Gly的176mM磷酸缓冲液(pH6.5)中添加10μl含蛋白质脱酰胺酶的水溶液,在37℃下温育10分钟后,加入100μl 12%TCA溶液终止反应。
(2)此时,用20mM的磷酸缓冲液(pH6.0)进行适当稀释,使酶浓度达到0.05mg/ml,离心(12000rpm,4℃,5分钟)后利用F-kit氨(Roche制)测定上清液中的NH3量。
(3)向100μl试剂II液(F-kit附属品)中加入10μl上清液和190μl 0.1M的三乙醇胺缓冲液(pH8.0),在室温下放置5分钟后使用100μl来测定340nm下的吸光度。向剩下的200μl加入1.0μl试剂III(F-kit附属品,谷氨酸脱氢酶)后再在室温下放置20分钟,之后测定剩下的200μl在340nm下的吸光度。使用F-kit附属的氨标准液作成的表示氨浓度和吸光度(340nm)变化量的关系的标准曲线,由该曲线求出反应液中的氨浓度。
(4)蛋白质浓度的测定使用蛋白质分析CBB(考马斯亮蓝)溶液(ナカラィテスク制)在检测波长595nm下进行测定。使用BSA(Pierce)作为标准。
(5)通过下式求出蛋白质脱酰胺酶的活性。
比活性(U/mg)=(反应液中的氨浓度(μmol/ml)×反应液量(ml)×酶稀释率)÷(酶量(ml)×蛋白质浓度(mg/ml)×反应时间(min))
本发明中的肌肉蛋白质为:存在于肌纤维中的肌浆蛋白、与肌肉收缩有关的肌原纤维蛋白或存在于***中的***蛋白质。肌浆蛋白是细胞质可溶性蛋白质,其例子有:含有与糖酵解***相关的大部分酶的白蛋白、肌红蛋白等。肌原纤维蛋白的例子有:作为主要构成成分的肌球蛋白、肌动蛋白、肌动球蛋白、原肌球蛋白、肌钙蛋白、肌联蛋白等。***蛋白质的例子有:作为主要构成蛋白质的骨胶原、弹性蛋白。该肌肉蛋白质通过各种加工等处理成为变性的原料、例如使骨胶原变性而得到的明胶等也包含在本发明的含有肌肉蛋白质的食品原料中。
含有肌肉蛋白质的食材是指例如畜肉、鸟肉、鱼肉或软体动物或甲壳类的肌肉、所谓的肉,是指除骨、牙齿、爪以外的包括肌肉、脂肪、血液、腱、内脏、髓、脑的部位。具体为来源于下述动物的肉:牛、猪、羊等畜产动物;鸡、野鸭、鸵鸟等鸟类;沙丁鱼、金枪鱼、鲑鱼、鳕鱼等鱼类;章鱼、墨鱼等软体动物;蟹、虾等甲壳动物;鳄鱼、蛇等爬行类;蛙等两栖类,本发明中使用的原料不论任何种类均可。
用上述食材加工的肉制品可列举如:火腿、香肠、叉烧肉、肉丸子、汉堡包、炸肉丸(ミ-トロ-フ)、肉糕、烤牛肉、烤猪肉等,还包括:分割肉食;经煮、烤等加热加工的肉食;经过酶或机械软化处理的肉食。水产糜制品可列举出:磨碎的鱼肉、鱼糕、蟹糕、鱼肉山芋丸子、鱼卷、炸鱼糕、氽鱼丸子、鱼肉火腿、鱼肉香肠、鱼丸等,只要是由肉蛋白质制成的制品即可,对其种类没有限定。
向食材中添加蛋白质脱酰胺酶的方法为:当为香肠、鱼糕等糜制品时,可以在将食材切细、磨碎、糊化的过程中将酶液或酶粉末单独或与调料等其他原料一起添加,也可以在糊化后将酶液或酶粉末单独或与调料等其他原料一起添加。当为火腿等时,可以将酶液注入到原料肉中,也可以将原料肉浸在酶液中。还可以将酶液或酶粉末撒在原料肉上。添加酶的方式可以是将酶粉末与粉末原料事先混合来使用,也可以将酶溶解在调味液等液体原料中来使用。
相对于1g食材即1g原料肉,蛋白质脱酰胺酶的添加量优选0.01~100单位,更优选0.1~10单位。对蛋白质脱酰胺酶的反应条件(反应时间、温度、反应体系的pH等)没有特别限定,优选的反应温度为5~70℃。反应体系的pH优选2~10,更优选为4~8,进一步优选为pH5~8。反应时间优选10秒~5天,更优选为10分钟~24小时。上述条件可以根据使用的酶的纯度或食材中含有的蛋白质的种类或状态、纯度等适当变更或调节。
实施发明的最佳方式
以下列举实施例来更详细地说明本发明。本发明并不受该实施例的任何限制。
实施例1
本实施例中,蛋白质脱酰胺酶使用来源于金黄杆菌属(Chryseobacterium)的蛋白质谷氨酰胺酶。来源于解朊金黄杆菌(Chryseobacterium proteolyticum)株的蛋白质谷氨酰胺酶(EC.3.5.1)基因的序列已经确定[Eur.J.Biochem.268.1410-1421(2001)]。以该序列为参考,进行向谷氨酸棒杆菌(Corynebacterium glutamicum)中使用频率高的密码子的变换,构建序列号1所示的基因序列。该序列包括蛋白质谷氨酰胺酶的信号序列(pre部分)和pro部分以及成熟型蛋白质谷氨酰胺酶的编码区。通过合成来制作全基因序列。以构建的序列号1的基因序列信息为基础,合成序列号5(5’-CATGAAGAACCTTTTCCTGTC-3’)和序列号6(5’-GTAAAAGGATCCATTAATTAAAATCC-3’)所示序列的引物。序列号5所示的引物包括蛋白质谷氨酰胺酶的信号序列的N末端序列,序列号6所示的引物包括成熟型蛋白质谷氨酰胺酶的C末端和BamHI的识别序列。以具有序列号1所示序列的DNA为模板,使用序列号5和序列号6所示序列的引物进行PCR,扩增蛋白质谷氨酰胺酶的pro部分和成熟型蛋白质谷氨酰胺酶的编码区。将该PCR片段***到日本特开平9-070291号公报记载的pVC7的SmaI部位后,导入到大肠杆菌(E.coli)JM109的感受态细胞(宝酒造公司制)中。取得保持克隆有蛋白质谷氨酰胺酶基因的质粒的菌株,回收质粒。测定该质粒中克隆片段的碱基序列,确认与序列号1所示序列一致。
来源于大肠杆菌的包括TorA信号肽的TorA基因序列已经确定(Mol.Microbiol.11:1169-1179(1994))。以该序列为参考,合成序列号7(5’-ATGAACAATAACGATCTCTTTCAGG-3’)和序列号8(5’-CCGGATCCTGGTCATGATTTCACCTG-3’)所示的引物,以按照常规方法(齐藤、三浦的方法[Biochim.Biophys.Acta,72,619(1963)])制备的大肠杆菌W3110株的染色体DNA为模板,通过PCR法扩增TorA编码区和位于其上游的包括信号序列的区域。PCR反应中使用PyrobestDNA聚合酶(宝酒造公司制),反应条件采用本领域技术人员推荐的方案。应说明的是,序列号8的序列包括限制酶BamHI的识别序列。编码TorA的信号序列的DNA序列如序列号3所示。
以国际公开小册子WO01/23591记载的质粒pPKSPTG1为模板,通过使用具有序列号9(5’-AAATTCCTGTGAATTAGCTGATTTAG-3’)、序列号10(5’-AAGAGATCGTTATTGTTCATAGAGGCGAAGGCTCCTTGAATAG-3’)所示序列的引物进行PCR,扩增编码启动子和信号肽的区域。序列号10的序列包括编码TorA信号肽的基因的5’末端的序列。其次,将该PCR产物、以及包括由具有序列号7和序列号8所示序列的引物扩增的包括编码TorA的基因序列和位于其上游的信号序列的区域的PCR产物按1∶1进行混合,以它们为模板,利用具有序列号8和序列号9所示序列的引物来进行交换(crossover)PCR。由此使包括含有PS2启动子区域的序列、TorA信号序列和编码TorA的序列的融合基因得到扩增。将该交换PCR产物用限制酶ScaI和BamHI消化后,利用琼脂糖凝胶电泳检测出约3.1kbp的DNA片段。从琼脂糖凝胶中切出该DNA片段,使用EasyTrapVer.2(宝酒造公司制)进行回收,将其***到日本特开平9-322774号公报记载的质粒pPK4的ScaI-BamHI部位,得到质粒pPKT-TorA。测定***到该质粒中的基因序列的碱基序列的结果,确认构建了预想的融合基因。以该质粒为模板,使用具有序列号9和序列号11(5’-GATTTCCTGGTTGCCGTTGGAATCCGCAGTCGCACGTCGCGGCG-3’)所示序列的引物,通过PCR来扩增包括PS2的启动子区域和编码TorA信号肽的区域的部分。应说明的是,序列号11所示的序列具有编码带有pro结构的蛋白质脱酰胺酶的区域的5’末端序列。其次,以克隆有蛋白质谷氨酰胺酶的质粒为模板,通过使用具有序列号6和序列号12(5’-GATTCCAACGGCAACCAGGA-3’)所示序列的引物进行PCR,扩增编码带有pro结构的蛋白质谷氨酰胺酶的区域。并将这些PCR产物按1∶1进行混合,以它们为模板,通过使用具有序列号6和序列号9所示序列的引物来进行交换PCR,扩增PS2启动子区域和TorA信号序列与编码带有pro结构的蛋白质脱酰胺酶的基因的融合基因。将该PCR产物用限制酶ScaI和BamHI消化后,进行琼脂糖凝胶电泳,检测出约3.1kbp的DNA片段。从琼脂糖凝胶中切出该DNA片段,使用EasyTrapVer.2(宝酒造公司制)进行回收,将其***到日本特开平9-322774号公报记载的质粒pPK4的ScaI-BamHI部位,得到质粒pPKT-PPG。测定质粒中的***序列的碱基序列,确认构建了预想的融合基因。应说明的是,带有pro结构的蛋白质谷氨酰胺酶的氨基酸序列如序列号2所示,TorA信号肽的氨基酸序列如序列号4所示。但是,直接按照天然型蛋白质谷氨酰胺酶的氨基酸序列利用市售蛋白酶进行成熟化时,预测不能正确切断pro序列。因此,为了将pro序列切断使其具有与天然型蛋白质谷氨酰胺酶的N末端序列相同的序列,将pro序列的C末端序列“QTNK”变更为“FGPK”。向“FGPK”变更时使用具有序列号13(5’-CTTGGGGCCGAAGCCCTTGACTTCTTTGGTCAG-3’)和序列号14(5’-TTCGGCCCCAAGTTGGCGTCCGTCATTCCAGAT-3’)所示序列的引物。序列号13的序列是用于扩增pro序列部分的引物,序列号14的序列是用于扩增成熟体部分的引物。以pPKT-PPG为模板,使用具有序列号12和序列号13所示序列的引物来扩增蛋白质谷氨酰胺酶的pro序列部分,使用具有序列号14和序列号6所示序列的引物来扩增蛋白质谷氨酰胺酶的成熟体部分。并且,将它们的PCR产物按1∶1进行混合,以它们为模板通过使用具有序列号6和序列号12所示序列的引物来进行交换PCR,扩增带有pro序列C末端变更为FGPK的pro结构的蛋白质谷氨酰胺酶基因。将该交换PCR产物克隆在pUC18的SmaI位点(pUCPPG(FGPK)),进行碱基序列的确认时发现pro序列已变更。其次,连接pPKT-PPG的AatII-BstPI片段(大)和pUCPPG(FGPK)的AatII-BstPI片段(小),构建pPKT-PPG(FGPK)。
使用构建的质粒pPKT-PPG(FGPK),对谷氨酸棒杆菌(C.glutamicum)ATCC13869进行转化,选择在含有25mg/l卡那霉素的CM2G琼脂培养基上生长的菌株。在30℃下将选择的菌株在含有25mg/l卡那霉素的MM液体培养基中培养48小时。用过滤器(0.45μm)过滤谷氨酸棒杆菌(C.glutamicum)培养液的离心上清液,使用超滤膜(排除分子量1万以下)浓缩该滤液。用50mM的磷酸缓冲液(pH7.5)进行缓冲液交换,通过胰蛋白酶切断蛋白质脱酰胺酶的pro结构部分,进行成熟化。之后,再次进行浓缩、缓冲液交换(20mM醋酸缓冲液,pH5.0),将该浓缩样品供给阳离子交换层析,回收蛋白质脱酰胺酶的活性组分,作为酶纯品。按照上述方法测定酶纯品中的蛋白质的活性时,活性为约100~140U/mg。
将100重量份猪腕(豚腕)肉馅、20重量份10%食盐水装入食物切碎机中混合15秒钟后,加入5重量份水(对照品)。将100重量份猪腕肉馅、20重量份10%食盐水装入食物切碎机中混合-细切15秒钟后,相对于1 g猪腕肉馅,将相当于0.1单位的上述蛋白质脱酰胺酶纯品(100U/mg)添加到5重量份水中混合后,将其加入到猪肉中(试验品1)。与试验品1同样,相对于1g猪腕肉而言,将馅添加了相当于0.2单位的蛋白质脱酰胺酶纯品的试验品作为试验品2、添加了相当于1单位的蛋白质脱酰胺酶纯品的试验品作为试验品3、添加了相当于10单位的蛋白质脱酰胺酶纯品的试验品作为试验品4。将各原料合并后,用刮铲搅拌,再次用食物切碎机混合15秒钟。重复该搅拌、混合的操作4次,之后填充到直径为3cm的骨胶原人造肠衣管中,在5℃下静置1小时。之后将其经在60℃的干燥环境下干燥40分钟、在75℃下蒸煮2小时的工序,冷却。应说明的是,酶添加品(试验品1~4:均为本发明品)在干燥工序中进行酶反应,在蒸煮工序中酶基本失活。测定对照品和试验品1~4的加热产率和物理性质,并通过感官检验来评价食感和味道。加热产率用加热后重量/加热前重量(%)表示。关于物理性质,将试验品切成高为3cm的圆柱,使用结构分析仪(STABLEMICROSYSTEMS制,TA.XT2i)测定在断面上以1mm/秒刺破5mm球时的断裂应力。感官评价中将切至3cm厚的样品让8名训练有素的评审员试吃,评价硬度、柔嫩度。评价结果如表1所示。
与对照品相比,试验品2~4柔软且顺滑度提高,综合评价也基本有所提高。试验品2~4呈强烈的布丁样食感,口感顺滑,断面有光泽,纹理趋于变得细腻,作为细切型香肠品质理想。相对于1g食材蛋白质脱酰胺酶的添加量为1单位以上时上述效果显著,但即使添加0.1单位也可以达到上述效果。并且,将对照品和试验品3密封,在90℃的水中煮10分钟后进行感官评价时,对照品食感***,而试验品3仍维持顺滑的食感。
表1.香肠的感官评价结果
实施例2
将FA级冷冻磨碎鱼肉解碎成薄片状,取1,000g磨碎鱼肉用斯蒂芬切碎机切细,搅拌(低速1.5分钟→中速1.5分钟→高速1.5分钟)。接着,加入30g食盐和600g冰水,用斯蒂芬切碎机切细,搅拌(低速1.0分钟→中速30秒→高速2分钟)。其次,添加50g马铃薯淀粉“ェスサン银领”(味之素(株)制)、50g砂糖、20g料酒、10g鲜味料“味之素”(味之素(株)制)和每1g原料磨碎鱼肉添加5单位按照实施例1记载的方法制备的蛋白质脱酰胺酶纯品(100U/mg),之后再次用斯蒂芬切碎机以中速进行搅拌直至样品温度达到8~10℃。将由此得到的肉糜填充到气密性的亚乙烯肠衣管中,在40℃下加热放置40分钟后,在85℃下加热30分钟,得到鱼糕香肠(试验品)。对照则不添加酶而以同样的方法在40℃下加热放置40分钟来试制鱼糕(对照品)。针对上述鱼糕,使用结构分析仪测定在断面上以1mm/秒刺破5mm球时的断裂应力和洼陷(断裂时的形变)。测定加热后的产率、观察保存两周后的脱水状态并进行感官评价。其结果如表2所示。
如表2所示,与对照品相比,试验品(本发明品)的断裂应力下降,洼陷增加。另外,本发明品其食感变得柔软且柔嫩。加热后测定去除脱水后的重量,结果本发明品重量变化少,相对于对照品而言加热产率提高。另一方面,味道、风味等与对照品相同。并且,观察在5℃下冷藏保存两周后的脱水状态,结果本发明品的蒸鱼糕几乎没有脱水,食感、味道、风味等也和保存前相同。
表2.鱼糕的感官评价结果
◎:非常令人满意;○:令人满意;△:一般
×:不令人满意
±:略有一些;+++:多
使用按照相同方法制备的鱼糕进行强制脱水评价。研究高压釜(121℃,30分钟)处理后产生的脱水和-30℃下冷冻、融化后产生的脱水这两个项目。脱水率以脱水重量(g)/处理前的重量(g)来计算。其结果如表3所示。本发明品的脱水率均得到抑制,特别是每1g原料添加0.2单位以上蛋白质脱酰胺酶时脱水率得到显著抑制。这样,添加蛋白质脱酰胺酶而制备的鱼糕即使进行容易产生脱水的处理,其脱水也被抑制。
表3.鱼糕的强制脱水评价
每1g磨碎鱼肉原料的酶添加量 | 高压釜处理后脱水(%) | 冷冻融化后脱水(%) |
未添加(对照品) | 11.0 | 7.2 |
0.1单位(本发明品) | 10.5 | 6.9 |
0.2单位(本发明品) | 9 | 6.3 |
1单位(本发明品) | 7.7 | 5.5 |
使用按照相同方法制备的鱼糕,测定由电炉加热(500W,20~60秒)引起的水分损失量,进行保水性评价。结果如表4所示。通过向每1g磨碎鱼肉原料中添加0.1单位以上的蛋白质脱酰胺酶,水分损失量得到抑制,抑制效果依赖于酶浓度而提高。对照品鱼糕表面干燥且硬、皱纹多,而本发明品柔嫩、维持着弹力状态。在食感方面,对照品发生硬化、柔嫩度受到破坏,而本发明品几乎未发现柔软度和柔嫩度的劣化。这表明本发明品由加热引起的水分蒸发和由此引起的食感劣化(***、柔嫩度受到破坏)得到抑制。由本结果可预期,利用本发明来提高实施了压热处理或炖等过度加工处理的含肉蛋白质食品的品质。
表4.鱼糕的保水性评价
电炉处理时间 | 每1g磨碎鱼肉原料的酶添加量 | |||
时间(秒) | 对照品 | 0.1单位(本发明品) | 0.2单位(本发明品) | 1单位(本发明品) |
20 | 7.6 | 7.3 | 6 | 5.6 |
40 | 29.1 | 26.7 | 22.3 | 22.2 |
60 | 49.9 | 46.3 | 40.7 | 40.1 |
水分蒸发率(%)=电炉处理后的重量/电炉处理前的重量×100
(单位:%)
实施例3
将100重量份猪里脊肉、20重量份10%食盐水、5重量份水合并,真空包装后在冷藏条件下使其在揉肉机中旋转一晚进行盐渍(对照品)。相对于1g猪里脊肉,将按照实施例1记载的方法制备的蛋白质脱酰胺酶纯品(100U/mg)按0.1单位、1单位、5单位相当量溶解在水中,按照与对照品相同的要领盐渍猪里脊肉(分别为试验品1~3:均为本发明品)。第二天,将盐渍的肉填充到气密性的圆筒亚乙烯肠衣(直径7cm)中,经在60℃的干燥环境下干燥60分钟,继续在60℃下烟熏30分钟,并在60℃下蒸煮2小时和在75℃下蒸煮30分钟的工序,冷却,得到火腿。测定对照品和试验品1~3除掉脱水后的重量,算出加热后重量/加热前重量(%)的值,求出加热产率。并且使用切至2mm厚的火腿,由8名评审员进行感官评价。感官评价中,首先通过手摸来评价火腿的切割面光滑度,接着试吃,对硬度、润湿感按5个等级进行评价。试制结果如表5所示。
本发明品的加热产率与对照品相比有所增加,酶添加量越多效果越好。本发明品火腿的切割面非常光滑,食感也柔软。并且本发明品在咀嚼时松散感明显减少,咽下时的吞咽次数少,因此评价为容易吞咽。
表5.火腿的感官评价结果
每1g原料的酶添加量 | 加热产率(%) | 切割面的光滑度 | 硬度 | 湿润感 |
-(对照品) | 84.3 | 3(基准) | 3(基准) | 3(基准) |
0.1单位(本发明品) | 84.9 | 3 | 3 | 3.5 |
1单位(本发明品) | 85.6 | 4 | 2 | 4 |
5单位(本发明品) | 86.0 | 5 | 2 | 5 |
研究以相同的记载方法试制的火腿中每1g肉添加1单位酶而制作的火腿的再加热脱水。即,测定将火腿真空包装后在沸水(100℃)中加热5分钟后产生的脱水量,求出脱水率(脱水率(%)=脱水量(g)/原来的重量(g))。结果如表6所示。与对照品相比,本发明品火腿的脱水率减少。该结果表明,将包装后的火腿表面再加热来进行杀菌时脱水受到抑制,品质可以得到提高。
表6.火腿的再加热脱水
每1g肉的酶添加量 | 加热时的脱水率(%) |
对照品 | 13.5 |
1单位(本发明品) | 11.2 |
实施例4
按表7所示的食谱制备两种浸渍液。即,仅含食盐的浸渍液(对照品)、含蛋白质脱酰胺酶的浸渍液(试验品)。用作原料的猪里脊肉块事先切断肌腱,测定各自的重量,每100g肉原料加入各25g浸渍液,真空包装。在4℃下静置12小时使浸渍液充分扩散到肉中,得到腌制肉。再用电热板(约160℃)将正反面各烤1.5分钟,得到烤肉。通过下式计算烤制时的加热产率。
加热产率(%)=(加热后的固体部分重量)/(加热前的总重量)
并且,由7名评审员进行感官评价,对“肉的柔软度”按5个等级进行评价。
加热产率和感官评价的结果如表8所示。与使用对照品浸渍液的猪肉相比,使用试验品浸渍液的猪肉(本发明品)其加热产率提高。另外,与使用对照品浸渍液的猪肉相比,使用试验品浸渍液的猪肉(本发明品)保持肉原本具有的纤维感,多汁且食感柔软,嚼起来有种沙沙感。除猪里脊肉之外,即使用牛腰肉、鸡胸肉来进行同样的试制,也可得到同样的效果。即,利用蛋白质脱酰胺酶可以软化肉食,由此确认该酶可以用作肉食软化剂。
表7.浸渍液配方
表8.烤肉的产率和感官评价结果
比较例1
如实施例4所示,本发明中使用的蛋白质脱酰胺酶与用于使肉柔软而经常使用的蛋白酶具有相同的效果。因此,将其与蛋白酶进行比较。向表7记载的浸渍液中溶解相对浸渍液为0.01%的蛋白酶制剂(木瓜蛋白酶,天野酶制)来代替蛋白质脱酰胺酶,按照与实施例7相同的方法制备猪里脊肉和鸡胸肉的盐渍肉。烤制猪里脊肉,鸡胸肉真空包装后在沸水中加热10分钟。对它们进行感官评价,发现蛋白酶使用品虽然在硬度方面均变得柔软,但肉特有的纤维感被破坏,品质与本发明品不同。特别是鸡肉,由于软化过度,一部分鸡肉溶化,肉完全没有咬头。这样,若使用蛋白酶作为肉食软化剂,当反应过度进行时会导致过度软化、肉质(味道、食感)下降,因此问题在于该反应非常难以控制。但是蛋白质脱酰胺酶使肉保持本来的适度纤维感,当用作肉食软化剂时反应非常容易控制,不易受流通、保存时间的影响,因此可以供应品质稳定的商品。这是由于蛋白质脱酰胺酶的软化机制不是分解肉食蛋白质,而是缓和肉食蛋白质的加热凝聚性。
产业应用性
根据本发明,可以提供抑制含肌肉蛋白质的食品因加工(加热、冷冻、冷藏等)、保存中发生的该蛋白质变性而引起的产率下降、脱水,保持柔嫩且柔软的食感,抑制味道、风味劣化的食品和这种食品的制造方法,因此本发明在食品领域中是非常有用的。
序列表
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Claims (5)
1.肉制品或水产糜制品的制造方法,其特征在于:向含有肌肉蛋白质的食材中添加蛋白质脱酰胺酶,使该酶与该肌肉蛋白质发生作用。
2.权利要求1的方法,其特征在于:肌肉蛋白质为来源于畜肉、鸟肉、鱼肉、软体动物或甲壳类的肌肉蛋白质。
3.权利要求1或2的方法,其特征在于:相对于1g食材蛋白质脱酰胺酶的添加量为0.01~100单位。
4.肉制品或水产糜制品,其特征在于:该产品是通过权利要求1至3中任一项的方法得到的。
5.肉食软化剂,其特征在于:该肉食软化剂含有蛋白质脱酰胺酶。
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JP2003250460A (ja) * | 2002-03-04 | 2003-09-09 | Amano Enzyme Inc | 乳蛋白質の機能性改質方法 |
JP2004089181A (ja) * | 2002-07-08 | 2004-03-25 | Ajinomoto Co Inc | 食品素材の改質方法 |
US20050048166A1 (en) * | 2003-07-01 | 2005-03-03 | Novozymes A/S | Compositions and methods for tenderizing meat |
-
2006
- 2006-01-11 CN CNA2006800015034A patent/CN101090644A/zh active Pending
- 2006-01-11 KR KR1020077013958A patent/KR20070104528A/ko not_active Application Discontinuation
- 2006-01-11 MY MYPI20060124A patent/MY148140A/en unknown
- 2006-01-11 DK DK06700828.4T patent/DK1836907T3/en active
- 2006-01-11 JP JP2006553030A patent/JP4763621B2/ja active Active
- 2006-01-11 ES ES06700828.4T patent/ES2547222T3/es active Active
- 2006-01-11 EP EP06700828.4A patent/EP1836907B1/en active Active
- 2006-01-11 WO PCT/JP2006/300573 patent/WO2006075771A1/ja active Application Filing
- 2006-01-12 TW TW095101237A patent/TW200637501A/zh unknown
-
2007
- 2007-07-13 US US11/777,554 patent/US20070254066A1/en not_active Abandoned
Cited By (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN101731668B (zh) * | 2009-12-30 | 2013-01-16 | 大连水产学院 | 扇贝柱肉糜制品的制备方法 |
CN115867144A (zh) * | 2020-06-08 | 2023-03-28 | 天野酶制品株式会社 | 蛋白质口感改良 |
Also Published As
Publication number | Publication date |
---|---|
MY148140A (en) | 2013-02-28 |
DK1836907T3 (en) | 2015-08-24 |
ES2547222T3 (es) | 2015-10-02 |
US20070254066A1 (en) | 2007-11-01 |
TW200637501A (en) | 2006-11-01 |
EP1836907B1 (en) | 2015-08-05 |
JP4763621B2 (ja) | 2011-08-31 |
WO2006075771A1 (ja) | 2006-07-20 |
EP1836907A1 (en) | 2007-09-26 |
KR20070104528A (ko) | 2007-10-26 |
EP1836907A4 (en) | 2012-08-01 |
JPWO2006075771A1 (ja) | 2008-06-12 |
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