Milk clotting activity of protease, extracted from rhizome of Taffin giwa ginger ( Zingiber officinale ) cultivar, from northwestern Nigeria

Ya'u Murtala, A. Babandi, K. Babagana, M. Rajah, H. Yakasai, A. Ibrahim, D. Shehu, A. Alhassan
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引用次数: 3

Abstract

The increasing prices of calf rennets, their accessibility and ethical concerns associated with the production of such enzymes for general cheese making have led to systematic investigations on the possibility and suitability of their substitution by other enzymes of plant origin. In this study, ammonium sulphate ((NH 4 ) 2 SO 4 ) fractionation, characterization and milk clotting activity (MCA) of protease extracted from Taffin Giwa ginger rhizome cultivar of the family Zingiberaceae from northwestern Nigeria were carried out. The protease extracted showed optimum activity at temperatures near 60 °C and pH value of 6.5 with a relative activity in a broad pH range of 5.0 to 8.0 accordingly. The enzyme was completely denatured at higher temperature of 100 °C and higher pH range of 12.0. The milk clotting property of the protease indicated 3.1 and 2.2 folds of MCA and MSCA respectively in relation to the commercial calf rennet with MCA/PA ratio of 2.52. The properties of Taffin Giwa protease shown in this study, especially its milk clotting activity, make it a potential candidate for substituting calf rennet in the food industries, particularly in cheese making processes. Keywords: Ginger Protease, Milk Clotting Activity, Calf rennet, Characterization, Extraction
产自尼日利亚西北部的Taffin giwa生姜(Zingiber officinale)品种根茎中提取的蛋白酶凝乳活性
小牛凝乳酶的价格不断上涨,它们的可获得性以及与生产此类酶用于一般奶酪制作相关的伦理问题,导致了对其他植物源酶替代它们的可能性和适用性的系统调查。本研究采用硫酸铵(nh4) 2so4)对产自尼日利亚西北部姜科Taffin Giwa姜根的蛋白酶进行分离、鉴定和凝乳活性测定。所提取的蛋白酶在温度接近60℃,pH值为6.5时活性最佳,相对pH值为5.0 ~ 8.0时活性最佳。酶在100℃的高温和12.0的pH范围下完全变性。该蛋白酶的凝乳性能是商品犊牛凝乳酶的3.1倍和2.2倍,MCA/PA比值为2.52。本研究显示的塔芬吉瓦蛋白酶的特性,特别是其凝乳活性,使其成为食品工业中替代小牛凝乳酶的潜在候选物,特别是在奶酪制作过程中。关键词:生姜蛋白酶,凝乳活性,小牛凝乳酶,表征,提取
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