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一株产低温碱性磷脂酶A_1耐冷细菌的筛选及发酵条件的初步研究 被引量:13

Screening of psychrotrophic bacteria producing cold-adapted alkaline phospholipase A_1 and preliminary studies on its fermentation conditions
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摘要 从新疆天山一号冰川冻土中筛选到一株产低温碱性磷脂酶A1的菌株xjF1,初步鉴定为居泉沙雷氏菌(Serratia fonticola)。该菌属于耐冷菌,具有产两种酶的特性。其产生磷脂酶A1的最适碳源为木糖,最适氮源为磷酸氢二铵。在接种量为2%,250mL三角瓶装液量为50mL,25℃,250r/min摇床振荡培养36h时,磷脂酶A1活力最高达17.5U/mL。该磷脂酶A1的最适作用温度和pH值是35℃和9.0,在12℃仍具有69%的酶活力,但在60℃保温10min即丧失86%的活力,对热敏感。 A strain, x-jF1 producing mid-adapted alkaline phospholipase A1 was isolated from the No. 1 glacier soil samples of Mountain Turn, Xinjiang. On the basis of the observation of modality and the 16S rDNA sequence analysis, xjF1 was identified as Serratia fonticola. The strain belonged to psychrotroph and had the capability of producing two enzymes. Xylose was carlton source and (NH4)2HPO4 was nitrogen source for higher production of phospholipase A1. The strain produced maximum phospholipase A1 activity, as high as 17.5U/mL, after growth at medium volume 50mL in a 250mL flask, inoculation volume 2% at 2512 for 36h on a shaker with speed of 250r/min. The optimum temperature and pH for the phospholipase A1 activity were 35℃ and 9.0, respectively. The enzyme still remained 69% of its maximum activity at 12℃. However, it lost 86% of activity after incubation at 60℃ for 10min. The phospholipase A1 showed high thermolability.
出处 《工业微生物》 CAS CSCD 北大核心 2008年第5期12-16,共5页 Industrial Microbiology
基金 新疆自然科学基金项目(编号:200421109) 新疆特殊环境微生物资源重点实验室项目(编号:XJYS0203-2004-06)
关键词 居泉沙雷氏菌 低温碱性磷脂酶A1 发酵条件 Serratia fonticola cold-adapted alkaline phospholipase A1 fermentation conditions
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参考文献14

  • 1李秋生,杨继国,杨博,林炜铁,余若黔.不同磷脂酶用于植物油脱胶的研究[J].中国油脂,2004,29(1):19-22. 被引量:38
  • 2杨博,王宏建.经济环保的酶法脱胶技术[J].中国油脂,2004,29(3):21-23. 被引量:21
  • 3杨继国,杨博,李秋生,林炜铁.新型磷脂酶Lecitase Ultra用于菜籽油脱胶的研究[J].中国油脂,2003,28(12):31-34. 被引量:23
  • 4杨继国,杨博,孟炯,李秋生,林炜铁.新型磷脂酶Lecitase Ultra用于大豆油脱胶的研究[J].中国油脂,2003,28(10):10-13. 被引量:40
  • 5Scandella CJ, Komberg A. A membrane-bound phospholipase A1 purified fied from Escherichia coli. Biochemistry , 1971, 10:4447-4456
  • 6Pete MJ, Ross AH, Exton JH. Purification and properties of phospholipase A1 from bovine brain. J Biol Chem, 1994, 269 : 19494- 19500.
  • 7G. H. dehaas, N. M. postema, W. nieuwenhuizen et al. Purification and properties of phospholipase A1 from rat and calf brain. Biochim. Biophys. Acta, 1968, 159:103
  • 8Hoang J. H. B, Hirschberg Jan-Willem. F. A, Simons Niek Dekker et al. Cloning, expression, purification and characterization of patatin, a novel phospholipase A. Eur. J. Biochem, 2001, 268:5037-5044
  • 9Kim, Myung Kee, Joon Shick Rhee. Purification and bichemical properties of extracelluar phospholipase A1 from serratia sp. MK1. Journal f Microbiology and Biotechnology, 1996, 6:407-413
  • 10Kim MK, Kim JK, Rhee JS. Isolation of a phospholipase A1 - producing microorganism, J Ind Microbiol Biotechnd, 1996 b, 16:171-174

二级参考文献10

  • 1Buchold H, Boensch R, Schroeppel J. Process for enzymatically degumming vegetable oil[P].US patent,5558781
  • 2Loeffler F, Plainer H, Sproessler B. Vegetable oil enzymatic degumming process by means of Aspergillus phospholipase[P]. US patent,6001640.
  • 3Clausen I G,Patkar S A,Borch K,et al. Method for reducing phosphorus content of edible oil[P]. US patent,6103505.
  • 4Hasida M, Tsutsumi N, Halkier T, et al. Acid phospholipase,production and method using thereof[P]. US patent,6127137.
  • 5Roy S K, Rao B V S K, Prasad R B N. Enzymatic degumming of rice bran oil[J]. J. Am. Oil Chem. Soc.,2002,79:845 -846.
  • 6S. K. Roy,B. V. S. K. Rao,R. B. N. Prasad. Enzymatic degumming of rice bran oil[J] 2002,Journal of the American Oil Chemists’ Society(8):845~846
  • 7韩世温.植物油的酶催化脱胶过程分析[J].中国油脂,1998,23(2):7-8. 被引量:16
  • 8裘爱泳,张绪媛,刘晔,王兴国.大豆油酶催化脱胶初探[J].中国油脂,1999,24(4):17-20. 被引量:15
  • 9杨博,杨继国,孟庆博,孟炯,林炜铁.Lecitase Novo用于大豆油脱胶的研究[J].中国油脂,2003,28(9):19-21. 被引量:16
  • 10杨继国,杨博,孟炯,李秋生,林炜铁.新型磷脂酶Lecitase Ultra用于大豆油脱胶的研究[J].中国油脂,2003,28(10):10-13. 被引量:40

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