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食品发酵用霉菌产内肽酶的研究进展 被引量:3

Research Progress on Fermentation Production Technology and Physicochemical Properties of Endopeptidases by Molds
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摘要 食品发酵中常用来生产内肽酶的霉菌包括藻状菌纲的根霉、毛霉;子囊菌纲的红曲霉;半知菌纲的曲霉和青霉等。霉菌内肽酶对乳制品和豆类发酵制品有很重要的实用价值,主要体现在凝乳、制备蛋白质水解产物及其良好风味的贡献等方面。本文综述了霉菌中毛霉、曲霉和根霉产内肽酶的性质、发酵条件等方面,重点比较不同来源霉菌生产的内肽酶特性、对底物作用的切割位点及各自发酵参数,为深入研究霉菌产酶特性,进一步开发有特色的蛋白酶酶制剂提供科学研究基础。 In food fermentation, some molds including Mucor and Rhizopus of Phycomycetes, Monascus of Ascomycetes, and Aspergillus and Penicillium of Deuteromycetes were usually used to produce endopeptidases, which is of important practical value in milk coagulation, hydrolyte preparation from protein and contribution to nice flavor in the production of dairy products and soybean fermentation products. This paper reviewed the properties and the fermentation conditions for endopeptidase production by Mucor, Aspergillus and Rhizopus, respectively, emphatically compared the endopeptidase characteristics, cleavage sites for substrate reaction and fermentation parameters, hoping to provide some scientific bases for deep study on the properties of endopeptidase production by the above three molds and further development of distinctive protease preparation.
出处 《食品科学》 EI CAS CSCD 北大核心 2009年第9期219-224,共6页 Food Science
基金 国家自然科学基金项目(30770056)
关键词 霉菌 毛霉 曲霉 根霉 发酵 内肽酶 mold Mucor Aspergillus Rhizopus fermentation endopeptidase
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  • 1李理,罗泽民,卢向阳.毛霉蛋白酶的制备及其酶解产物的分析[J].食品与机械,1999,15(3):18-19. 被引量:9
  • 2邓靖,林亲录,赵谋明,周俊清.米曲霉M_3产蛋白酶特性研究[J].中国调味品,2005,30(1):16-20. 被引量:8
  • 3KOAZE Y, GOI H, EZEAWAK, et al. Fungal proeolytic enzymes. Part 1. Isolation of two kinds of acid-protease excreted by Aspergillul niger vat. macrosporus[J]. Agricultural and Biological Chemistry, 1964, 28: 216-223.
  • 4STERNBRG M Z, MARSCHALL D. Crystalline milk clotting protease from Mucor miehei and some of its properties[J]. Journal of Dairy Science, 1971, 54(2): 159-167.
  • 5MACHALINSKI C, PIRPIGNANI M L, MARINO C, et al. Structural aspects of the Mucor bacilliformis proteinase, a new member of the aspartyl proteinase family[J]. Journal of Biotechnology, 2006, 123(4): 443-452.
  • 6ARIMA K, YU J, LWASAKI S. Milk-clotting enzyme from Mucor pusillus var. lindt[J]. Methods in Enzymology, 1970, 19: 446-459.
  • 7FUMAMOTO J, TSURU D, YAMAMOTO T. A rennin-like enzyme from Rhizopus chinesis[J]. Agricultural and Biological Chemistry, 1967, 31: 710-717.
  • 8HORIUCHI H, YANAI K, OKAZAKI T. Isolation and sequencing of a genomic clone encoding aspartic proteinase of Rhizopus niveus[J]. Journal of Bacteriology, 1988, 170(1): 272-278.
  • 9HOFMANN T, SHAW R. Proteolytic enzymes of Penicillium janthinellum: I Purification and properties of a trypsinogen-activation enzyme (peptidase A) [J]. Bioehim Biophys Acta, 1964, 92: 543-557.
  • 10MORIHARA K, OKA T. Comparative specificity of microbial acid proteinases for synthetic peptides. Ⅲ. Relationship with their trypsinogen activating ability[J]. Arch Biochem Biophys, 1973, 157: 561-572.

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