The selection of alkaline protease-producing yeasts from marine environments and evaluation of their bioactive peptide production

Jing Li; Zhenming Chi; Xianghong Wang; Ying Peng; Zhe Chi

doi:10.1007/s00343-009-9198-8

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The selection of alkaline protease-producing yeasts from marine environments and evaluation of their bioactive peptide production

Updated：2023-05-16

- The selection of alkaline protease-producing yeasts from marine environments and evaluation of their bioactive peptide production
- Journal of Oceanology and Limnology Vol. 27, Issue 4, Pages: 753-761(2009)
- Affiliations：
  
  UNESCO Chinese Center of Marine Biotechnology Ocean University of China
- Author bio：
- Funds：
- DOI：10.1007/s00343-009-9198-8
  CLC：
- Online First：04 December 2009，
  
  Published：2009
- Accepted：
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Li, J., Chi, Z., Wang, X. et al. The selection of alkaline protease-producing yeasts from marine environments and evaluation of their bioactive peptide production., Chin. J. Ocean. Limnol. 27, 753–761 (2009). https://doi.org/10.1007/s00343-009-9198-8
DOI：

Li, J., Chi, Z., Wang, X. et al. The selection of alkaline protease-producing yeasts from marine environments and evaluation of their bioactive peptide production., Chin. J. Ocean. Limnol. 27, 753–761 (2009). https://doi.org/10.1007/s00343-009-9198-8 DOI：

摘要

Abstract

A total of 400 yeast strains from seawater

sediments

saltern mud

marine fish guts

and marine algae were obtained. The protease activity of the yeast cultures was estimated

after which four strains (HN3.11

N11b

YF04C and HN4.9) capable of secreting extracellular alkaline protease were isolated. The isolated strains were identified as Aureobasidium pullulans

Yarrowia lipolytica

Issatchenkia orientalis and Cryptococcus cf. aureus. The optimal pH of the protease activity produced by strains HN3.11

YF04C

and HN4.9 was 9.0

while that of the protease produced by strain N11b was 10.0. The optimal temperature for protease activity was 45°C for strains HN3.11

N11b

and YF04C

and 50°C for strain HN4.9. After digestion of shrimp (Penaeus vannamei) protein and spirulina (Arthospira platensis) protein with the four crude alkaline proteases

the filtrate from spirulina (Arthrospira platensis) powder digested by the crude alkaline protease of strain HN3.11 was found to have the highest antioxidant activity (61.4%) and the highest angiotensin I converting enzyme (ACE)-inhibitory activities (68.4%). The other filtrates had much lower antioxidant activity and ACE-inhibitory activities.

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references

Anwar A, Saleemuddin M. 1998. Alkaline protease: a review. Bioresource Technol., 64(3): 175–183.

Barth G, Garlardin C. 1996. Yarrowia lipolytica. In: Wolf K ed. Nonconventional yeasts in biotechnology. Springer-Verlag. Press, Berlin, Germany. p. 313–388.

Bradford M M. 1976. A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72(1–2): 248–254.

Chi Z M, Liu Z Q. 2006. Marine yeasts and their applications in mariculture. J. Ocean University of China, 5(3): 243–247.

Chi Z M, Ma C L, Wang P, Li H F. 2007. Optimization of medium and cultivation conditions for alkaline protease production by the marine yeast Aureobasidium pullulans. Bioresource Technol., 98(3): 534–538.

Costas M, Deive F J, Longo M A, 2004. Lipolytic activity in submerged cultures of Issatchenkia orientalis. Process Biochem., 39(12): 2 109–2 114.

Donaghy J A, McKay A M. 1993. Production and properties of alkaline protease by Aureobasidium pullulans. J. Appl. Microbiol., 74(6): 662–666.

Felsenstein J. 1995. PHYLIP (Phylogenetic Inference Package), Version 3.75. Distributed by author, Department of Genetics, University of Washington, Seattle, WA.

Jain M R, Zinjarde S S, Deobagkar D D, Deobagkar D N. 2004. 2,4,6-Trinitrotoluene transformation by a tropical marine yeast, Yarrowia lipolytica NCIM 3589. Mar. Pollut. Bull., 49(9–10): 783–788.

Kimura M. 1980. A simple method for estimating evolutionary rate of base substitutions through comparative studies on nucleotide sequences. J. Mol. Evo., 16(2): 87–90.

Kumar C G, Takagi H. 1999. Microbial alkaline proteases: From a bioindustrial viewpoint. Biotechnol. Adv., 17(7): 561–594.

Kurtzman C P, Fell J W. 2000. The yeasts. A taxonomic Study. Elsevier Press, Amsterdam, Lausanne, New York, Oxford, Shannon, Singapore, Tokyo. 1 055p.

Li G H, Liu H, Shi Y H, Le G W. 2005. Direct spectrophotometric measurement of angiotensin I-converting enzyme inhibitory activity for screening bioactive peptides. J. Pharmaceut. Biomed., 37(2): 219–224.

Lowry O H, Rosebrough N J, Farr A L, Randall R J. 1951. Protein measurement with Folin phenol reagent. J. Biol. Chem., 193(1): 265–275.

Ma C L, Ni X M, Chi Z M, Ma L Y, Gao L M. 2007. Purification and characterization of an alkaline protease from the marine yeast Aureobasidium pullulans for bioactive peptide production from different sources. Mar. Biotechnol., 9(3): 343–351.

Ogrydziak D M, Scharf S. 1982. Alkaline extracellular protease produced by Saccharomycopsis lipolytica CX161-1B. J. Gen. Microbiol., 128(6): 1 225–1 234.

Ogrydziak D M. 1993. Yeast extracellular proteases. Crit. Rev. Biotechnol., 13(1): 1–55.

Prillinger H, Molnár O, Eliskases-Lechner F, Lopandic K. 1999. Phenotypic and genotypic identification of yeasts from cheese. Anton. Leeuw., 75(4): 267–283.

Re R, Pellergini N, Proteggente A, Pannala A, Yang M, Rice-Evans C. 1999. Antioxidant activity applying an improved ABTS radical cation decolorization assay. Free Radical Bio. Med., 26(9–10): 1 231–1 237.

Sambrook J, Fritsch E F, Maniatis T. 1989. Molecular cloning: a laboratory manual. Cold Spring Harbor Laboratory Press. Jin D Y, Li M F. Beijing, Science Press, 1992: 367–370. (in Chinese)

Sheng J, Chi Z M, Li J, Gao L M, Gong F. 2007. Inulinase production by the marine yeast Cryptococcus aureus G7a and inulin hydrolysis by the crude inulinase. Process Biochem., 42(5): 805–811.

Silva S V, Malcata F X. 2005. Caseins as source of bioactive peptides. Intern. Dairy J., 15: 1–15.

Sugita T, Takashima M, Kodama M, Tsuboi R, Nishikawa A. 2003. Description of a new yeast species, Malassezia japonica, and its detection in patients with atopic dermatitis and healthy subjects. J. Clin. Microbiol., 41(10): 4 695–4 699.

Takashima M, Sugita T, Shinoda T, Nakase T. 2003. Three new combinations from the Cryptococcus laurentii complex: Cryptococcus aureus, Cryptococcus carnescens and Cryptococcus peneaus. Int. J. Syst. Evol. Mic., 53(4): 1 187–1 194.

Tobe S, Takami T, Ikeda S, Horikoshi K. 1976. Production of some enzymatic properties of alkaline protease of Candida lipolytica. Agric. Biol. Chem., 40(3): 1 087–1 092.

Yarrow D. 1998. Methods for the isolation, maintenance and identification of yeasts. In: Kurtzman C P and Fell J W ed. The Yeasts, A Taxonomic Study. Elsevier Press, Amsterdam. p. 77–100.

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