Secretion of collagenases by Saccharomyces cerevisiae for collagen degradation
Tóm tắt
The production and processing of animal-based products generates many collagen-rich by-products, which have received attention both for exploitation to increase their added value and to reduce their negative environmental impact. The collagen-rich by-products can be hydrolyzed by collagenases for further utilization. Therefore, collagenases are of benefit for efficient collagen materials processing. An alternative and safe way to produce secreted collagenases is needed.
Two collagenases from
Sufficient calcium and zinc ions are essential for active collagenase production by yeast. Collagenase secretion was increased by optimization of expression cassettes. Collagenase expression imposed metabolic burden and cofactor perturbations on yeast cells, which could be improved through metabolic engineering. Our work provides a useful way to produce collagenases for collagen resource utilization.
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Tài liệu tham khảo
Henchion M, Hayes M, Mullen AM, Fenelon M, Tiwari B. Future protein supply and demand: strategies and factors influencing a sustainable equilibrium. Foods. 2017;6(7):53.
Nazer DW, Al-Sa’ed RM, Siebel MA. Reducing the environmental impact of the unhairing–liming process in the leather tanning industry. J Clean Prod. 2006;14(1):65–74.
Lemes AC, Egea MB, de Oliveira Filho JG, Gautério GV, Ribeiro BD, Coelho MAZ. Biological approaches for extraction of bioactive compounds from agro-industrial by-products: a review. Front Bioeng Biotechnol. 2022;9:802543–802543.
Song Y, Fu Y, Huang S, Liao L, Wu Q, Wang Y, Ge F, Fang B. Identification and antioxidant activity of bovine bone collagen-derived novel peptides prepared by recombinant collagenase from Bacillus cereus. Food Chem. 2021;349: 129143.
Mirzapour-Kouhdasht A, Moosavi-Nasab M, Yousefi R, Eun J-B. Bio/multi-functional peptides derived from fish gelatin hydrolysates: technological and functional properties. Biocatal Agric Biotechnol. 2021;36: 102152.
Mei F, Liu J, Wu J, Duan Z, Chen M, Meng K, Chen S, Shen X, Xia G, Zhao M. Collagen peptides isolated from salmo salar and tilapia nilotica skin accelerate wound healing by altering cutaneous microbiome colonization via upregulated NOD2 and BD14. J Agric Food Chem. 2020;68(6):1621–33.
Yang X, Xiao X, Liu D, Wu R, Wu C, Zhang J, Huang J, Liao B, He H. Optimization of collagenase production by Pseudoalteromonas sp. SJN2 and application of collagenases in the preparation of antioxidative hydrolysates. Mar Drugs. 2017;15(12):377.
Harrington DJJI. Bacterial collagenases and collagen-degrading enzymes and their potential role in human disease. Infect Immun. 1996;64(6):1885–91.
Duarte AS, Correia A, Esteves AC. Bacterial collagenases—a review. Crit Rev Microbiol. 2016;42(1):106–26.
Warwick D, Arandes-Renu JM, Pajardi G, Witthaut J, Hurst LC. Collagenase Clostridium histolyticum: emerging practice patterns and treatment advances. J Plast Surg Hand Surg. 2016;50(5):251–61.
Azmi W, Chauhan S, Gautam M. An overview on therapeutic potential and various applications of microbial collagenases. J Microbiol Biotechnol Res. 2017;7:17–29.
Gabrielson AT, Spitz JT, Hellstrom WJG. Collagenase Clostridium Histolyticum in the treatment of urologic disease: current and future impact. Sexual Medicine Reviews. 2018;6(1):143–56.
Bond MD, Van Wart HE. Characterization of the individual collagenases from Clostridium histolyticum. Biochemistry. 1984;23(13):3085–91.
Bond MD, Van Wart HE. Purification and separation of individual collagenases of Clostridium histolyticum using red dye ligand chromatography. Biochemistry. 1984;23(13):3077–85.
Bond MD, Van Wart HE. Relationship between the individual collagenases of Clostridium histolyticum: evidence for evolution by gene duplication. Biochemistry. 1984;23(13):3092–9.
Yoshihara K, Matsushita O, Minami J, Okabe A. Cloning and nucleotide sequence analysis of the colH gene from Clostridium histolyticum encoding a collagenase and a gelatinase. J Bacteriol. 1994;176(21):6489–96.
Matsushita O, Jung C-M, Katayama S, Minami J, Takahashi Y, Okabe A. Gene duplication and multiplicity of collagenases in Clostridium histolyticum. J Bacteriol. 1999;181(3):923–33.
Matsushita O, Jung C-M, Minami J, Katayama S, Nishi N, Okabe A. A study of the collagen-binding domain of a 116-kDa Clostridium histolyticum collagenase. J Biol Chem. 1998;273(6):3643–8.
Matsushita O, Koide T, Kobayashi R, Nagata K, Okabe A. Substrate recognition by the collagen-binding domain of Clostridium histolyticum Class I collagenase. J Biol Chem. 2001;276(12):8761–70.
Johnson P, White S, London N. Collagenase and human islet isolation. Cell Transplant. 1996;5(4):437–52.
Ducka P, Eckhard U, Schonauer E, Kofler S, Gottschalk G, Brandstetter H, Nuss D. A universal strategy for high-yield production of soluble and functional clostridial collagenases in E. coli. Appl Microbiol Biotechnol. 2009;83(6):1055–65.
Bertuzzi F, Cuttitta A, Ghersi G, Mazzola S, Salamone M, Seidita G: Clostridium histolyticum recombinant collagenases and method for the manufacture thereof. In.: Google Patents; 2014.
Wang G, Huang M, Nielsen J. Exploring the potential of Saccharomyces cerevisiae for biopharmaceutical protein production. Curr Opin Biotechnol. 2017;48:77–84.
Huang M, Bai Y, Sjostrom SL, Hallstrom BM, Liu Z, Petranovic D, Uhlen M, Joensson HN, Andersson-Svahn H, Nielsen J. Microfluidic screening and whole-genome sequencing identifies mutations associated with improved protein secretion by yeast. Proc Natl Acad Sci USA. 2015;112(34):E4689–96.
Eckhard U, Schonauer E, Nuss D, Brandstetter H. Structure of collagenase G reveals a chew-and-digest mechanism of bacterial collagenolysis. Nat Struct Mol Biol. 2011;18(10):1109–14.
Ohbayashi N, Yamagata N, Goto M, Watanabe K, Yamagata Y, Murayama K. Enhancement of the structural stability of full-length clostridial collagenase by calcium ions. Appl Environ Microbiol. 2012;78(16):5839.
Eckhard U, Schonauer E, Brandstetter H. Structural basis for activity regulation and substrate preference of clostridial collagenases G, H, and T. J Biol Chem. 2013;288(28):20184–94.
Caviness P, Bauer R, Tanaka K, Janowska K, Roeser JR, Harter D, Sanders J, Ruth C, Matsushita O, Sakon J. Ca2+-induced orientation of tandem collagen binding domains from clostridial collagenase ColG permits two opposing functions of collagen fibril formation and retardation. FEBS J. 2018;285(17):3254–69.
Zhang Y, Liu H, Tang K, Liu J, Li X. Effect of different ions in assisting protease to open the collagen fiber bundles in leather making. J Clean Prod. 2021;293: 126017.
Eckhard U, Schönauer E, Ducka P, Briza P, Nüss D, Brandstetter H. Biochemical characterization of the catalytic domains of three different clostridial collagenases. Biol Chem. 2009;390(1):11–8.
Tanaka S, Takeuchi Y, Matsumura H, Koga Y, Takano K, Kanaya S. Crystal structure of Tk-subtilisin folded without propeptide: Requirement of propeptide for acceleration of folding. FEBS Lett. 2008;582(28):3875–8.
Boon L, Ugarte-Berzal E, Vandooren J, Opdenakker G. Protease propeptide structures, mechanisms of activation, and functions. Crit Rev Biochem Mol Biol. 2020;55(2):111–65.
Overkamp KM, Bakker BM, Kötter P, Luttik MAH, Van Dijken JP, Pronk JT. Metabolic engineering of glycerol production in Saccharomyces cerevisiae. Appl Environ Microbiol. 2002;68(6):2814–21.
Da Silva NA, Srikrishnan S. Introduction and expression of genes for metabolic engineering applications in Saccharomyces cerevisiae. FEMS Yeast Res. 2012;12(2):197–214.
Blazeck J, Alper HS. Promoter engineering: Recent advances in controlling transcription at the most fundamental level. Biotechnol J. 2013;8(1):46–58.
Bakker BM, Overkamp KM, van Maris AJA, Kötter P, Luttik MAH, van Dijken JP, Pronk JT. Stoichiometry and compartmentation of NADH metabolism in Saccharomyces cerevisiae. FEMS Microbiol Rev. 2001;25(1):15–37.
Görgens JF, van Zyl WH, Knoetze JH, Hahn-Hägerdal B. Amino acid supplementation improves heterologous protein production by Saccharomyces cerevisiae in defined medium. Appl Microbiol Biotechnol. 2005;67(5):684–91.
van Rensburg E, den Haan R, Smith J, van Zyl WH, Görgens JF. The metabolic burden of cellulase expression by recombinant Saccharomyces cerevisiae Y294 in aerobic batch culture. Appl Microbiol Biotechnol. 2012;96(1):197–209.
Tyo KEJ, Liu Z, Petranovic D, Nielsen J. Imbalance of heterologous protein folding and disulfide bond formation rates yields runaway oxidative stress. BMC Biol. 2012;10(1):16.
French MF, Mookhtiar KA, Van Wart HE. Limited proteolysis of type I collagen at hyperreactive sites by class I and II Clostridium histolyticum collagenases: complementary digestion patterns. Biochemistry. 1987;26(3):681–7.
French MF, Bhown A, Van Wart HE. Identification of Clostridium histolyticum collagenase hyperreactive sites in type I, II, and III collagens: lack of correlation with local triple helical stability. J Protein Chem. 1992;11(1):83–97.
Breite AG, McCarthy RC, Dwulet FE. Characterization and functional assessment of Clostridium histolyticum Class I (C1) collagenases and the synergistic degradation of native collagen in enzyme mixtures containing Class II (C2) collagenase. Transplant Proc. 2011;43(9):3171–5.
Bauer R, Janowska K, Taylor K, Jordan B, Gann S, Janowski T, Latimer EC, Matsushita O, Sakon J. Structures of three polycystic kidney disease-like domains from Clostridium histolyticum collagenases ColG and ColH. Acta Crystallogr D Biol Crystallogr. 2015;71:565–77.
Green Michael R, Sambrook J. Molecular Cloning: a laboratory manual. New York: Cold Spring Harbor Laboratory Press; 2012.
Gietz RD, Schiestl RH. Frozen competent yeast cells that can be transformed with high efficiency using the LiAc/SS carrier DNA/PEG method. Nat Protoc. 2007;2:1–4.
Zhang Y, Fu Y, Zhou S, Kang L, Li C. A straightforward ninhydrin-based method for collagenase activity and inhibitor screening of collagenase using spectrophotometry. Anal Biochem. 2013;437(1):46–8.