Patents by Inventor Shun-ichi Tanaka
Shun-ichi Tanaka has filed for patents to protect the following inventions. This listing includes patent applications that are pending as well as patents that have already been granted by the United States Patent and Trademark Office (USPTO).
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Publication number: 20240018216Abstract: The current application describes various compositions and methods for the production of FN3-based binding proteins with improved stability properties. Aspects of the disclosure relate to polypeptides comprising a variant fibronectin type III (FN3) domain from Sulfolobus tokodaii or Pyrococcus horikoshii comprising one or more amino acid substitutions or insertions in a loop region of FN3, in a non-loop region of FN3, or in both.Type: ApplicationFiled: May 4, 2023Publication date: January 18, 2024Applicant: The University of ChicagoInventors: Shohei KOIDE, Shun-Ichi TANAKA, Akiko KOIDE
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Patent number: 11680091Abstract: The current application describes various compositions and methods for the production of FN3-based binding proteins with improved stability properties. Aspects of the disclosure relate to polypeptides comprising a variant fibronectin type III (FN3) domain from Sulfolobus tokodaii or Pyrococcus horikoshii comprising one or more amino acid substitutions or insertions in a loop region of FN3, in a non-loop region of FN3, or in both.Type: GrantFiled: February 21, 2019Date of Patent: June 20, 2023Assignee: The University of ChicagoInventors: Shohei Koide, Shun-Ichi Tanaka, Akiko Koide
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Patent number: 11459400Abstract: Aspects of the disclosure relate to compositions of enzyme-binding polypeptides (EBPs) that modify the substrate specificity of an enzyme and a method for identifying an EBP that modifies substrate specificity of an enzyme binding at least one substrate, the method comprising: contacting the enzyme with a polypeptide library comprising a plurality of EBPs that bind different epitopes of the enzyme; identifying EBPs that bind to the enzyme to form an EBP-enzyme complex; assaying for the activity level and substrate specificity of the EBP-enzyme complex; and identifying EBPs that modify the substrate specificity of the enzyme by identifying EBPs that, when in an EBP-enzyme complex, have a different substrate specificity than un-complexed EBP; wherein the catalytic rate constant of the EBP-enzyme complex is ?50% of the un-complexed enzyme for at least one substrate and/or wherein the EBP-enzyme complex retains binding to a substrate.Type: GrantFiled: July 15, 2016Date of Patent: October 4, 2022Assignee: The University of ChicagoInventors: Shohei Koide, Shun-Ichi Tanaka, Akiko Koide
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Publication number: 20210079063Abstract: The current application describes various compositions and methods for the production of FN3-based binding proteins with improved stability properties. Aspects of the disclosure relate to polypeptides comprising a variant fibronectin type III (FN3) domain from Sulfolobus tokodaii or Pyrococcus horikoshii comprising one or more amino acid substitutions or insertions in a loop region of FN3, in a non-loop region of FN3, or in both.Type: ApplicationFiled: February 21, 2019Publication date: March 18, 2021Inventors: Shohei KOIDE, Shun-Ichi TANAKA, Akiko KOIDE
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Patent number: 10870840Abstract: The present invention addresses a problem of providing a lipase derived from a microorganism that is specific for short-chain to medium-chain fatty acids. A modified lipase is obtained by making a substitution in the amino acid sequence of a Candida cylindracea derived lipase, wherein the substitution is (1) a substitution of asparagine for an amino acid corresponding to the amino acid at position 428 in the amino acid sequence set forth in SEQ ID NO: 1; or (2) a substitution of phenylalanine, methionine, or isoleucine for an amino acid corresponding to the amino acid at position 429 in the amino acid sequence set forth in SEQ ID NO: 1.Type: GrantFiled: July 26, 2019Date of Patent: December 22, 2020Assignee: AMANO ENZYME INC.Inventors: Yuki Ishigaki, Satoru Ishihara, Shun-ichi Tanaka
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Patent number: 10526423Abstract: The present invention addresses the problem of providing an eggshell membrane solubilization method that is capable of solving the problems associated with carrying out treatment using acids and alkalis, or problems associated with the processing methods of the conventional art that use proteases; in other words, an eggshell membrane solubilization method that is capable of solving at least one of the following problems: (1) the need for pretreatment such as pulverization, sonication or boiling; (2) the need for prolonged treatment; and (3) a low decomposition rate (approximately 20%). Eggshell membranes are efficiently solubilized by using a protease in combination with a reducing agent.Type: GrantFiled: August 12, 2011Date of Patent: January 7, 2020Assignee: AMANO ENZYME INC.Inventor: Shun-ichi Tanaka
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Publication number: 20190345465Abstract: The present invention addresses a problem of providing a lipase derived from a microorganism that is specific for short-chain to medium-chain fatty acids. A modified lipase is obtained by making a substitution in the amino acid sequence of a Candida cylindracea derived lipase, wherein the substitution is (1) a substitution of asparagine for an amino acid corresponding to the amino acid at position 428 in the amino acid sequence set forth in SEQ ID NO: 1; or (2) a substitution of phenylalanine, methionine, or isoleucine for an amino acid corresponding to the amino acid at position 429 in the amino acid sequence set forth in SEQ ID NO: 1.Type: ApplicationFiled: July 26, 2019Publication date: November 14, 2019Inventors: Yuki Ishigaki, Satoru Ishihara, Shun-ichi Tanaka
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Patent number: 10415023Abstract: The present invention addresses a problem of providing a lipase derived from a microorganism that is specific for short-chain to medium-chain fatty acids. A modified lipase is obtained by making a substitution in the amino acid sequence of a Candida cylindracea derived lipase, wherein the substitution is (1) a substitution of asparagine for an amino acid corresponding to the amino acid at position 428 in the amino acid sequence set forth in SEQ ID NO: 1; or (2) a substitution of phenylalanine, methionine, or isoleucine for an amino acid corresponding to the amino acid at position 429 in the amino acid sequence set forth in SEQ ID NO: 1.Type: GrantFiled: December 8, 2014Date of Patent: September 17, 2019Assignee: AMANO ENZYME INC.Inventors: Yuki Ishigaki, Satoru Ishihara, Shun-ichi Tanaka
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Publication number: 20180208678Abstract: Aspects of the disclosure relate to compositions of enzyme-binding polypeptides (EBPs) that modify the substrate specificity of an enzyme and a method for identifying an EBP that modifies substrate specificity of an enzyme binding at least one substrate, the method comprising: contacting the enzyme with a polypeptide library comprising a plurality of EBPs that bind different epitopes of the enzyme; identifying EBPs that bind to the enzyme to form an EBP-enzyme complex; assaying for the activity level and substrate specificity of the EBP-enzyme complex; and identifying EBPs that modify the substrate specificity of the enzyme by identifying EBPs that, when in an EBP-enzyme complex, have a different substrate specificity than un-complexed EBP; wherein the catalytic rate constant of the EBP-enzyme complex is ?50% of the un-complexed enzyme for at least one substrate and/or wherein the EBP-enzyme complex retains binding to a substrate.Type: ApplicationFiled: July 15, 2016Publication date: July 26, 2018Inventors: Shohei Koide, Shun-Ichi Tanaka, Akiko Koide
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Publication number: 20160319259Abstract: The present invention addresses a problem of providing a lipase derived from a microorganism that is specific for short-chain to medium-chain fatty acids. A modified lipase is obtained by making a substitution in the amino acid sequence of a Candida cylindracea derived lipase, wherein the substitution is (1) a substitution of asparagine for an amino acid corresponding to the amino acid at position 428 in the amino acid sequence set forth in SEQ ID NO: 1; or (2) a substitution of phenylalanine, methionine, or isoleucine for an amino acid corresponding to the amino acid at position 429 in the amino acid sequence set forth in SEQ ID NO: 1.Type: ApplicationFiled: December 8, 2014Publication date: November 3, 2016Inventors: Yuki Ishigaki, Satoru Ishihara, Shun-ichi Tanaka
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Publication number: 20130224830Abstract: The present invention addresses the problem of providing an eggshell membrane solubilization method that is capable of solving the problems associated with carrying out treatment using acids and alkalis, or problems associated with the processing methods of the conventional art that use proteases; in other words, an eggshell membrane solubilization method that is capable of solving at least one of the following problems: (1) the need for pretreatment such as pulverization, sonication or boiling; (2) the need for prolonged treatment; and (3) a low decomposition rate (approximately 20%). Eggshell membranes are efficiently solubilized by using a protease in combination with a reducing agent.Type: ApplicationFiled: August 12, 2011Publication date: August 29, 2013Applicant: AMANO ENZYME INC.Inventor: Shun-ichi Tanaka
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Patent number: 6358999Abstract: A new use of a zinc tranexamate compound in the treatment of diabetes is disclosed. Oral administration of the compound adequately slows down absorption of glucose from digestive tracts by inhibiting &agr;-glucosidase in vivo. The zinc tranexamate compound is also effective in the treatment of insulin-resistant type II diabetes.Type: GrantFiled: March 7, 2001Date of Patent: March 19, 2002Assignee: Hamari Chemicals, LTDInventors: Hajime Fujimura, Masakatsu Nozaki, Shun-ichi Tanaka, Reiko Natsuki
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Publication number: 20010031785Abstract: A new use of a zinc tranexamate compound in the treatment of diabetes is disclosed. Oral administration of the compound adequately slows down absorption of glucose from digestive tracts by inhibiting &agr;-glucosidase in vivo. The zinc tranexamate compound is also effective in the treatment of insulin-resistant type II diabetes.Type: ApplicationFiled: March 7, 2001Publication date: October 18, 2001Inventors: Hajime Fujimura, Masakatsu Nozaki, Shun-ichi Tanaka, Reiko Natsuki